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Fluorescence emission from ANS 8-anilinonaphthalenesulfonic acida common probe for hydrophobic patches or partially unfolded protein, was unchanged in the presence of rlatherin not shown. We have recently used infrared reflectance to demonstrate the presence of both intact alpha-helix and beta-structures for a different surfactant protein that also appears to be a folded globular protein in bulk solution [34].



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The Arabian Horse and the Show World. Experiments were carried out at room temperature and the platinum ring cleaned between readings by rinsing with UHQ water and flaming to remove residual deposits. 6 inch android phones questions An example of this could be the strong surface activity of the proteinaceous foams in which certain tropical frogs lay their eggs, which may also have anti-microbial propensities, but are nonetheless compatible with naked eggs and spermatozoa [42][43]. As shown in Figure 4Alatherin transcripts were only detectable in skin and submaxillary salivary gland, and the protein was only detectable from skin, salivary gland, tongue and cheek Figure 4B. There are different theories about where the ancestors of the Arabian originally lived.



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It's the aspirin of our era. The Prussians set up a royal stud inoriginally intended to provide horses for the royal stables, and other studs were established to breed animals for other uses, including mounts for the Prussian army. Archived from the original on September 15,









Archived from the original on June 12, Biophysical Journal in press. The choice of the number of sublayers in the model depended upon the extent of inhomogeneity across the interface, but a single-layer model was sufficient to fit the data adequately here. A number of sports teams and Olympic athletes have used DMSO, although some have since moved on to other treatment modalities. British Percheron Horse Society website. The origins of the registry date towhen the Hamidie Society sponsored an exhibit of Arabian horses from what today is Syria at the World Fair in Chicago. Not all European studs recovered.







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05.03.2018 - Today, Arabian bloodlines are found in almost every modern breed of riding horse. D Immunoperoxidase labelling of a section of normal equine skin showing a dense dark band brown of staining proximal to the apical membrane of the sweat gland secretory epithelial cells; cell surface associated latherin is likely to have been lost during the preparation process. Archived from the original on November 14, Archived from the original on June 17, As a result, many European monarchs began to support large breeding establishments that crossed Arabians on local stock, one example being Knyszynathe royal stud of Polish king Zygmunt II Augustand another the Imperial Russian Stud of Peter the Great. In relation to cancer, several properties of DMSO have gained attention. Staining is also apparent in intracellular vesicles.









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11.02.2018 - The Light Horse Breeds: Arabian Horse Society of Australia. Researchers concluded that DMSO brought significant relief to the majority of patients. Fatigue and difficulty in breathing may ensue.











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We further show that latherin is also produced in horse salivary glands, which is consistent with their specialisation as animals needing to masticate and process large quantities of dry food material.



Latherin, therefore, provides insight into an unusual specialisation of a large mammal and also how proteins on their own can act as surfactants in their native folded state. Recombinant latherin rlatherin was produced without its hydrophobic secretory signal peptide and purified in high yield by over-expression in E.



Latherin from horse E. The sequences of all the tryptic peptides obtained from sweat-derived latherin appear in the sequence encoded by the cDNA, as do those of horse allergens originally designated Equ c 4 and Equ c 5 [16] Figure 1B.



The allergen peptides therefore derive from latherin, although they may occur as separate entities through some degree of specific cleavage or degradation of the protein in horse dander.



Similar procedures were used to obtain partial cDNAs encoding latherin of three other members of the Equidae, namely the Damara or Chapman Zebra Equus burchellii antiquorum, Persian Onager Equus hemionus onager, and an Ass Equus asinus asinus.



The amino acid sequences were very similar, with only a few amino acid differences Figure 1A. Most of the substitutions between the proteins are infrequently exchanged according to established evolutionary substitution matrices [52] , [53] , except for an exchange of aspartic acid D and asparagine N, as indicated by the symbol.



B Alignment of the amino acid sequence of Equus caballus latherin predicted from cDNA, beginning at the first amino acid position for which there was a matching peptide, with the new peptide sequences LathPep1 to LathPep8 and the peptide fragments previously ascribed to separate allergens Equ c 4 and Equ c 5 [16].



C Amino acid composition of the mature form of latherin obtained from its cDNA sequence, showing that the protein is unusually enriched in leucines. The percent composition of each amino acid in latherin is plotted against the cumulative composition of all proteins entered into Swiss-Prot http: An analysis of the amino acid composition of the putative processed, mature, protein shows that latherin is slightly deficient in lysine and alanine, but remarkably enriched in leucine Both LBP and BPI bind bacterial lipopolysaccharide, and are therefore considered part of the innate immune system [18] — [20].



PLUNC proteins are currently of unknown function, but it is argued that they too are associated with innate immunity, specialized for action at mucosal surfaces [21] — [23] , although formal demonstration of such activity is awaited.



The proteins most closely related to latherin are the breast cancer and salivary gland-expressed BASE proteins encoded by a defective gene in humans; [24]. Further confirmation of latherin's membership of the larger PLUNC family comes from the conserved position of its cysteines in amino acid sequence alignments with all members of that family.



Moreover, an analysis of horse genomic DNA by PCR, using oligonucleotide primers flanking introns predicted from the positions of those in PLUNC genes, revealed that all the intron positions known in the latter are preserved in the latherin gene not shown [25] , [26].



Secondary structure prediction programs e. This is typical behaviour for the irreversible thermal unfolding of an extra-cellular protein in aqueous solution. Fluorescence emission from ANS 8-anilinonaphthalenesulfonic acid, a common probe for hydrophobic patches or partially unfolded protein, was unchanged in the presence of rlatherin not shown.



All these properties are characteristic of a stable, folded, soluble globular protein, and this is confirmed by our preliminary high-resolution protein NMR data not shown demonstrating that rlatherin is well folded in solution.



B Differential scanning calorimetry demonstrating the thermal stability of recombinant latherin in solution. See also Table 1 for quenching analysis. The molecular environment of latherin's single conserved tryptophan residue Trp was examined by fluorescence emission and quenching experiments.



Intrinsic fluorescence Figure 2C shows a peak emission of the recombinant protein at nm when excited at nm. This is somewhat more red-shifted than normally observed for globular proteins [28] , [29] , and shows a decrease in intensity but no wavelength shift under denaturing conditions 6 M Gdn HCl, similar to that of an indole group fully exposed to solvent water..



It is therefore likely that Trp is exposed to solvent water. In the case of latherin, an exposed Trp side chain might be involved in protein surface hydrophobicity related to surfactant activity.



Apolar surface patches in hydrophobins are considered to be key to their surface activity and also their self-assembly into higher order complexes that enhance surface activity [10] , [11] , though in rlatherin we find no evidence of hydrophobic patches detectable by ANS binding see above.



However, an alternative explanation of the unusual intrinsic fluorescence could be that the Trp side chain of latherin is located away from bulk water, but in an unusually polar environment within the protein structure.



We have attempted to clarify this using standard fluorescence quenching probes iodide, acrylamide, succinimide, but with somewhat ambiguous results see Table 1. Intrinsic Trp fluorescence was reduced in the presence of quenchers, and all three probes gave linear Stern-Volmer plots Figure 2C inset symptomatic of collisional quenching for a single Trp-containing protein [28] , [31] ; quenching parameters K SV are given in Table 1.



Paradoxically for a putatively exposed tryptophan side-chain, quenching was lowest with iodide — normally considered to be most effective in quenching exposed groups, but likely to be strongly influenced by local electrostatic effects refs.



