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Topic:Peptides

Peptides are short chains of amino acids that are involved in various biological processes in horses. They function as signaling molecules, influencing physiological activities such as metabolism, immune response, and tissue repair. Peptides can be naturally occurring or synthetically derived, and they may serve as therapeutic agents in veterinary medicine. In equine health, peptides are studied for their potential applications in enhancing performance, supporting recovery, and managing conditions like osteoarthritis. This page compiles peer-reviewed research studies and scholarly articles that explore the structure, function, and potential applications of peptides in the context of equine health and disease management.
The regulatory peptide system of the large bowel in equine grass sickness.
Experientia    August 15, 1984   Volume 40, Issue 8 801-806 doi: 10.1007/BF01951962
Bishop AE, Hodson NP, Major JH, Probert L, Yeats J, Edwards GB, Wright JA, Bloom SR, Polak JM.In recent years, distinct changes in regulatory peptides have been found in a number of gastrointestinal diseases. Grass sickness is a fatal disease of horses for which the etiology has yet to be fully ascertained. In this study, the peptide-containing nerves and ganglionic and mucosal endocrine cells of the ileum, colon and rectum were investigated in horses with sub-acute or chronic grass sickness and compared with normal controls using immunocytochemistry, at both the light and electron microscopical levels, and radioimmunoassay. A substantial loss of both peptide-containing cells and nerve...
Antigenic reactivity of the major glycoprotein of equine infectious anemia virus, a retrovirus.
Virology    July 30, 1984   Volume 136, Issue 2 368-374 doi: 10.1016/0042-6822(84)90173-9
Montelaro RC, West M, Issel CJ.The immunogenic contributions of the carbohydrate and peptide portions of the major envelope glycoprotein of equine infections anemia virus, EIAV gp90, were analyzed by measuring the effects of specific glycosidase and protease digestions on the reactivity of the glycoprotein with immune sera from infected horses. The results of both direct and competitive radioimmunoassay demonstrated that immune sera contained antibodies reactive with both the carbohydrate and protein moieties of EIAV gp90, with the predominant reactivity apparently against the gp90 peptide epitopes. These results contrast w...
The distribution and origin of a novel brain peptide, neuropeptide Y, in the spinal cord of several mammals.
The Journal of comparative neurology    July 20, 1984   Volume 227, Issue 1 78-91 doi: 10.1002/cne.902270109
Gibson SJ, Polak JM, Allen JM, Adrian TE, Kelly JS, Bloom SR.The distribution of neuropeptide Y [NPY]-immunoreactive material was examined in the spinal cord and dorsal root ganglia of rat, guinea-pig, cat, marmoset, and horse. Considerable concentrations of NPY and similar distribution patterns of immunoreactive nerve fibres were found in the spinal cord of all species investigated. The dorsal root ganglia of the cat and the horse contained numerous immunoreactive nerve fibres, but in these species, as in the other three studied [rat, guinea-pig, marmoset], no positively stained cell bodies were found. Neuropeptide Y-immunoreactive nerves were observed...
[Multiple forms of horse pepsin].
Biokhimiia (Moscow, Russia)    June 1, 1984   Volume 49, Issue 6 1026-1037 
Gonchar MV, Lavrenova GI, Rudenskaia GN, Gaĭda AV, Stepanov VM.Using ion-exchange and affinity chromatography and isoelectrofocusing, eight forms of pepsin with pI 1.6, 1.8, 2.1, 2.3, 2.6, 2.8, 3.2 and 3.6, were isolated from horse gastric juice. The molecular weights, amino acid composition, N-terminal sequence and functional activity of these multiple forms were determined. Partial primary structure of tryptic peptides of pepsin with pI 2.3 was investigated. The analyzed partial sequences of the forms with pI 1.8, 2.1, 2.3, and 2.6 have identical structures which differ from the amino acid sequence of pepsin with pI 3.2 by four substituents. In terms of...
Immunocytochemical distribution of endocrine cells in the gastrointestinal tract of the horse.
Equine veterinary journal    March 1, 1984   Volume 16, Issue 2 103-107 doi: 10.1111/j.2042-3306.1984.tb01870.x
Kitamura N, Yamada J, Calingasan NY, Yamashita T.Endocrine cells immunoreactive for somatostatin, gastrin, glicentin, glucagon, secretin, cholecystokinin, motilin and neurotensin were identified immunocytochemically in the gastrointestinal mucosa of the horse. Somatostatin-, glicentin- and glucagon-immunoreactive cells were very numerous in the cardiac and fundic regions of the stomach, whereas most gastrin-immunoreactive cells were confined to the pyloric region. Somatostatin-immunoreactive cells also were detected in all portions of the small intestine while gastrin-immunoreactive cells were confined exclusively to the upper portion and gl...
