Is collagenolytic activity present in the blood of ruminants?

Document Type : Original Research Article (Regular Paper)

Authors

Department of Animal Science, Shahrekord University, Shahrekord, Iran

Abstract

In the present study, collagenolytic activity was investigated in two separate experiments using blood plasma or serum. Two separate experiments were conducted at different times. The first experiment involved the analysis of blood plasma from 16 rams, 6 goat bucks, and 3 lactating cows. The rams and goat bucks were randomly divided into two equal heads groups (control and treated), and they did not exhibit any sexual problems. In the second experiment, twelve calves (5 males and 7 females) with a mean age 152 days, and weight of 128 kg, were selected and randomly divided into two groups. One group received a total mixed ration (TMR) plus a feed block (22 kg weight), while the other group received only TMR. Blood serum from all calves was utilized for collagenolytic activity. Bovine Achilles' tendon collagen served as the substrate for measuring collagenolytic activity, while hydroxyproline (HYP) was employed as a product for activity measurement. The results revealed the presence of the enzyme(s) in the blood samples of all the experimental animals, albeit at varying levels of activity. It was observed that the activity was significantly inhibited by cupric sulfate as a metal ion. Furthermore, notable positive and significant correlations were found between the daily gain of sheep and collagenolytic activity in blood samples, while negative correlations were observed between the age of the calves and collagenolytic activity. These results supported the hypothesis that enzyme activity is associated with growth. The results revealed the presence of the enzyme(s) in the blood samples of all the experimental animals, albeit at varying levels of activity. It was observed that the activity was significantly inhibited by cupric sulfate as a metal ion. Furthermore, notable positive and significant correlations were found between the daily gain of sheep and collagenolytic activity in blood samples, while negative correlations were observed between the age of the calves and collagenolytic activity. These results supported the hypothesis that enzyme activity is associated with growth.

Keywords

Main Subjects

References

References
 Almeida, A.M., Schwalbach, L.M.J., de Waal, H.O., Greyling, J.P.C., Cardoso, L.A., 2006. Plasma free amino acid profiles of Boer goat bucks as influenced by two feeding regimens. South African Journal of Animal Science 36,14-17.
Bannister, D.W., Burns, A.B., 1972. The presence of collagenolytic activity in avian serum. International Journal of Biochemistry 3, 216-224.
Bannister, D.W., Tylor, T.G. Burns, A.B., 1970. Changes with age in the level of plasma hydroxyproline in the domestic fowl. International Journal of Biochemistry 1,735-742.
Black, H.E., Capen, C.C., 1971. Urinary and plasma hydroxyproline during pregnancy, parturition and lactation in cows with parturient hypocalcemia. Metabolism 20, 337-344.
Canty, E.G., Kadler, K.E., 2005. Procollagen trafficking, processing and fibrillogenesis. Journal of Cell Science 118, 1341–1353.
Gries, G., Buresch, H., Strauch, L., 1970. Collagenolytic enzymes in human serum. Experientia 26, 31-33.
Izmirli, S. Aldavood, S.J., Yasar, A., Phillips, C.J.C., 2010. Introducing ethical evaluation of the use of animals in experiments in the near east. ATLA 38, 331-336.
Klein, L., 1964. Urinary hydroxyproline during late pregnancy and postpartum involution. Metabolism 13, 386-390.
Klein, L., Teree, T.M., 1966. Skeletal metabolism in early infancy: Urinary hydroxyproline. Journal of Pediatric 69, 266-273.
Lee, C.A., Lloyd, H.M., 1964. Urinary hydroxylproline in diseases involving bone and calcium metabolism. Medical Journal of Australia 27, 992-995.
Lenaers-Claeys, G., Vaes, G., 1979. Collagenase, procollagenase and bone resorption effects of heparin, parathyroid hormone and calcitonin. Biochemistry and Biophysics, Acta 584, 375-388.
National Research Council 2001. Nutrient Requirements of Dairy Cattle. 7th revised Ed. National Academy Press, Washington, USA.
National Research Council 2007. Nutrient Requirements of Small Ruminants: Sheep, Goats, Cervids and New World Camelids. 1st Ed. National Academy Press, Washington, USA.
Neuman, R.E., Logan, M.A., 1950. The determination of collagen and elastin in tissues. Journal of Biological Chemistry 186, 549-556.
Orgel, J.P., Irving, T.C., Miller, A., Wess, T.J., 2006. Microfibrillar structure of type I collagen in situ. Proceeding of National Academic Science. USA, 103, 9001–9005.
Pachence, J.M.,1996. Collagen-based devices for soft tissue repair. Journal of Biomedical Material Research 33, 35-40.
Patel, B.G., 2004. Extrusion and evaluation of degradation rate and porosity of small diameter collagen tubes. A MSc. Thesis. Biomedical Engineering Department. New Jersey Institute of Technology.
Prockop. D.J., Kivirikkov, K.I., 1967. Relationship of hydroxyproline excretion in urine to collagen metabolism. Annual International Medicine 66,1243-1266.
Rajabi, M., Solomon, S., Poole, A.R.,1991. Biochemical evidence of collagenase-mediated collagenolysis as a mechanism of cervical dilatation at parturition in the guinea pig. Biology of Reproduction 45, 764-772.
Ramachandran, G.N., Kartha, G., 1955. Structure of collagen. Nature 176, 593–595.
 
Rosenblum, G., Van den Steen, P.E., Cohen, S.R., Bitler, A., Brand, D.D., 2010. Direct visualization of protease action on collagen triple helical structure. PLoS ONE 5(6), e11043. doi:10.1371/journal.pone.0011043
Rosol, T.J., Capen, C.C., 1997. Calcium-Regulating Hormones and Diseases of Abnormal Mineral (Calcium, Phosphorus, Magnesium) Metabolism. In: J. Jerry Kaneko John W. Harvey. Michael L. Bruss. Clinical Biochemistry of Domestic Animals. 5th Ed. Academic Press, P. 619-702.
Seifter, S., Takahashi, S., Warper, E., 1970. Further demonstration that cysteine reacts with the metal component of collagenase. Biochemistry and Biophysics Acta 214, 559-561.
Siddiqi, N.J., Alhomida, A.S., 2000. A study of the distribution of total, free, peptide-bound and protein bound hydroxyproline in the plasma of Arabian camel (Camelus dromedarius). Comparative Haematology International 10,144–147.
Siddiqi, N.J., Al-Jafari, A.A., Alhomida, A.S., 2000. Investigation of total, free, peptide-bound, protein-bound, soluble and insoluble collagen hydroxyproline content in tissues from the Arabian camel (Camelus dromedarius). Cell Biochemistry Function 18,243-248.
Starcher, B.C., Hill, C.H., Madaras, J.G., 1980. Effect of zinc deficiency on bone collagenase and collagen turnover. Journal of Nutrition 110, 2095-2102.
Stegmann, H., Stalder, K., 1967. Determination of hydroxyproline. Clinical Chemical Acta 18, 267-273.
 
Journal of Livestock Science and Technologies
Volume 11, Issue 2
December 2023
Pages 25-32

Files

Share

How to cite

Statistics