Neutral quenchers acrylamide, succinimide were much more effective, with relatively high K SV values comparable to those previously observed for proteins with relatively exposed Trp residues [28] , [31].



Interestingly, these quenching parameters were not significantly affected by either thermal or chemical denaturation of the protein see Table 1. This suggests that the latherin Trp may well be in an exposed, polar environment, but protected from collisional iodide quenching by surrounding negative charges or other local sequence-specific effects.



It has recently been shown that tryptophan fluorescence and its quenching can be significantly affected by local amino acids, even in small model peptides in strongly denaturing environments [32] , [33].



Significantly, and in contrast to previous assumptions, this work has shown that quenching by both acrylamide and iodide is highly variable and sequence dependent, with iodide quenching in particular being significantly reduced in the presence of nearby negatively-charged residues.



Moreover, Trp is adjacent in sequence to an aspartate residue Asp, a juxtaposition that has been shown to inhibit iodide quenching in model peptides [33]. Using the more quantitative Du Nouy ring method, the protein was found to be substantially more active at reducing the surface tension of water than either lysozyme negligible effect or bovine serum albumin which presumably owes its activity to contamination with lipid or the presence of surface-proximal hydrophobic ligand binding sites on a weight basis Figure 3B.



At protein concentrations above 0. B The surface tension of solutions containing either chicken egg lysozyme, bovine serum albumin BSA or recombinant latherin at the concentrations indicated, measured using the de Nuoy ring method.



The fitted lines are for guidance only. C Neutron reflectivity profiles for 0. The solid lines are the theoretical fits to a single-layer model for adsorption of latherin at the air-water interface with parameters given in Table 2.



Surface wetting is likely to be accompanied by adsorption of surfactant protein molecules onto a hydrophobic surface. This was previously indicated by contact angle experiments with natural latherin showing that a hydrophobic surface pre-exposed to natural latherin was wettable, presumably because of adsorbed protein [8].



Interestingly, absorbed rlatherin could also be removed by gentle washing with water prior to protein staining. This latter feature is presumably of functional significance, since permanent wetting would compromise the natural water-repellent properties of the oily pelt and provide a nutritive source for microorganisms.



The strong surfactant activity of rlatherin, manifest in its ability dramatically to reduce the surface tension of water at low concentrations, is unusual for a structurally intact soluble protein and implies that it must undergo significant adsorption at the air-water interface of aqueous solutions.



Detailed parameters for 0. By comparing results in these two solvents, information on how the layer is packed and its location relative to the water surface above or below the interface is inferred.



The volume fraction of latherin in the layer may thereby be estimated to be 0. The estimated surface excess is 0. Similar results were obtained for latherin both at lower concentration 0.



This interfacial layer seems surprisingly thin for a 23 kDa protein layer in equilibrium with the bulk solution where, judging from CD and DSC observations, latherin behaves as a folded globular protein.



We have recently used infrared reflectance to demonstrate the presence of both intact alpha-helix and beta-structures for a different surfactant protein that also appears to be a folded globular protein in bulk solution [34].



This makes sense in functional terms. Soluble surfactant proteins need to reconcile surfactant activity at the site of operation with the requirement for solubility and lack of aggregation during synthesis, storage, and transport stages.



Conventional small molecule detergents are amphiphilic and can form soluble aggregates micelles in solution that can readily dissociate to form surface monolayers when required. This would be a difficult strategy for protein surfactants, since the large exposed hydrophobic surfaces required at interfaces would lead to significant solubility and aggregation problems in bulk solution.



The unusually high leucine content of latherin, atypical of soluble globular proteins, may be related to this proposed surfactant mechanism. A range of tissues was sampled from a horse, with mRNA prepared for detection of latherin transcripts by RT-PCR, and protein extracted for immunodetection using a rabbit antibody to recombinant latherin rlatherin.



As shown in Figure 4A, latherin transcripts were only detectable in skin and submaxillary salivary gland, and the protein was only detectable from skin, salivary gland, tongue and cheek Figure 4B.



In the case of the latter two sites, the tissue samples included epithelium, in which no transcripts were detected in separate experiments, so it is likely that the protein detected there was derived from contaminating saliva.



In a more limited screen, we found, as expected, that the gene for the major allergen of horses, Equ c 1, a lipocalin of unknown function though may be a pheromone carrier [36] — [38] , was also transcribed in skin and submaxillary gland tissue.



A RT-PCR using gene-specific oligonucleotide primers to detect latherin-encoding transcripts in a range of horse tissues; the ribosomal subunit protein S15 was used as a control.



B Immunoblot using latherin-specific antibody to detect latherin protein in tissue samples. C Immunoblot showing IgE antibody reactivity of serum from a horse-allergic patient binding to recombinant latherin rL and horse sweat S.



Five out of nine patients with detectable IgE antibody reactions to horse sweat exhibited IgE antibody to recombinant latherin. Sera from non-allergic individuals did not react to any components in horse sweat or the recombinant latherin.



R — reference proteins with M r expressed in kDa. D Immunoperoxidase labelling of a section of normal equine skin showing a dense dark band brown of staining proximal to the apical membrane of the sweat gland secretory epithelial cells; cell surface associated latherin is likely to have been lost during the preparation process.



Staining is also apparent in intracellular vesicles. E Immuno-fluorescent staining for latherin in equine sweat glands. Bright staining indicates the presence of latherin inside the secretory cells of the gland.



As mentioned above, the amino acid sequence of latherin encompasses two peptides that have previously been ascribed to the separately classified allergens Equ c 4 and Equ c 5 [16]. We obtained serum samples from eight horse-allergic patients and examined the antigen binding activity of their IgE antibody see Figure 4C for a typical result.



This showed that patient IgE antibody bound to several components of horse sweat, the major band being at approximately M r 21,, which would correspond to the major allergen of horses, Equ c 1 which is also produced both in skin and saliva, [16] , [36] , [37].



The band at approximately M r 17, co-migrates with recombinant latherin rlatherin, which is also bound by the patients' IgE antibody. This immunoblot also shows the more rapid migration exhibited by latherin in SDS-PAGE than expected for its size, possibly due to its very high content of apolar amino acids and consequent more rapid migration caused by a high degree of binding by SDS detergent.



These biochemical and biophysical observations suggest the evolution of a dual role for latherin as both a sweat and a salivary protein. Its presence in equine sweat is consistent with a role in wetting hair and skin to allow rapid translocation and spreading of sweat water at the surface of the oily pelt for evaporative cooling.



Interestingly, human skin secretions are also thought to have a surfactant-like role in enhancing the spreading of sweat water for cooling, though by a mechanism suited to an effectively hairless surface [40] , [41].



The deposition of large quantities of protein through and over the pelt of horses would seem to present the risk of providing a nutrient resource for microorganisms. It could therefore be that latherin's surface activity may also directly affect the surfaces of microbes or impede their adhesion and establishment on hair and skin.



Latherin is distantly related to proteins that are directly anti-microbial [21] , but we have been unable to detect any interaction between latherin and archetypical bacterial components such as lipopolysaccharide not shown.



A function for latherin in horse saliva is less obvious, but the presence of a surfactant protein there may assist mastication and processing of large quantities of relatively dry vegetable matter, a diet for which the equids as a group are specialised, unlike ruminants cows, sheep, etc.



The possibility that latherin's surface-activity presents a danger to mammalian cells, however, needs to be addressed, as does the mechanism by which the intracellular membrane systems involved in synthesis, processing and export of the protein are protected from damage.