The relationship between alpha-MSH level and coat color in white Camarque horses.
The Journal of investigative dermatology    February 1, 1984   Volume 82, Issue 2 199-201 doi: 10.1111/1523-1747.ep12259846
Altmeyer P, Holzmann H, Stöhr L, Koch HJ.White horses are subject to age-dependent coat depigmentation. They are dark gray or black at birth and lose their coloring between their second and fourth year. Beginning at about age 10 their coat takes on a characteristic silver-gray coloring. The purpose of this paper was to find out to what extent the endogenic alpha-MSH level changes with the change in pigmentation. alpha-MSH plasma levels were determined by radioimmunologic analysis in 3 age groups of white Camarque horses: age group 1 consisted of dark horses with a mean age of 1.2 years and a mean alpha-MSH level of 106.4 pg/ml +/- 18...
Radioimmunological measurement of beta-endorphin in equine plasma. Bossut DF, Leshin LS, Malven PV.Radioimmunoassay procedures were developed and validated for the quantification of beta-endorphin (beta-EP)-like immunoreactivity in equine plasma. beta-EP could be quantitatively extracted from plasma with silicic acid powder and subsequently assayed, however, valid estimates of this hormone could also be obtained on unextracted plasma. Although beta-lipotropin (beta-LPH) cross-reacted in the assay, it was not necessary to correct for beta-LPH activity when assaying unextracted plasma because chromatographic analyses showed that 92% of the immunoreactivity in plasma extracts was similar in mo...
Synthesis and properties of equine beta-melanotropin analogs with substitution in residue position 1.
International journal of peptide and protein research    April 1, 1983   Volume 21, Issue 4 364-368 doi: 10.1111/j.1399-3011.1983.tb03116.x
Nádasdi L, Yamashiro D, Li CH, Izdebski J.Five analogs of equine β-melanotropin have been synthesized by the solid phase method. The NH2-terminal aspartic acid was substituted with amino acids (Gly, Trp, Ile, Lys and Nα-acetyl-Asp) differing widely in physicochemical properties. On the basis of their lipolytic potencies it was concluded that this position plays a negligible role in this activity.
Specific fragmentation of natural inhibitor of mitochondrial ATPase by thrombin.
Biochemical and biophysical research communications    July 30, 1982   Volume 107, Issue 2 435-441 doi: 10.1016/0006-291x(82)91510-8
Dianoux AC, Freyssinet JM.No abstract available
Changes in circulating gut hormones in the horse during long distance exercise.
Equine veterinary journal    July 1, 1982   Volume 14, Issue 3 209-212 doi: 10.1111/j.2042-3306.1982.tb02395.x
Hall GM, Adrian TE, Bloom SR, Lucke JN.Venous blood samples were collected before and immediately after an 80 km ride and a 42 km race. They were analysed for blood glucose and lactate, and for plasma non-esterified fatty acids, insulin, pancreatic glucagon, pancreatic polypeptide, gastrin, gastric inhibitory peptide, somatostatin and vasoactive intestinal polypeptide concentrations. The 80 km ride was associated with marked hypoglycaemia and a slight lactic acidaemia together with an increase in plasma glucagon, somatostatin, pancreatic polypeptide and vasoactive intestinal polypeptide values. The 42 km race produced hyperglycaemi...
Equine Cushing’s disease: plasma immunoreactive proopiolipomelanocortin peptide and cortisol levels basally and in response to diagnostic tests.
Endocrinology    April 1, 1982   Volume 110, Issue 4 1430-1441 doi: 10.1210/endo-110-4-1430
Orth DN, Holscher MA, Wilson MG, Nicholson WE, Plue RE, Mount CD.No abstract available
Synthesis and properties of equine beta-melanotropin and its naturally occurring des-Asp analog.
International journal of peptide and protein research    April 1, 1982   Volume 19, Issue 4 327-333 doi: 10.1111/j.1399-3011.1982.tb02611.x
Izdebski J, Yamashiro D, Ng TB, Li CH.No abstract available
Chemotaxis of horse polymorphonuclear leukocytes to N-formyl-L-methionyl-L-leucyl-L-phenylalanine.
