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Investigation into the Distribution of Total, Free, Peptide-bound, Protein-bound, Soluble-and Insoluble-Collagen Hydroxyproline in Various Bovine Tissues

  • Siddiqi, Nikhat J. (Department of Biochemistry, King Saud University, College of Science) ;
  • Alhomida, Abdullah S. (Department of Biochemistry, King Saud University, College of Science)
  • 발행 : 2003.03.31

초록

Collagen is a family of proteins which consists of several genetically distinct molecular species and is intimately involved in tissue organization, function, differentiation and development. The purpose of this study was to investigate the concentration of different hydroxyproline (Hyp) fractions viz., total, free, peptide-bound, protein-bound, soluble- and insoluble-collagen hydroxyproline (Hyp) in various bovine tissues. Results showed that liver had the highest concentration of free Hyp followed by kidney, brain, spleen, lungs, muscle and heart. Liver also had the highest concentration of peptide-bound collagen Hyp followed by kidney, heart, spleen, lungs, brain and muscle. The concentration of protein-bound collagen Hyp was highest in the liver, followed by kidney, spleen, lungs, muscle, brain and heart. Total Hyp was highest in the liver, followed by kidney, spleen, brain, heart, muscle and lungs. Liver also had significantly high concentration of collagen as compared to other tissues examined (P<0.001). Spleen had the significantly higher concentration of soluble-collagen Hyp when compared to other tissues (P<0.001). This was followed by heart, muscle, lungs, brain, kidney and liver. Heart had the highest concentration of insoluble-collagen Hyp followed by lungs, kidney, liver, muscle, spleen and brain. The variation among the insoluble-collagen Hyp concentration of heart and muscle, spleen and brain was significant (P<0.001). We speculate that these differences could be due to the variation in turn over of rate of collagen metabolism in this species.