A simple small molecule detergent would normally be extremely damaging to cellular membranes, but it is possible that proteins can be designed to perform detergent-like functions without endangering cell membranes.



An example of this could be the strong surface activity of the proteinaceous foams in which certain tropical frogs lay their eggs, which may also have anti-microbial propensities, but are nonetheless compatible with naked eggs and spermatozoa [42] , [43].



It is possible that latherin is specially packaged by the synthesising cells before release, and our immunohistological observations on horse skin using anti-latherin antibody indicate that the protein is localised to the protein granules of the cells in the fundus region of the sweat gland, which are known to be exocytosed directly upon sweating [39].



At a more fundamental level, the mechanism by which small-molecule detergents solubilise lipid bilayer membranes is likely to be inapplicable to larger, surfactant proteins. Conventional synthetic detergents such as SDS, Triton, etc.



In contrast, although specific surfactant proteins do partition into the air-water interface [42] , their size and presumably structure precludes any equivalent of micelle formation in the bulk solution, therefore minimizing disruption of lipid bilayers.



There are now several different classes of protein that exhibit biologically relevant, intrinsic surface-activity, including latherin, the hydrophobins and frog foam nest foam proteins ranaspumins.



It would be valuable to know what structural characteristics separate or unify these proteins so as to extend our understanding of how proteins can do what they do. In the case of latherin, we are fortunate that it can be produced in soluble recombinant form in bacteria, and we have already obtained high quality protein NMR spectra as a preliminary to solving its solution structure R.



A structure for latherin may also improve our understanding of the PLUNC and BASE proteins, some of which may also possess intrinsic surface activity in order to operate in mucosal surfaces. Meanwhile, in the absence of indications that PLUNC family members are produced in mammalian skin, latherin may represent a remarkable adaptation of a salivary protein for heat dissipation from skin by horses and their ilk, and a readily available protein with which to study intrinsic surface activity of a naturally folded protein from a mammal.



All tissue samples used in the study were collected from animals that died from, or were euthanised for, clinical causes entirely unconnected to the investigation, and with permission from the owners, and for which no formal ethical permission is required under UK Home Office regulations.



Sweat was collected from racehorses by gentle use of an equine sweat collector in Scotland under permission of the owners and Glasgow University's Veterinary Ethics and Welfare Committee and in Trinidad under permission from the owners and the Chief Veterinary Officer of the Republic of Trinidad and Tobago.



Sweat was collected from racehorses in Scotland and Trinidad. Natural latherin was purified from horse sweat and tryptic peptide fragments were sequenced as described previously [8].



Specifically, portions of reduced and carboxymethylated latherin were dissolved in 0. Substantial precipitation occurred in both enzymic digests, and the insoluble peptides were separated by centrifugation.



Peptide fractions were lyophilised repeatedly to remove ammonium bicarbonate. The soluble S peptides were dissolved in 0. Aliquots of the S and I peptide mixtures were fractionated by reversed phase chromatography on a silica-C8 reversed phase column Waters, Elstree, Hertfordshire, UK using a solvent gradient of increasing acetonitrile concentration containing 0.



Peptide fractions were pooled and aliquots hydrolysed and subjected to amino acid analysis [8]. Samples of peptides were sent for analysis by liquid phase automated Edman degradation at the Department of Biochemistry, University of Aberdeen.



This procedure provided cDNA sequence for horse latherin, and the encoded protein contained all the peptide sequences obtained from sweat-derived latherin Figure 1B and Table S1. Similar procedures were used to obtain partial cDNA sequences from the other equid species, using additional primer sets designed to overlap those of the original primer positions to ensure that the final sequences were fully correct for each species.



The cultures were grown until an OD of 0. The thioredoxin tag was cleaved by overnight incubation with recombinant enterokinase Novagen, and the enzyme removed by passing through a column packed with EK Agarose Novagen.



The solution was diluted with binding buffer 20 mM Tris, 0. Skin samples were obtained from lateral neck skin of horses in the UK immediately after euthanasia for veterinary reasons not associated with skin complaints.



Four-micron sections of equine skin containing sweat glands were mounted on 3-aminopropyl-triethoxy-silane APES treated slides. Endogenous avidin and biotin sites were blocked using an Avidin Biotin Blocking kit Vector Laboratories, Orton Southgate, Peterborough, UK involving incubation with each blocker for 30 min.



The Arabian also developed the high spirit and alertness needed in a horse used for raiding and war. This combination of willingness and sensitivity requires modern Arabian horse owners to handle their horses with competence and respect.



The Arabian is a versatile breed. Arabians dominate the discipline of endurance riding, and compete today in many other fields of equestrian sport. They are one of the top ten most popular horse breeds in the world.



Arabian horses have refined, wedge-shaped heads, a broad forehead, large eyes, large nostrils, and small muzzles. Most display a distinctive concave, or "dished" profile.



Many Arabians also have a slight forehead bulge between their eyes, called the jibbah by the Bedouin, that adds additional sinus capacity, believed to have helped the Arabian horse in its native dry desert climate.



This structure of the poll and throatlatch was called the mitbah or mitbeh by the Bedouin. In the ideal Arabian it is long, allowing flexibility in the bridle and room for the windpipe.



Other distinctive features are a relatively long, level croup, or top of the hindquarters, and naturally high tail carriage. Some individuals have wider, more powerfully muscled hindquarters suitable for intense bursts of activity in events such as reining, while others have longer, leaner muscling better suited for long stretches of flat work such as endurance riding or horse racing.



They are especially noted for their endurance, [6] [7] and the superiority of the breed in Endurance riding competition demonstrates that well-bred Arabians are strong, sound horses with superior stamina.



At international FEI - sponsored endurance events, Arabians and half-Arabians are the dominant performers in distance competition. Some Arabians, though not all, have 5 lumbar vertebrae instead of the usual 6, and 17 pairs of ribs rather than However, the croup is formed by the sacral vertebrae.



The hip angle is determined by the attachment of the ilium to the spine, the structure and length of the femur, and other aspects of hindquarter anatomy, which is not correlated to the topline of the sacrum.



Thus, the Arabian has conformation typical of other horse breeds built for speed and distance, such as the Thoroughbred, where the angle of the ilium is more oblique than that of the croup.



Horses bred to gallop need a good length of croup and good length of hip for proper attachment of muscles, and so unlike angle, length of hip and croup do go together as a rule. The breed standard stated by the United States Equestrian Federation, describes Arabians as standing between However, the Arabian horse is noted for a greater density of bone than other breeds, short cannons, sound feet, and a broad, short back, [2] all of which give the breed physical strength comparable to many taller animals.



For tasks where the sheer weight of the horse matters, such as farm work done by a draft horse, [16] any lighter-weight horse is at a disadvantage. For centuries, Arabian horses lived in the desert in close association with humans.



On the other hand, the Arabian is also classified as a "hot-blooded" breed, a category that includes other refined, spirited horses bred for speed, such as the Akhal-Teke, the Barb, and the Thoroughbred.



Like other hot-bloods, Arabians' sensitivity and intelligence enable quick learning and greater communication with their riders; however, their intelligence also allows them to learn bad habits as quickly as good ones, [20] and they do not tolerate inept or abusive training practices.



The Arabian Horse Association registers purebred horses with the coat colors bay, gray, chestnut, black, and roan. Black skin provided protection from the intense desert sun. Although many Arabians appear to have a "white" hair coat, they are not genetically "white".