American journal of veterinary research    April 1, 1982   Volume 43, Issue 4 613-616 
Zinkl JG, Brown PD.Horse polymorphonuclear leukocytes (PMN) isolated from horse blood by sedimentation and isotonic lysis and having about 25% accompanying lymphocytes were as effective at chemotaxis as nearly pure PMN isolated by density gradient techniques. N-Formyl-L-methionyl-L-leucyl-L-phenylalanine (FMLP), used as a representative of the formylmethionyl peptides (produced by prokaryocytic organisms), was effective as a chemoattractant only at the high concentration of 10(-4) M. When serum was preincubated with FMLP at concentrations as low as 10(-8) M, the serum attracted horse PMN. This activity was not g...
Grass sickness of horses: changes in the regulatory peptide system of the bowel.
The Veterinary record    March 20, 1982   Volume 110, Issue 12 276 doi: 10.1136/vr.110.12.276
Hodson N, Edwards GB, Barnett SW, Bishop AE, Cole GA, Probert L, Bloom SR, Polak JM.No abstract available
Proopiolipomelanocortin peptides in normal pituitary, pituitary tumor, and plasma of normal and Cushing’s horses.
Endocrinology    March 1, 1982   Volume 110, Issue 3 941-954 doi: 10.1210/endo-110-3-941
Wilson MG, Nicholson WE, Holscher MA, Sherrell BJ, Mount CD, Orth DN.Using RIAs for six regions within proopiolipomelanocortin (proOLMC), gel filtration, and electrophoresis, we studied pituitary peptides in a normal horse and one with Cushing's disease caused by a pars intermedia adenoma. Almost all immunoreactive (IR) ACTH (78%) was 4,500 mol wt (4.5K) ACTH in normal pars distalis, but it was almost 100% corticotropin-like intermediate lobe peptide (CLIP) in normal pars intermedia. alpha MSH and beta MSH were found mainly in pars intermedia: equal concentrations of the beta MSH precursors, beta-lipotropin (beta LPH) and gamma LPH, were found in pars distalis....
Limited trypsinolysis of porcine and equine colipases. Spectroscopic and kinetic studies.
Biochimica et biophysica acta    December 29, 1981   Volume 671, Issue 2 155-163 doi: 10.1016/0005-2795(81)90129-x
Rathelot J, Canioni P, Bosc-Bierne I, Sarda L, Kamoun A, Kaptein R, Cozzone PJ.Porcine and equine colipases have been submitted to mild tryptic digestion. Proteolysis occurs at the Arg5-Gly6 bond with the loss of the N-terminal pentapeptide. Studies of native and trypsin-treated colipases by circular dichroism and laser chemically induced dynamic nuclear polarization indicate that proteolysis induces conformational changes in the region of the tyrosine cluster. Experiments in the presence of phospholipid provide further evidence showing that these residues are in or close to the region of the protein interacting with aggregated lipids. Kinetic studies of the reaction of ...
Isolation and properties of beta-endorphin-(1-27), N alpha-acetyl-beta-endorphin, corticotropin, gamma-lipotropin and neurophysin from equine pituitary glands.
International journal of peptide and protein research    November 1, 1981   Volume 18, Issue 5 443-450 doi: 10.1111/j.1399-3011.1981.tb03005.x
Ng TB, Chung D, Li CH.No abstract available
Primary structure of 3-phosphoglycerate kinase from horse muscle. I. Purification of cyanogen bromide peptides and amino acid sequence of peptide CB5 (104 residues).
The Journal of biological chemistry    October 25, 1981   Volume 256, Issue 20 10284-10292 
Hardy GW, Darbre A, Merrett M.3-Phosphoglycerate kinase was isolated from horse muscle and subjected to the action of cyanogen bromide. The resulting peptides were separated using gel filtration combined with either ion exchange chromatography on phosphocellulose in 6 M urea or high voltage paper electrophoresis. The sequence of the largest peptide, CB5, has been determined by a combination of automated and manual Edman degradation carried out on the intact peptide and derivatives obtained by proteolytic digestion. The isolation of two peptides derived from CB5 by cleavage of the bond between Asp109 and Pro110 facilitated ...
Antigenic and structural conservation of herpesvirus DNA-binding proteins.