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참고문헌

  1. Adams, E. and Frank, L. (1980) Metabolism of proline and the hydroxyprolines. Annu. Rev. Biochem. 49, 1005-1061. https://doi.org/10.1146/annurev.bi.49.070180.005041
  2. Bentley, J. P. and Hanson, A. N. (1969) The hydroxyproline of elastin. Biochem. Biophys. Acta 175, 339-344.
  3. Bomstein, P. (1980) Structurally distinct Collagen types. Annu. Rev. Biochem. 49, 957-1003. https://doi.org/10.1146/annurev.bi.49.070180.004521
  4. Edwards, C. A and O'Brien, W. D. Jr. (1980) Modified assay for determination of hydroxyproline in a tissue hydrolyzate. Clin. Chim. Acta 104, 161-167. https://doi.org/10.1016/0009-8981(80)90192-8
  5. Fujiwara, S. and Nagai Y. (1981) Bovine renal cortex type I collagen; High contents of 3- and 4- Hydroxyprolines. J. Biochem.89, 1397-1401.
  6. Gosline, J., Lillie, M., Carrington, E., Guerette, P., Ortlepp, C. and Savage, K. (2002) Elastic proteins: biological roles and mechanical properties. Philos. Trans. R. Soc. London B BioI. Sci. 357, 121-132. https://doi.org/10.1098/rstb.2001.1022
  7. Gullberg, D. E. and Lundgren-Akerlund, E. (2002) Collagen-Binding I domain intergins-What do they do? Prog. Histochem. Cytochem. 37, 3-54. https://doi.org/10.1016/S0079-6336(02)80008-0
  8. Jimenez, S., Harsch, M. and Rosenbloom, J. (1973) Hydroxyproline stabilizes the triple helix of chick tendon collagen. Biochem. Biophys. Res. Commun. 52, 106-114. https://doi.org/10.1016/0006-291X(73)90960-1
  9. Kivirikko, K. I., Laitinen, O, Aer, J. and Halme, J. (1965) Studies with $14_{C}$_proline on the action of cortisomine on metabolism of collagen in rat. Biochem. Pharmacol. 14, 1445-1451. https://doi.org/10.1016/0006-2952(65)90178-4
  10. Khubchandani, K. R. and Snyder J. M. (2001) Surfactant protein A (SP-A): the alveolus and beyond. FASEB. J. 15, 59-69. https://doi.org/10.1096/fj.00-0318rev
  11. Nemethy, G. and Scheraga, H. A (1986) Stabilization of collagen fibrils by hydroxyproline. Biochem. 152, 267-273.
  12. Nony, P. A and Schnellman, R. J. (2001) Interaction between collagen IV and collagen binding intergins in renal cell repair after sublethal injury. Mol. Pharmacol. 60, 1226-1234.
  13. Pihlajaniemi, T., Myllya, R. and Krivirikko, K. I. (1991) Proly 4- hydroxylase and its role in collagen synthesis. J. Hepatol. 13, S2-S7.
  14. Prockop, D. J. (1964) Isotopic studies on collagen degradation and the urinary excretion of hydroxyproline. J. Clin. Invest. 43, 453-460. https://doi.org/10.1172/JCI104930
  15. Prockop, D. J. and Kivirikko, K. I. (1967) Relationship of hydroxyproline excretion in urine to collagen metabolism. Ann. Internl. Med. 66, 1243-1250. https://doi.org/10.7326/0003-4819-66-6-1243
  16. Prockop, D. J., Berj, R. A., Kivirikko, K. L. and Vitto, J. (1976) Biochemistry of collagen, Ramachandran GN, Reddi AH (eds); Plenum: New York, pp. 163-273.
  17. Reddy, K. and Enwemeka, C. S. (1996) A simplified method for the analysis of hydroxyproline in biological tissues. Clin. Biochem. 29, 225-229. https://doi.org/10.1016/0009-9120(96)00003-6
  18. Siddiqi, N. J. (2000) Determination of total, free, peptide-bound, protein-bound, soluble- and insoluble-collagen hydroxyproline content in tissues from the Arabian Sand Gazelles (Gazella subgutturosa marica). Saudi J. BioI. Sci. 7, 104-112.
  19. Siddiqi, N. J., AI-Jafari, A. A. and 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 Biochem. Funct. 18, 243-248. https://doi.org/10.1002/1099-0844(200012)18:4<243::AID-CBF878>3.0.CO;2-N
  20. Siddiqi, N. J. and Alhomida, A. S. (2001) A study of the distribution of total, free, peptide-bound, protein-bound, hydroxyproline in the plasma of Arabian Camel (Camelus dromedarius). Camp. Haematol. Int. 10, 144-147. https://doi.org/10.1007/s005800070006
  21. Siddiqi, N. J., Sharma, B. and Alhomida, A. S. (2001) A study of different hydroxyproline fractions in the bovine ocular tissues. Mol. Cell Biochem. 217, 67-71. https://doi.org/10.1023/A:1007236301956
  22. Siddiqi, N. J. and Alhomida, A. S. (2002) Distribution of total, free, peptide-bound and protein-bound hydroxyproline in the erythrocytes from different species. Comp. Clin. Pathol. 11, 123-128. https://doi.org/10.1007/s005800200010
  23. Siddiqi, N. J., Alhomida, A. S. and Pandey V. C. (2002) Hydroxyproline Distribution in the plasma of various mammals. J. Biochem. Mol. BioI. Biophys. 6, 159-162. https://doi.org/10.1080/10258140290027324
  24. Varghese, Z., Moorhead, J. F. and Wills, M. R. (1981) Plasma hydroxyproline fractions in patients with dialysis osteodystrophy. Clin. Chim. Acta 110, 105-111. https://doi.org/10.1016/0009-8981(81)90306-5
  25. Weiss, J. B., Jayson, M. I. V. (1982) Collagen in Health and Disease, pp. 414-423, Churchill Livingstone, New York, New York.

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