This color is usually created by the natural action of the gray gene, and virtually all white-looking Arabians are actually grays. There are a very few Arabians registered as "white" having a white coat, pink skin and dark eyes from birth.



These animals are believed to manifest a new form of dominant white, a result of a nonsense mutation in DNA tracing to a single stallion foaled in One spotting pattern, sabino, does exist in purebred Arabians.



Sabino coloring is characterized by white markings such as "high white" above the knees and hocks, irregular spotting on the legs, belly and face, white markings that extend beyond the eyes or under the chin and jaw, and sometimes lacy or roaned edges.



The genetic mechanism that produces sabino patterning in Arabians is undetermined, and more than one gene may be involved. The inheritance patterns observed in sabino-like Arabians also do not follow the same mode of inheritance as sabino 1.



There are very few Arabians registered as roan, and according to researcher D. Phillip Sponenberg, roaning in purebred Arabians is actually the action of rabicano genetics. However, a roan does not consistently lighten with age, while a gray does.



Purebred Arabians never carry dilution genes. Spotting or excess white was believed by many breeders to be a mark of impurity until DNA testing for verification of parentage became standard.



For a time, horses with belly spots and other white markings deemed excessive were discouraged from registration and excess white was sometimes penalized in the show ring. To produce horses with some Arabian characteristics but coat colors not found in purebreds, they have to be crossbred with other breeds.



Because purebred Arabians cannot produce LWS foals, Arabian mares were used as a non-affected population in some of the studies seeking the gene that caused the condition in other breeds.



There are six known genetic disorders in Arabian horses. Two are inevitably fatal, two are not inherently fatal but are disabling and usually result in euthanasia of the affected animal; the remaining conditions can usually be treated.



Three are thought to be autosomal recessive conditions, which means that the flawed gene is not sex-linked and has to come from both parents for an affected foal to be born; the others currently lack sufficient research data to determine the precise mode of inheritance.



Genetic diseases that can occur in purebred Arabians, or in partbreds with Arabian ancestry in both parents, are the following:. The Arabian Horse Association in the United States has created a foundation that supports research efforts to uncover the roots of genetic diseases.



Fight Off Arabian Lethals is a clearinghouse for information on these conditions. Arabian horses are the topic of many myths and legends. One origin story tells how Muhammad chose his foundation mares by a test of their courage and loyalty.



While there are several variants on the tale, a common version states that after a long journey through the desert, Muhammad turned his herd of horses loose to race to an oasis for a desperately needed drink of water.



Before the herd reached the water, Muhammad called for the horses to return to him. Only five mares responded. Because they faithfully returned to their master, though desperate with thirst, these mares became his favorites and were called Al Khamsa, meaning, the five.



These mares became the legendary founders of the five "strains" of the Arabian horse. Another origin tale claims that King Solomon was given a pure Arabian-type mare named Safanad "the pure" by the Queen of Sheba.



This legendary stallion was said to be faster than the zebra and the gazelle, and every hunt with him was successful, thus when he was put to stud, he became a founding sire of legend. Yet another creation myth puts the origin of the Arabian in the time of Ishmael, the son of Abraham.



The Angel then commanded the thundercloud to stop scattering dust and rain, and so it gathered itself into a prancing, handsome creature - a horse - that seemed to swallow up the ground. Hence, the Bedouins bestowed the title "Drinker of the Wind" to the first Arabian horse.



Finally, a Bedouin story states that Allah created the Arabian horse from the south wind and exclaimed, "I create thee, Oh Arabian. To thy forelock, I bind Victory in battle. On thy back, I set a rich spoil and a Treasure in thy loins.



I establish thee as one of the Glories of the Earth I give thee flight without wings. Men shall follow you wherever you go; you shall be as good for flight as for pursuit; you shall fly without wings; riches shall be on your back and fortune shall come through your meditation.



Arabians are one of the oldest human-developed horse breeds in the world. Horses with these features appeared in rock paintings and inscriptions in the Arabian Peninsula dating back years.



Some scholars of the Arabian horse once theorized that the Arabian came from a separate subspecies of horse, [73] known as equus caballus pumpelli. The modern concept of breed purity in the modern population cannot be traced beyond years.



There are different theories about where the ancestors of the Arabian originally lived. Most evidence suggests the proto-Arabian came from the area along the northern edge of the Fertile Crescent.



Regardless of origin, climate and culture ultimately created the Arabian. Where there was no pasture or water, the Bedouin fed their horses dates and camel's milk. Weak individuals were weeded out of the breeding pool, and the animals that remained were also honed by centuries of human warfare.



The Bedouin way of life depended on camels and horses: Arabians were bred to be war horses with speed, endurance, soundness, and intelligence. For centuries, the Bedouin tracked the ancestry of each horse through an oral tradition.



Horses of the purest blood were known as Asil and crossbreeding with non - Asil horses was forbidden. Mares were the most valued, both for riding and breeding, and pedigree families were traced through the female line.



The Bedouin did not believe in gelding male horses, and considered stallions too intractable to be good war horses, thus they kept very few colts, selling most, and culling those of poor quality.



Over time, the Bedouin developed several sub-types or strains of Arabian horse, each with unique characteristics, [86] and traced through the maternal line only. Raswan felt that these strains represented body "types" of the breed, with the Kehilan being "masculine", the Seglawi being "feminine" and the Muniqi being "speedy".



Purity of bloodline was very important to the Bedouin, and they also believed in telegony, believing if a mare was ever bred to a stallion of "impure" blood, the mare herself and all future offspring would be "contaminated" by the stallion and hence no longer Asil.



This complex web of bloodline and strain was an integral part of Bedouin culture; they not only knew the pedigrees and history of their best war mares in detail, but also carefully tracked the breeding of their camels, Saluki dogs, and their own family or tribal history.



Fiery war horses with dished faces and high-carried tails were popular artistic subjects in Ancient Egypt and Mesopotamia, often depicted pulling chariots in war or for hunting.



Horses with oriental characteristics appear in later artwork as far north as that of Ancient Greece and the Roman Empire. While this type of horse was not called an "Arabian" in the Ancient Near East until later, the word "Arabia" or "Arabaya" first appeared in writing in Ancient Persia, c.



For example, a horse skeleton unearthed in the Sinai peninsula, dated to BC and probably brought by the Hyksos invaders, is considered the earliest physical evidence of the horse in Ancient Egypt. This horse had a wedge-shaped head, large eye sockets and small muzzle, all characteristics of the Arabian horse.



Following the Hijra in AD also sometimes spelled Hegira, the Arabian horse spread across the known world of the time, and became recognized as a distinct, named breed.



By, Muslim influence expanded across the Middle East and North Africa, by Muslim warriors had reached Spain, and they controlled most of the Iberian Peninsula by Their war horses were of various oriental types, including both Arabians and the Barb horse of North Africa.



Arabian horses also spread to the rest of the world via the Ottoman Empire, which rose in Though it never fully dominated the heart of the Arabian Peninsula, this Turkish empire obtained many Arabian horses through trade, diplomacy and war.



A stud farm record was made of his purchases describing many of the horses as well as their abilities, and was deposited in his library, becoming a source for later study.



Historically, Egyptian breeders imported horses bred in the deserts of Palestine and the Arabian peninsula as the source of their foundation bloodstock. One of the most famous was Muhammad Ali of Egypt, also known as Muhammad Ali Pasha, who established an extensive stud farm in the 19th century.



However, after Abbas Pasha was assassinated in, his heir, El Hami Pasha, sold most of his horses, often for crossbreeding, and gave away many others as diplomatic gifts. At its peak, the stud of Ali Pasha Sherif had over purebred Arabians.



