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Topic:Proteolysis

Proteolysis in horses refers to the breakdown of proteins into smaller polypeptides or amino acids, a process facilitated by enzymes known as proteases. This biochemical process is essential for various physiological functions, including digestion, cellular repair, and the regulation of metabolic pathways. In horses, proteolysis is involved in muscle turnover, tissue remodeling, and the response to injury or disease. The regulation of proteolytic activity is complex and involves multiple enzymes and inhibitors to maintain homeostasis. Aberrations in proteolysis can be associated with pathological conditions, such as muscle wasting or inflammatory diseases. This page compiles peer-reviewed research studies and scholarly articles that explore the mechanisms, regulation, and implications of proteolysis in equine physiology and health.
Markers of muscle atrophy and impact of treatment with pergolide in horses with pituitary pars intermedia dysfunction and muscle atrophy.
Domestic animal endocrinology    February 18, 2021   Volume 76 106620 doi: 10.1016/j.domaniend.2021.106620
Banse HE, Whitehead AE, McFarlane D, Chelikani PK.Pituitary pars intermedia dysfunction (PPID) is a common endocrine disorder of aged horses, with muscle atrophy as one of the clinical signs. We sought to compare muscle mass and regulation of skeletal muscle proteolysis between horses with PPID and muscle atrophy to older horses without PPID, and to assess the impact of treatment with pergolide (dopaminergic agonist) on PPID horses. We hypothesized that PPID-associated muscle atrophy is a result of increased proteolysis, and that markers of muscle atrophy and proteolysis would improve over time with pergolide treatment. Markers of muscle atro...
Detection of peginesatide in equine serum using liquid chromatography-tandem mass spectrometry for doping control purposes.
European journal of mass spectrometry (Chichester, England)    September 14, 2012   Volume 18, Issue 4 407-412 doi: 10.1255/ejms.1189
Möller I, Thomas A, Wingender A, Machnik M, Schänzer W, Thevis M.Erythropoietin (EPO) and its recombinant analogues are suspected to be illicitly administered to horses for performance enhancing purposes and, consequently, prohibited in equine sports. Recently, a new erythropoiesis-stimulating agent, peginesatide (Omontys, formerly referred to as Hematide), belonging to the upcoming class of EPO-mimetic peptides, received approval for the treatment of anaemia in humans with chronic kidney disease on dialysis. As the pegylated dimeric peptide of approximately 45 kDa without sequence homology to EPO is not detectable by conventional EPO detection assays, spec...
The role of activated neutrophils in the early stage of equine laminitis.
Veterinary journal (London, England : 1997)    July 23, 2010   Volume 189, Issue 1 27-33 doi: 10.1016/j.tvjl.2010.06.008
de la Rebière de Pouyade G, Serteyn D.Despite ongoing research and a widening range of treatment options, laminitis remains a severely damaging condition with poorly understood pathophysiology. Results obtained from cytokine regulation studies during the last decade have highlighted the inflammatory nature of laminitis. This review will describe the role of systemic activation and local infiltration of neutrophils in laminar tissues in the induction of laminitis. Particular emphasis is placed on the role of neutrophil activation in subsequent vascular dysfunction and oxidative and proteolysis imbalances that are pathways previousl...
Gene expression of proteolytic systems and growth regulators of skeletal muscle in horses with myopathy associated with pituitary pars intermedia dysfunction.
American journal of veterinary research    June 2, 2010   Volume 71, Issue 6 664-670 doi: 10.2460/ajvr.71.6.664
Aleman M, Nieto JE.To investigate gene expression of the major proteolytic systems and growth regulators in skeletal muscle of horses with myopathy associated with pituitary pars intermedia dysfunction (PPID). Methods: 14 horses with PPID-associated myopathy and 7 healthy control horses. Methods: Horses with PPID and controls were age matched (15 to 28 years old). Muscle biopsy specimens were collected from both groups and processed for RNA and cDNA extraction. Validation of the most stable housekeeping genes for skeletal muscle was performed and used to compare gene expression of the following proteolytic syste...
Protective effect of magnesium and potassium ions on the permeability of the external mitochondrial membrane.
Archives of biochemistry and biophysics    January 29, 2007   Volume 461, Issue 1 13-23 doi: 10.1016/j.abb.2007.01.007
Gorgoglione V, Laraspata D, La Piana G, Marzulli D, Lofrumento NE.The data reported are fully consistent with the well-known observation that exogenous cytochrome c (cyto-c) molecules do not permeate through the outer membrane of mitochondria (MOM) incubated in isotonic medium (250 mM sucrose). Cyto-c is unable to accept electrons from the sulfite/cyto-c oxido-reductase (Sox) present in the intermembrane space, unless mitochondria are solubilized. Mitochondria incubated in a very high hypotonic medium (25 mM sucrose), in contrast to any expectation, continue to be not permeable to added cyto-c even if Sox and adenylate kinase are released into the medium. Th...
Profiles of matrix metalloproteinase activity in equine tear fluid during corneal healing in 10 horses with ulcerative keratitis.