The Journal of general virology    October 1, 1981   Volume 56, Issue Pt 2 409-419 doi: 10.1099/0022-1317-56-2-409
Littler E, Yeo J, Killington RA, Purifoy DJ, Powell KL.Previously, we have shown a common antigen of several herpesviruses (pseudorabies virus, equine abortion virus and bovine mammillitis virus) to be antigenically related to the major DNA-binding proteins of herpes simplex virus types 1 and 2. In this study we have purified the cross-reacting polypeptide from cells infected with pseudorabies virus, equine abortion virus and bovine mammillitis virus and shown the cross-reacting protein to be a major DNA-binding protein for each virus. Tryptic peptide analysis of the cross-reacting DNA-binding proteins of all five viruses has shown structural simi...
beta-Endorphin: isolation, amino acid sequence and synthesis of the hormone from horse pituitary glands.
International journal of peptide and protein research    September 1, 1981   Volume 18, Issue 3 242-248 doi: 10.1111/j.1399-3011.1981.tb02978.x
Li CH, Ng TB, Yamashiro D, Chung D, Hammonds RG, Tseng LF.Beta-endorphin has been isolated from equine pituitaries. Its amino acid sequence is identical to that of ovine, bovine and camel beta-endorphins except for substitution of the threonine residue at position 6 by serine. The equine beta-endorphin has also been synthesized by the solid-phase method. In comparison with the human hormone, equine beta-endorphin was shown to possess 3 times the receptor-binding activity in rat membrane preparations and 1.6 times the analgesic potency in the mouse tail-flick assay.
Amino acid sequence of horse colipase B.
Biochimica et biophysica acta    June 29, 1981   Volume 669, Issue 1 39-45 doi: 10.1016/0005-2795(81)90221-x
Bonicel J, Couchoud P, Foglizzo E, Desnuelle P, Chapus C.The complete sequence of the 96 residues composing horse colipase B has been determined by automated analysis of the intact protein, of two CNBr peptides and two tryptic peptides arising, respectively, from the citraconylated chain and from the unreduced protein. The single histidine of the protein is located at position 29 as in horse colipase A. His86, present in the C-terminal region of the pig cofactor and supposed to play a role in the folding molecule, is not conserved in horse B. Large pieces of the pig and horse B chains were found to be identical or very similar, especially the N-term...
Stabilization of the C-terminal part of pig and horse colipase by carboxypeptidase and trypsin inhibitors.
European journal of biochemistry    March 16, 1981   Volume 115, Issue 1 99-105 doi: 10.1111/j.1432-1033.1981.tb06203.x
Chapus C, Desnuelle P, Foglizzo E.Pig and horse colipases have been purified by a common procedure using trypsin and carboxypeptidase inhibitors as stabilizers. Two forms of pig colipase were identified: a predominant A1 form with about 103-105 residues, and a minor slightly degraded A2 form in which the last two C-terminal residues, Asp and Ser, were lacking. This type of degradation is considerably slowed down by carboxypeptidase inhibitors. A total of four forms of the horse cofactor were characterized: two (A1 and B1) were probably isocolipases which differed by only a few substitutions. Both contained the same number of r...
GnRH localization in the equine brain and infundibulum: an immunohistochemical study.
Brain research    March 9, 1981   Volume 208, Issue 1 123-134 doi: 10.1016/0006-8993(81)90625-9
Dees WL, Sorensen AM, Kemp WM, McArthur NH.Immunohistochemical localization of the decapeptide gonadotropin releasing hormone (GnRH) in neural structures in the pony brain and infundibulum (INF) was conducted at the light-microscopic level. This procedure utilized an antiserum generated against GnRH conjugated to bovine serum albumin. In the rostral INF, GnRH was distributed mainly in the external layer, with greatest concentrations adjacent to the long capillary loops of the hypophyseal portal system. The intermediate portion of the INF contained the hormone throughout the external layer, especially in the dorsolateral regions just ve...
The cleavage of the Met-Lys bond in a bradykinin derivative by glandular kallikreins.