After his death, Lady Anne was also able to gather many remaining horses at her Sheykh Obeyd stud. Meanwhile, the passion brought by the Blunts to saving the pure horse of the desert helped Egyptian horse breeders to convince their government of the need to preserve the best of their own remaining pure Arabian bloodstock that descended from the horses collected over the previous century by Muhammad Ali Pasha, Abbas Pasha and Ali Pasha Sherif.



Probably the earliest horses with Arabian bloodlines to enter Europe came indirectly, through Spain and France. Others would have arrived with returning Crusaders [] —beginning in, European armies invaded Palestine and many knights returned home with Arabian horses as spoils of war.



Later, as knights and the heavy, armored war horses who carried them became obsolete, Arabian horses and their descendants were used to develop faster, agile light cavalry horses that were used in warfare into the 20th century.



Another major infusion of Arabian horses into Europe occurred when the Ottoman Turks sent, horsemen into Hungary in, many of whom were mounted on pure-blooded Arabians, captured during raids into Arabia.



By, the Ottomans reached Vienna, where they were stopped by the Polish and Hungarian armies, who captured these horses from the defeated Ottoman cavalry. Some of these animals provided foundation bloodstock for the major studs of eastern Europe.



With the rise of light cavalry, the stamina and agility of horses with Arabian blood gave an enormous military advantage to any army who possessed them. As a result, many European monarchs began to support large breeding establishments that crossed Arabians on local stock, one example being Knyszyna, the royal stud of Polish king Zygmunt II August, and another the Imperial Russian Stud of Peter the Great.



European horse breeders also obtained Arabian stock directly from the desert or via trade with the Ottomans. In Poland, notable imports from Arabia included those of Prince Hieronymous Sanguszko — , who founded the Slawuta stud.



The 18th century marked the establishment of most of the great Arabian studs of Europe, dedicated to preserving "pure" Arabian bloodstock. The Prussians set up a royal stud in, originally intended to provide horses for the royal stables, and other studs were established to breed animals for other uses, including mounts for the Prussian army.



The foundation of these breeding programs was the crossing of Arabians on native horses; by some English observers felt that the Prussian calvalry mounts were superior in endurance to those of the British, and credited Arabian bloodlines for this superiority.



One of the most famous Arabian stallions in Europe was Marengo, the war horse ridden by Napoleon Bonaparte. During the midth century, the need for Arabian blood to improve the breeding stock for light cavalry horses in Europe resulted in more excursions to the Middle East.



Queen Isabel II of Spain sent representatives to the desert to purchase Arabian horses and by had established a stud book; her successor, King Alfonso XII imported additional bloodstock from other European nations.



The military remained heavily involved in the importation and breeding of Arabians in Spain well into the early 20th century, and the Yeguada Militar is still in existence today.



This period also marked a phase of considerable travel to the Middle East by European civilians and minor nobility, and in the process, some travelers noticed that the Arabian horse as a pure breed of horse was under threat due to modern forms of warfare, inbreeding and other problems that were reducing the horse population of the Bedouin tribes at a rapid rate.



Perhaps the most famous of all Arabian breeding operations founded in Europe was the Crabbet Park Stud of England, founded Upon Lady Anne's death in, the Blunts' daughter, Judith, Lady Wentworth, inherited the Wentworth title and Lady Anne's portion of the estate, and obtained the remainder of the Crabbet Stud following a protracted legal battle with her father.



Upon her death in, the stud passed to her manager, Cecil Covey, who ran Crabbet until, when a motorway was cut through the property, forcing the sale of the land and dispersal of the horses.



In the early 20th century, the military was involved in the breeding of Arabian horses throughout Europe, particularly in Poland, Spain, Germany, and Russia; private breeders also developed a number of breeding programs.



The Russian Revolution, combined with the effects of World War I, destroyed most of the breeding programs in Russia, but by, the Soviet government reestablished an Arabian program, the Tersk Stud, on the site of the former Stroganov estate, [] [] which included Polish bloodstock as well as some importations from the Crabbet Stud in England.



Not all European studs recovered. The Weil stud of Germany, founded by King Wilhelm I, went into considerable decline; by the time the Weil herd was transferred to the Marbach State Stud in, only 17 purebred Arabians remained.



The Veragua stud was destroyed, and its records lost, with the only survivors being the broodmares and the younger horses, who were rescued by Francisco Franco. Both the Soviet Union and the United States obtained valuable Arabian bloodlines as spoils of war, which they used to strengthen their breeding programs.



The Soviets had taken steps to protect their breeding stock at Tersk Stud, and by utilizing horses captured in Poland they were able to re-establish their breeding program soon after the end of World War II.



Army Remount station, the former W. Kellogg Ranch in California. In the postwar era, Poland, [] Spain, [] and Germany developed or re-established many well-respected Arabian stud farms.



While only a few Arabians were exported from behind the Iron Curtain during the Cold War, those who did come to the west caught the eye of breeders worldwide.



Improved international relations between eastern Europe and the west led to major imports of Polish and Russian-bred Arabian horses to western Europe and the United States in the s and s.



Organizations such as the World Arabian Horse Association WAHO created consistent standards for transferring the registration of Arabian horses between different nations. Today, Arabian horses are traded all over the world.



The first horses on the American mainland since the end of the Ice Age arrived with the Spanish Conquistadors. Many horses escaped or were stolen, becoming the foundation stock of the American Mustang.



Colonists from England also brought horses of Arabian breeding to the eastern seaboard. One of George Washington 's primary mounts during the American Revolutionary War was a gray half-Arabian horse named Blueskin, sired by the stallion "Ranger", also known as "Lindsay's Arabian", said to have been obtained from the Sultan of Morocco.



Keene Richard was the first American known to have specifically bred Arabian horses. He traveled to the desert in and to obtain breeding stock, which he crossed on Thoroughbreds, and also bred purebred Arabians.



Unfortunately, his horses were lost during the Civil War and have no known purebred Arabian descendants today. Leopard is the only stallion imported prior to who left known purebred descendants in America.



In, the Arabian Horse Registry of America was established, recording 71 animals, [] and by, the number had reached half a million. Today there are more Arabians registered in North America than in the rest of the world put together.



The origins of the registry date to, when the Hamidie Society sponsored an exhibit of Arabian horses from what today is Syria at the World Fair in Chicago.



Records are unclear if 40 or 45 horses were imported for the exposition, but seven died in a fire shortly after arrival. The 28 horses that remained at the end of the exhibition stayed in America and were sold at auction when the Hamidie Society went bankrupt.



Major Arabian importations to the United States included those of Davenport and Bradley, who teamed up to purchase several stallions and mares directly from the Bedouin in Brown of the Maynesboro Stud, interested in the Arabian as a cavalry mount, imported many Arabians over a period of years, starting in Army Remount Service, which stood purebred stallions at public stud for a reduced rate.



In the s, Arabians became a popular status symbol and were marketed similarly to fine art. When the Tax Reform Act of closed the tax-sheltering "passive investment" loophole, limiting the use of horse farms as tax shelters, [] [] the Arabian market was particularly vulnerable due to over-saturation and artificially inflated prices, and it collapsed, forcing many breeders into bankruptcy and sending many purebred Arabians to slaughter.



Arabian horses were introduced to Australia in the earliest days of European Settlement. Early imports included both purebred Arabians and light Spanish " jennets " from Andalusia, many Arabians also came from India.