Veterinary ophthalmology    October 30, 2004   Volume 7, Issue 6 397-405 doi: 10.1111/j.1463-5224.2004.04052.x
Ollivier FJ, Brooks DE, Van Setten GB, Schultz GS, Gelatt KN, Stevens GR, Blalock TD, Andrew SE, Komaromy AM, Lassaline ME, Kallberg ME, Cutler TJ.Levels of tear film matrix metalloproteinases (MMPs) activity are significantly elevated in horses with ulcerative keratitis and contribute to the excessive breakdown of stromal collagen. Changes in the amount of proteolytic activity in horse tear film during corneal healing and stromal remodeling have not yet been reported, but we hypothesize they should decrease. In the present study we analyzed serial tear fluid from horses with ulcerative keratitis to identify any changes in MMP activity during corneal healing and stromal remodeling. Methods: Samples of tear fluid were obtained from both e...
Budding of equine infectious anemia virus is insensitive to proteasome inhibitors.
Journal of virology    February 28, 2002   Volume 76, Issue 6 2641-2647 doi: 10.1128/jvi.76.6.2641-2647.2002
Patnaik A, Chau V, Li F, Montelaro RC, Wills JW.The only retrovirus protein required for the budding of virus-like particles is the Gag protein; however, recent studies of Rous sarcoma virus (RSV) and human immunodeficiency virus have suggested that modification of Gag with ubiquitin (Ub) is also required. As a consequence, the release of these viruses is reduced in the presence of proteasome inhibitors, which indirectly reduce the levels of free Ub within the cell. Here we show that the budding of equine infectious anemia virus (EIAV) from infected equine cells is largely unaffected by these drugs, although use of one inhibitor (MG-132) re...
Preliminary characterisation of extracellular serine proteases of Dermatophilus congolensis isolates from cattle, sheep and horses.
Veterinary microbiology    October 29, 1998   Volume 62, Issue 4 321-335 doi: 10.1016/s0378-1135(98)00223-5
Ambrose NC, Mijinyawa MS, Hermoso de Mendoza J.Dermatophilus congolensis is a filamentous branching actinomycete that causes dermatophilosis, an exudative dermatitis in ruminants. The pathogenesis of this disease is poorly understood and virulence factors of D. congolensis have not been characterised. Culture filtrate (CF) of 14 D. congolensis isolates from cattle, 15 from sheep and four from horses were examined for proteolytic activity using azocasein as a non-specific substrate. The isolates were from a variety of geographical locations. All the isolates examined produced extracellular proteolytic activity. CF from 24 and 48 h cultures ...
The comparison of pepsin and trypsin action on goat, cow, mare and human caseins.
Roczniki Akademii Medycznej w Bialymstoku (1995)    January 1, 1995   Volume 40, Issue 3 486-493 
Jasińska B.The degree of proteolysis of micellar caseins of human, goat's, mare's and two breeds (Black&White and Red Polish) of cow's milk was compared for pepsin and trypsin action in vitro. Human and goat's caseins were hydrolysed in 100% and 96%, respectively, mare's casein--92%, Black&White cow's casein--90%, Red Polish cow's casein--76%. The differences can be related to the micelle structure, especially to the prevalence of beta casein in the human and goat's casein. The significant dissimilarity between the two breeds of investigated cows is surprising and indicates a different geometry o...
Decrease in the alpha 1-proteinase inhibitor Spi3 in equine bronchoalveolar lavage fluid.
American journal of veterinary research    October 1, 1994   Volume 55, Issue 10 1377-1380 
Milne EM, Pemberton AD, Dixon PM, McGorum BC, Scudamore CL, Miller HR.The alpha 1-proteinase inhibitors of trypsin, Spi1, Spi3A, and Spi3B, in bronchoalveolar lavage fluid (BALF) and serum of horses were separated by electrophoresis, and their proportions were quantified in 12 control horses and 12 with chronic obstructive pulmonary disease (COPD). A significantly lower proportion of Spi3B (P < 0.05) and higher proportion of Spi1 (P < 0.02 to P < 0.01) were detected in BALF, compared with serum, in control and COPD-affected horses and appeared to be attributable to reduced Spi3 activity in BALF. There was no significant difference between the control an...
Proteolysis and antiproteolysis–a delicate balance.
Equine veterinary journal    March 1, 1994   Volume 26, Issue 2 89-90 doi: 10.1111/j.2042-3306.1994.tb04341.x
Matthews AG.No abstract available
Studies on prolactin: conformational comparison of human, equine, and porcine pituitary prolactins.
Archives of biochemistry and biophysics    December 1, 1983   Volume 227, Issue 2 618-625 doi: 10.1016/0003-9861(83)90491-5
Bewley TA, Li CH.The conformations of human, equine, and porcine pituitary prolactins, as evidenced by various optical properties, have been compared. The alpha-helix contents of all three proteins are essentially identical to each other (60 +/- 5%), as well as to prolactins isolated from other mammalian species. Direct absorption (zero and second-order), difference absorption, fluorescence emission, and circular dichroism spectra suggest that the majority of tyrosine and tryptophan side chains in these three proteins exist in very similar microenvironments within the folded forms of the hormones. Thus, the ge...
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 ...
Changes in the activity of proteolytic enzymes and transaminases (G.O.T., G.P.T.) in horse leucocytes during hyperimmunization.
Archives roumaines de pathologie experimentales et de microbiologie    December 1, 1966   Volume 25, Issue 4 971-978 
Ségli G, Toma E, Oprişan R.No abstract available