Hoppe-Seyler's Zeitschrift fur physiologische Chemie    March 1, 1981   Volume 362, Issue 3 337-345 doi: 10.1515/bchm2.1981.362.1.337
Araujo-Viel MS, Juliano L, Prado ES.The synthetic tridecapeptide Gly-Leu-Met-Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg was used as a model substrate for horse urinary and porcine pancreatic kallikreins. The Met-Lys bond is hydrolyzed selectively by both enzymes. Oxidation of the methionine residue to sulfoxide made the peptide resistant to both kallikreins. Substitution of either the methionine or lysine residues by norleucine led to peptides in which the Nle-Lys or the Met-Nle bonds, respectively, were susceptible to the urinary kallikrein. The esterolytic and Met-Lys bond-splitting activities of both enzymes were inhibited simil...
Isolation and characterization of a new beta-melanotropin from horse pituitary glands.
Biochemical and biophysical research communications    February 12, 1981   Volume 98, Issue 3 621-627 doi: 10.1016/0006-291x(81)91159-1
Ng TB, Oosthuizen MM, Chung D, Li CH.No abstract available
Equine infectious anemia virus, a putative lentivirus, contains polypeptides analogous to prototype-C oncornaviruses.
Virology    December 1, 1980   Volume 107, Issue 2 520-525 doi: 10.1016/0042-6822(80)90319-0
Parekh B, Issel CJ, Montelaro RC.No abstract available
Occurrence of Leu-Lys-bradykinin and histidine-rich peptide in high-molecular-weight kininogen isolated from horse plasma.
Biochimica et biophysica acta    August 28, 1979   Volume 579, Issue 2 474-478 doi: 10.1016/0005-2795(79)90076-x
Sugo T, Kato H, Iwanaga S, Fujii S.On incubation of purified horse plasma high-molecular-weight kininogen with purified plasma kallikrein, three new peptides, named fragment 1.2, fragment 1 and fragment 2, were released, in addition to the vasopeptide, bradykinin. Fragment 2 contained an extremely high level of histidine, in which eleven residues out of the total 48 residues were characterized. Thus the result proves the existence of the histidine-rich region in horse high-molecular-weight kininogen, which is similar to the region previously identified in bovine high-molecular-weight kininogen. Moreover, we have identified a ne...
Specificity of response to viral proteins in horses infected with equine infectious anemia virus.
Infection and immunity    February 1, 1979   Volume 23, Issue 2 472-478 doi: 10.1128/iai.23.2.472-478.1979
Charman H, Long C, Coggins L.Three structural proteins of equine infectious anemia virus were purified, labeled with 125I, and utilized in radioimmunoassays with horse sera and antisera to heterologous retroviruses. Whereas radioimmunoassay titers for the major protein, p25, were 500- to 1,000-fold higher than titers in immunodiffusion, for clinical purposes these two procedures were equivalent. Antibodies to two low-molecular-weight proteins, p12 and p10, were also found in infected horses, but with a lower frequency and lower titers. As a rule, only sera positive for p25 also contained antibody to p12 and p10. Antisera ...
Lymphocyte specificity to protein antigens. II. Fine specificity of T-cell activation with cytochrome c and derived peptides as antigenic probes.
The Journal of experimental medicine    February 1, 1979   Volume 149, Issue 2 436-447 doi: 10.1084/jem.149.2.436
Corradin G, Chiller JM.Murine T-lymphocyte specificity was determined in a system of antigen driven in vitro T-cell proliferation using cytochrome c molecules from different species, their derived peptides and reconstituted hybrid proteins. It was observed that primed T cells could discriminate between peptide fragments which differed from each other at a single amino acid residue. These conclusions were substantiated by the pattern of cross-reactivity noted in the response of closely related cytochrome c proteins as well as when artificial hybrid molecules reconstituted by the covalent linkage of peptide fragments ...
Hemoglobin polymorphism in Equus przewalskii and E. caballus analyzed by isoelectric focusing.
Comparative biochemistry and physiology. B, Comparative biochemistry    January 1, 1979   Volume 62, Issue 4 305-308 doi: 10.1016/0305-0491(79)90093-2
Ryder OA, Sparkes RS, Sparkes MC, Clegg JB.1. Through the use of isoelectric focusing and peptide analysis, the hemoglobins of Przewalski's horse. Equus przewalskii and the domestic horse, E. caballus have been compared. 2. Przewalski's horses have two separate alpha-globin chain polymorphisms similar to domestic horses. Each hemoglobin phenotype could be accurately determined by isoelectric focusing. 3. Confirmation of the electrofocusing hemoglobin determinations was made by comparison to amino acid composition analyses of purified tryptic peptides and by analysis of the rare hemoglobins phenotypes observed in a family of Norwegian t...