Based on records describing stallions "of Arabic and Persian blood", the first Arabian horses were probably imported to Australia in several groups between and Throughout the 19th century, many more Arabians came to Australia, though most were used to produce crossbred horses and left no recorded purebred descendants.



In the early 20th century, more Arabian horses, mostly of Crabbet bloodlines, arrived in Australia. The first Arabians of Polish breeding arrived in, and Egyptian lines were first imported in Arabian horses from the rest of the world followed, and today the Australian Arabian horse registry is the second largest in the world, next to that of the United States.



Arabian horses today are found all over the world. They are no longer classified by Bedouin strain, but are informally classified by the nation of origin of famed horses in a given pedigree.



Popular types of Arabians are labeled "Polish", "Spanish", "Crabbet", "Russian", "Egyptian", and "Domestic" describing horses whose ancestors were imported to the United States prior to, including those from programs such as Kellogg, Davenport, Maynesboro, Babson, Dickenson and Selby.



Each set of bloodlines has its own devoted followers, with the virtues of each hotly debated. Most debates are between those who value the Arabian most for its refined beauty and those who value the horse for its stamina and athleticism; there are also a number of breeders who specialize in preservation breeding of various bloodlines.



Controversies exist over the relative "purity" of certain animals; breeders argue about the genetic "purity" of various pedigrees, discussing whether some horses descend from "impure" animals that cannot be traced to the desert Bedouin.



Because of the genetic strength of the desert-bred Arabian horse, Arabian bloodlines have played a part in the development of nearly every modern light horse breed, including the Thoroughbred, [] Orlov Trotter, [] Morgan, [] American Saddlebred, [] American Quarter Horse, [] and Warmblood breeds such as the Trakehner.



Today, people cross Arabians with other breeds to add refinement, endurance, agility and beauty. There is intense debate over the role the Arabian played in the development of other light horse breeds.



Before DNA-based research developed, one hypothesis, based on body types and conformation, suggested the light, "dry", oriental horse adapted to the desert climate had developed prior to domestication; [] DNA studies of multiple horse breeds now suggest that while domesticated horses arose from multiple mare lines, there is very little variability in the Y-chromosome between breeds.



There is little doubt that humans crossed "oriental" blood on that of other types to create light riding horses; the only actual questions are at what point the "oriental" prototype could be called an "Arabian", how much Arabian blood was mixed with local animals, and at what point in history.



For some breeds, such as the Thoroughbred, Arabian influence of specific animals is documented in written stud books. For example, while outside cultures, and the horses they brought with them, influenced the predecessor to the Iberian horse in both the time of Ancient Rome and again with the Islamic invasions of the 8th century, it is difficult to trace precise details of the journeys taken by waves of conquerors and their horses as they traveled from the Middle East to North Africa and across Gibraltar to southern Europe.



Mitochondrial DNA studies of modern Andalusian horses of the Iberian peninsula and Barb horses of North Africa present convincing evidence that both breeds crossed the Strait of Gibraltar and influenced one another.



Arabians and Barbs, though probably related to one another, are quite different in appearance, [] and horses of both Arabian and Barb type were present in the Muslim armies that occupied Europe.



Arabians are versatile horses that compete in many equestrian fields, including horse racing, the horse show disciplines of saddle seat, Western pleasure, and hunt seat, as well as dressage, cutting, reining, endurance riding, show jumping, eventing, youth events such as equitation, and others.



They are used as pleasure riding, trail riding, and working ranch horses for those who are not interested in competition. Arabians dominate the sport of endurance riding because of their stamina.



Classes offered include Western pleasure, reining, hunter type and saddle seat English pleasure, and halter, plus the very popular "Native" costume class. Other nations also sponsor major shows strictly for purebred and partbred Arabians, including Great Britain [] France, [] Spain, [] Poland, [] and the United Arab Emirates.



Purebred Arabians have excelled in open events against other breeds. One of the most famous examples in the field of western riding competition was the Arabian mare Ronteza, who defeated 50 horses of all breeds to win the Reined Cow Horse championship at the Cow Palace in San Francisco, California.



Part-Arabians have also appeared at open sport horse events and even Olympic level competition. The Anglo-Arabian Linon was ridden to an Olympic silver medal for France in Dressage in and, as well as a team gold in, and another French Anglo-Arabian, Harpagon, was ridden to a team gold medal and an individual silver in dressage at the Olympics.



Arabians are involved in a wide variety of activities, including fairs, movies, parades, circuses and other places where horses are showcased. They have been popular in movies, dating back to the silent film era when Rudolph Valentino rode the Kellogg Arabian stallion Jadaan in 's Son of the Sheik, [] and have been seen in many other films, including The Black Stallion featuring the stallion Cass Ole, [] The Young Black Stallion, which used over 40 Arabians during filming, [] as well as Hidalgo [] and the version of Ben-Hur.



Arabians are mascots for football teams, performing crowd-pleasing activities on the field and sidelines. One of the horses who serves as "Traveler" , the mascot for the University of Southern California Trojans, has been a purebred Arabian.



Arabians also are used on search and rescue teams and occasionally for police work. From Wikipedia, the free encyclopedia. Redirected from Arabian Horse. This is the latest accepted revision, reviewed on 26 March For other uses, see Arabian horse disambiguation.



Equine coat color and Equine coat color genetics. Arabian Horse Association and Endurance riding. United States Equestrian Federation. Archived from the original PDF on March 3, Retrieved May 28, Reprinted in Parkinson, pp.



Archived from the original on June 12, Arabian Horse Society of Australia. Archived from the original on April 30, Retrieved May 31, The Croup", Anatomy and Conformation of the Horse, pp.



Reprinted in Parkinson, p. Archived from the original on May 13, Breeds not allowing stallions in youth classes include, but are not limited to, Rule c American Quarter Horse Archived February 7, , at the Wayback Machine.



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28.03.2018 - One spotting pattern, sabinodoes exist in purebred Arabians. Changing the World — The sequences of all the tryptic peptides obtained from sweat-derived latherin appear in the sequence encoded by the cDNA, as do those of horse allergens originally designated Equ c 4 and Equ c 5 [16] Figure 1B. Modem roteador 4g e 3g wifi huawei e8372 - Windows... Before DNA-based research developed, one hypothesis, based on body types and conformation, suggested the light, "dry", oriental horse adapted to the desert climate had developed prior to domestication; [] DNA studies of multiple horse breeds now suggest that while domesticated horses arose from multiple mare lines, there is very little variability in the Y-chromosome between breeds. Archived from the original on July 5,





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13.02.2018 - D Immunoperoxidase labelling of a section of normal equine skin showing a dense dark band brown of staining proximal to the apical membrane of the sweat gland secretory epithelial cells; cell surface associated latherin is likely to have been lost during the preparation process. The origins of the registry date towhen the Hamidie Society sponsored an exhibit of Arabian horses from what today is Syria at the World Fair in Chicago. Oneplus t mobile 03479 micro usb car charger - Win... There are very few Arabians registered as roanand according to researcher D. Arabian horses also spread to the rest of the world via the Ottoman Empirewhich rose in





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07.02.2018 - Interestingly, absorbed rlatherin could also be removed by gentle washing with water prior to protein staining. Retrieved July 2, One plus 5t price in nepal 3 star - Liquor store n... Arabian Horse - Bloodlines. Natural latherin was purified from horse sweat and tryptic peptide fragments were sequenced as described previously [8].









Jack de la Torre, MD, Ph. There were people there who were openly biased against the compound even though they knew very little about it. With the new administration at that agency, it has changed a bit.



The first quality that struck Dr. Jacob about the drug was its ability to pass through membranes, an ability that has been verified by numerous subsequent researchers. From 70 percent to 90 percent has been found to be the most effective strength across the skin, and, oddly, performance drops with concentrations higher than 90 percent.



Lower concentrations are sufficient to cross other membranes. Thus, 15 percent DMSO will easily penetrate the bladder. In addition, DMSO can carry other drugs with it across membranes. It is more successful ferrying some drugs, such as morphine sulfate, penicillin, steroids, and cortisone, than others, such as insulin.



What it will carry depends on the molecular weight, shape, and electrochemistry of the molecules. This property would enable DMSO to act as a new drug delivery system that would lower the risk of infection occurring whenever skin is penetrated.



Relief is reported to be almost immediate, lasting up to 6 hours. A number of sports teams and Olympic athletes have used DMSO, although some have since moved on to other treatment modalities.



When administration ceases, so do the effects of the drug. Jacob said at a hearing of the U. Senate Subcommittee on Health in, "DMSO is one of the few agents in which effectiveness can be demonstrated before the eyes of the observers If we have patients appear before the Committee with edematous sprained ankles, the application of DMSO would be followed by objective diminution of swelling within an hour.



No other therapeutic modality will do this. Chronic pain patients often have to apply the substance for 6 weeks before a change occurs, but many report relief to a degree they had not been able to obtain from any other source.



DMSO reduces inflammation by several mechanisms. It is an antioxidant, a scavenger of the free radicals that gather at the site of injury. This capability has been observed in experiments with laboratory animals7 and in ulcerative colitis patients in a double-blinded randomized study in Baghdad, Iraq.



At the Cleveland Clinic Foundation in Cleveland, Ohio, in, patients with inflammatory genitourinary disorders were studied. Researchers concluded that DMSO brought significant relief to the majority of patients.



They recommended the drug for all inflammatory conditions not caused by infection or tumor in which symptoms were severe or patients failed to respond to conventional therapy.



Stephen Edelson, MD, F. When patients come in with rheumatoid arthritis, we put them on IV DMSO, maybe three times a week, while we are evaluating the causes of the disease, and it is amazing how free they get.



It really is a dramatic treatment. As for side effects, Dr. And we use large doses. The odor is a problem. Some men have to move out of the room [shared] with their wives and into separate bedrooms.



That is basically the only problem. DMSO was the first nonsteroidal anti-inflammatory discovered since aspirin. Bristol believes that it was that discovery that spurred pharmaceutical companies on to the development on other varieties of nonsteroidal anti-inflammatories.



Scleroderma is a rare, disabling, and sometimes fatal disease, resulting form an abnormal buildup of collagen in the body. The body swells, the skin--particularly on hands and face--becomes dense and leathery, and calcium deposits in joints cause difficulty of movement.



Fatigue and difficulty in breathing may ensue. Amputation of affected digits may be necessary. The cause of scleroderma is unknown, and, until DMSO arrived, there was no known effective treatment. Arthur Scherbel, MD, of the department of rheumatic diseases and pathology at the Cleveland Clinic Foundation, conducted a study using DMSO with 42 scleroderma patients who had already exhausted all other possible therapies without relief.



Scherbel and his coworkers concluded 26 of the 42 showed good or excellent improvement. Histotoxic changes were observed together with healing of ischemic ulcers on fingertips, relief from pain and stiffness, and an increase in strength.



The investigators noted, "It should be emphasized that these have never been observed with any other mode of therapy. It was inevitable that DMSO, with its pain-relieving, collagen-softening, and anti-inflammatory characteristics, would be employed against arthritis, and its use has been linked to arthritis as much as to any condition.



Yet the FDA has never given approval for this indication and has, in fact, turned down three Investigational New Drug IND applications to conduct extensive clinical trials. Moreover, its use for arthritis remains controversial.



Robert Bennett, MD, F. Jacob's university, says other drugs work better. Soluble surfactant proteins need to reconcile surfactant activity at the site of operation with the requirement for solubility and lack of aggregation during synthesis, storage, and transport stages.



Conventional small molecule detergents are amphiphilic and can form soluble aggregates micelles in solution that can readily dissociate to form surface monolayers when required.



This would be a difficult strategy for protein surfactants, since the large exposed hydrophobic surfaces required at interfaces would lead to significant solubility and aggregation problems in bulk solution.



The unusually high leucine content of latherin, atypical of soluble globular proteins, may be related to this proposed surfactant mechanism. A range of tissues was sampled from a horse, with mRNA prepared for detection of latherin transcripts by RT-PCR, and protein extracted for immunodetection using a rabbit antibody to recombinant latherin rlatherin.



As shown in Figure 4A, latherin transcripts were only detectable in skin and submaxillary salivary gland, and the protein was only detectable from skin, salivary gland, tongue and cheek Figure 4B.



In the case of the latter two sites, the tissue samples included epithelium, in which no transcripts were detected in separate experiments, so it is likely that the protein detected there was derived from contaminating saliva.



In a more limited screen, we found, as expected, that the gene for the major allergen of horses, Equ c 1, a lipocalin of unknown function though may be a pheromone carrier [36] — [38] , was also transcribed in skin and submaxillary gland tissue.



A RT-PCR using gene-specific oligonucleotide primers to detect latherin-encoding transcripts in a range of horse tissues; the ribosomal subunit protein S15 was used as a control.



B Immunoblot using latherin-specific antibody to detect latherin protein in tissue samples. C Immunoblot showing IgE antibody reactivity of serum from a horse-allergic patient binding to recombinant latherin rL and horse sweat S.



Five out of nine patients with detectable IgE antibody reactions to horse sweat exhibited IgE antibody to recombinant latherin. Sera from non-allergic individuals did not react to any components in horse sweat or the recombinant latherin.



R — reference proteins with M r expressed in kDa. D Immunoperoxidase labelling of a section of normal equine skin showing a dense dark band brown of staining proximal to the apical membrane of the sweat gland secretory epithelial cells; cell surface associated latherin is likely to have been lost during the preparation process.



Staining is also apparent in intracellular vesicles. E Immuno-fluorescent staining for latherin in equine sweat glands. Bright staining indicates the presence of latherin inside the secretory cells of the gland.



As mentioned above, the amino acid sequence of latherin encompasses two peptides that have previously been ascribed to the separately classified allergens Equ c 4 and Equ c 5 [16].



We obtained serum samples from eight horse-allergic patients and examined the antigen binding activity of their IgE antibody see Figure 4C for a typical result. This showed that patient IgE antibody bound to several components of horse sweat, the major band being at approximately M r 21,, which would correspond to the major allergen of horses, Equ c 1 which is also produced both in skin and saliva, [16] , [36] , [37].



The band at approximately M r 17, co-migrates with recombinant latherin rlatherin, which is also bound by the patients' IgE antibody. This immunoblot also shows the more rapid migration exhibited by latherin in SDS-PAGE than expected for its size, possibly due to its very high content of apolar amino acids and consequent more rapid migration caused by a high degree of binding by SDS detergent.



These biochemical and biophysical observations suggest the evolution of a dual role for latherin as both a sweat and a salivary protein. Its presence in equine sweat is consistent with a role in wetting hair and skin to allow rapid translocation and spreading of sweat water at the surface of the oily pelt for evaporative cooling.



Interestingly, human skin secretions are also thought to have a surfactant-like role in enhancing the spreading of sweat water for cooling, though by a mechanism suited to an effectively hairless surface [40] , [41].



The deposition of large quantities of protein through and over the pelt of horses would seem to present the risk of providing a nutrient resource for microorganisms. It could therefore be that latherin's surface activity may also directly affect the surfaces of microbes or impede their adhesion and establishment on hair and skin.



Latherin is distantly related to proteins that are directly anti-microbial [21] , but we have been unable to detect any interaction between latherin and archetypical bacterial components such as lipopolysaccharide not shown.



A function for latherin in horse saliva is less obvious, but the presence of a surfactant protein there may assist mastication and processing of large quantities of relatively dry vegetable matter, a diet for which the equids as a group are specialised, unlike ruminants cows, sheep, etc.



The possibility that latherin's surface-activity presents a danger to mammalian cells, however, needs to be addressed, as does the mechanism by which the intracellular membrane systems involved in synthesis, processing and export of the protein are protected from damage.



A simple small molecule detergent would normally be extremely damaging to cellular membranes, but it is possible that proteins can be designed to perform detergent-like functions without endangering cell membranes.



An example of this could be the strong surface activity of the proteinaceous foams in which certain tropical frogs lay their eggs, which may also have anti-microbial propensities, but are nonetheless compatible with naked eggs and spermatozoa [42] , [43].



It is possible that latherin is specially packaged by the synthesising cells before release, and our immunohistological observations on horse skin using anti-latherin antibody indicate that the protein is localised to the protein granules of the cells in the fundus region of the sweat gland, which are known to be exocytosed directly upon sweating [39].



At a more fundamental level, the mechanism by which small-molecule detergents solubilise lipid bilayer membranes is likely to be inapplicable to larger, surfactant proteins. Conventional synthetic detergents such as SDS, Triton, etc.



In contrast, although specific surfactant proteins do partition into the air-water interface [42] , their size and presumably structure precludes any equivalent of micelle formation in the bulk solution, therefore minimizing disruption of lipid bilayers.



There are now several different classes of protein that exhibit biologically relevant, intrinsic surface-activity, including latherin, the hydrophobins and frog foam nest foam proteins ranaspumins.



It would be valuable to know what structural characteristics separate or unify these proteins so as to extend our understanding of how proteins can do what they do. In the case of latherin, we are fortunate that it can be produced in soluble recombinant form in bacteria, and we have already obtained high quality protein NMR spectra as a preliminary to solving its solution structure R.



A structure for latherin may also improve our understanding of the PLUNC and BASE proteins, some of which may also possess intrinsic surface activity in order to operate in mucosal surfaces.



Meanwhile, in the absence of indications that PLUNC family members are produced in mammalian skin, latherin may represent a remarkable adaptation of a salivary protein for heat dissipation from skin by horses and their ilk, and a readily available protein with which to study intrinsic surface activity of a naturally folded protein from a mammal.



All tissue samples used in the study were collected from animals that died from, or were euthanised for, clinical causes entirely unconnected to the investigation, and with permission from the owners, and for which no formal ethical permission is required under UK Home Office regulations.



Sweat was collected from racehorses by gentle use of an equine sweat collector in Scotland under permission of the owners and Glasgow University's Veterinary Ethics and Welfare Committee and in Trinidad under permission from the owners and the Chief Veterinary Officer of the Republic of Trinidad and Tobago.



Sweat was collected from racehorses in Scotland and Trinidad. Natural latherin was purified from horse sweat and tryptic peptide fragments were sequenced as described previously [8].



Specifically, portions of reduced and carboxymethylated latherin were dissolved in 0. Substantial precipitation occurred in both enzymic digests, and the insoluble peptides were separated by centrifugation.



Peptide fractions were lyophilised repeatedly to remove ammonium bicarbonate. The soluble S peptides were dissolved in 0. Aliquots of the S and I peptide mixtures were fractionated by reversed phase chromatography on a silica-C8 reversed phase column Waters, Elstree, Hertfordshire, UK using a solvent gradient of increasing acetonitrile concentration containing 0.



Peptide fractions were pooled and aliquots hydrolysed and subjected to amino acid analysis [8]. Samples of peptides were sent for analysis by liquid phase automated Edman degradation at the Department of Biochemistry, University of Aberdeen.



This procedure provided cDNA sequence for horse latherin, and the encoded protein contained all the peptide sequences obtained from sweat-derived latherin Figure 1B and Table S1.



Similar procedures were used to obtain partial cDNA sequences from the other equid species, using additional primer sets designed to overlap those of the original primer positions to ensure that the final sequences were fully correct for each species.



The cultures were grown until an OD of 0. The thioredoxin tag was cleaved by overnight incubation with recombinant enterokinase Novagen, and the enzyme removed by passing through a column packed with EK Agarose Novagen.



The solution was diluted with binding buffer 20 mM Tris, 0. Skin samples were obtained from lateral neck skin of horses in the UK immediately after euthanasia for veterinary reasons not associated with skin complaints.



Four-micron sections of equine skin containing sweat glands were mounted on 3-aminopropyl-triethoxy-silane APES treated slides. Endogenous avidin and biotin sites were blocked using an Avidin Biotin Blocking kit Vector Laboratories, Orton Southgate, Peterborough, UK involving incubation with each blocker for 30 min.



Negative controls included omission of primary antibody. Enhanced chemiluminescence ECL reagents were used to detect specifically bound second layer antibodies according to the manufacturer's instructions.



Human sera from horse allergic and negative control subjects were obtained from an anonymous collection provided by Dr C. Immunoblotting membrane strips contained 0. Experiments were carried out at room temperature and the platinum ring cleaned between readings by rinsing with UHQ water and flaming to remove residual deposits.



Data were analyzed using standard MicroCal Origin instrumental software. Stern-Volmer quenching constants K SV were determined by linear regression according to the standard equation: Putative hydrophobic ligand binding in solution was probed by comparison of ANS ca.



The adsorption of recombinant latherin at the air-water interface was investigated by neutron reflection, as previously described for other surfactant protein systems [42] , [46].



Samples were prepared by dissolving lyophilized protein 0. As previously described [50] , [51] experimental neutron reflectivity profiles were analyzed by means of the optical matrix modelling formalism in which the calculated reflectivity of an assumed layer model was compared with the measured data.



The structural parameters were then varied by iteration in a least-squares procedure to give best fit. The choice of the number of sublayers in the model depended upon the extent of inhomogeneity across the interface, but a single-layer model was sufficient to fit the data adequately here.



Alignments of the four latherin sequences with the secondary structure predictions from SSPro 4. Adsorption of recombinant latherin onto a waxy surface. After a few minutes, each drop was carefully blotted off using a tip of absorbent paper towel.



The film was then stained for adsorbed protein by brief immersion in Coomassie Blue staining solution BioRad, followed by rinsing with water. Each stage was photographed by digital camera.



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The Crabbet Arabian Stud: Its History and Influence. Uses authors parameter link Barrie, Douglas M. The Roots of New World Horsemanship 1st ed. Retrieved December 3, Uses authors parameter link Bowling, A.



Outstanding Arabian Stallions and Mares. How the Horse Has Shaped Civilizations. Cyrino, Monica Silveira Derry, Margaret Elsinor Shorthorn Cattle, Collies, and Arabian Horses since





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Tojazil


Where there was no pasture or water, some travelers noticed that the Arabian horse as a pure breed of horse was under threat due to modern forms of warfare, Other names: Arabian, Arab.