Abstract
This study sought to evaluate whether the architecture of the matrix of cortical and trabecular bone is exactly the same. For this purpose we analyzed the extent of some posttranslational modifications of type I collagen, which is the major component of bone matrix. Ten female and 10 male 100-day-old rats were sacrificed and the content of hydroxylysine, glycosylated hydroxylysine, and pyridinium cross-links of collagen from cortical and trabecular bone was determined. The amount of each compound was expressed as a molar ratio with hydroxyproline. The collagen posttranslational modification pattern appears to be the same in both sexes but with a higher extent of differences in females compared with males. Comparing cortical and trabecular bone, the former contains a higher amount of hydroxylysine residues whereas in the latter, glycosylation of hydroxylysine is higher and pyridinium cross-link concentration is lower. Moreover, an inverse linear relationship between glycosylated hydroxylysine and pyridinium crosslinks concentration was established, both for female (r=−0.455,P=0.04) and male rats (r=−0.426;P=0.06). This paper discusses what these findings may mean in functional terms.
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References
Kivirikko KI, Myllyla R (1982) Post-translational enzymes in the biosynthesis of collagen: intracellular enzymes. Methods Enzymol 82:284–304
Pinnell SR, Fox R, Krane SM (1971) Human collagens: differences in glycosylated hydroxylysines in skin and bone. Biochim Biophys Acta 239:119–122
Bailey AJ, Wotton SF, Sims TJ, Thompson PW (1993) Biochemicl changes in the collagen of human osteoporotic bone matrix. Conn Tissue Res 29:119–132
Kuivaniemi H, Tromp G, Prockop DJ (1991) Mutations in collagen genes: causes of rare and some common diseases in humans. FASEB J 5:2052–2060
Cell and molecular biology of vertebrate hard tissues (1988) Ciba Found Symp 136. John Wiley & Sons, Chichester, UK
Baron R (1993) Anatomy and ultrastructure of bone. In: Murray J (ed) Primer on the metabolic bone diseases and disorders of mineral metabolism, 2nd ed. Raven Press, New York, pp 3–9
Manolagas SC, Jilka RL (1992) Cytokines, hematopoiesis, osteoclastogenesis, and estrogens. Calcif Tissue Int 50:199–202
Bain SD, Bailey MS, Celino DL, Lantry MM, Edwards MW (1993) High-dose estrogen inhibits bone resorption and stimulates bone formation in the ovariectomized mouse. J Bone Miner Res 8:435–442
Turner RT, Evans GL, Wakley GK (1993) Mechanism of action of estrogen on cancellous bone balance in tibiae of ovariectomized growing rats: inhibition on indices of formation and resorption. J Bone Miner Res 8:359–366
Kalu KN, Salerno E, Liu CC, Ferraro F, Arjmandi BN, Salih MA (1993) Ovariectomy-induced bone loss and the hematopoietic system. Bone Miner 23:145–161
Kalu DN, Salerno E, Higami Y, Liu CC, Ferraro F, Salih MA, Arjmandi BH (1993) In vivo effects of transforming growth factor-β in ovariectomized rats. Bone Miner 22:209–220
Horowitz MC (1993) Cytokines and estrogens in bone: antiosteoporotic effects. Science 260:626–627
Wallach S, Avioli LV, Feinblatt JD, Carstens JH (1993) Cytokines and bone metabolism. Calcif Tissue Int 53:293–296
Kalu DN (1991) The ovariectomized rat model of postmenopausal bone loss. Bone Miner 15:175–192
Frost HM, Jee WSS (1992) On the rat model of human osteopenias and osteoporosis. Bone Miner 18:227–236
Moro L, Modricky C, Stagni N, Vittur F, de Bernard B (1984) High-performance liquid chromatographic analysis of urinary hydroxylysyl glycosides as indicators of collagen turnover. Analyst 109:1621–1622
Gray WR (1967) Dansyl chloride procedure. Methods Enzymol 11:139–151
de Bernard B, Moro L, Gazzarrini C, Battista C (1989) Galactosyl-hydroxylysine as biochemical marker of bone collagen degradation. In: De Bastiani G, Pecile A, Pietrogrande V, Torri G (eds) Le osteoporosi e il loro trattamento. Monduzzi, Bologna, pp 9–15
Eyre DR, Dickson IR, Van Ness K (1988) Collagen cross-linking in human bone and articular cartilage. Biochem J 252:495–500
Teerlink T, Tavenier P, Netelenbos C (1989) Selective determination of hydroxyproline in urine by high-performance liquid chromatography using precolumn derivatization. Clin Chim Acta 183:309–316
Michalsky M, Noris Suarez K, Bettica P, Pecile A, Moro L (1993) Rat cortical and trabecular bone collagen glycosylation are differently influenced by ovariectomy. Biochem Biophys Res Commun 192:1281–1288
Black D, Farquharson C, Robins SP (1989) Excretion of pyridinium cross-links of collagen in ovariectomized rats as urinary markers for increased bone resorption. Calcif Tissue Int 44:343–347
Eyre DR, Glimcher MJ (1973) Analysis of a crosslinked peptide from calf bone collagen: evidence that hydroxylysyl glycoside participates in the crosslink. Biochem Biophys Res Commun 52:663–671
Robins SP, Bailey AJ (1973) Isolation and characterization of glycosyl derivatives of the reducible cross-links in collagens. FEBS Lett 38:334–336
Eyre DR, Paz MA, Gallop PM (1984) Cross-linking in collagen and elastin. Ann Rev Biochem 53: 717–748
Bailey AJ, Robins SP, Balian GA (1974) Biological significance of the cross-links of collagen. Nature 251: 105–109
Glimcher MJ (1976) The composition, structure and organisation of bone and other mineralised tissues and the mechanism of calcification. In: Greep RO, Astwood, EB (eds) Handbook of physiology: endocrinology, 7. American Physiological Society, Washington, pp 25–113
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Suarez, K.N., Romanello, M., Bettica, P. et al. Collagen type I of rat cortical and trabecular bone differs in the extent of posttranslational modifications. Calcif Tissue Int 58, 65–69 (1996). https://doi.org/10.1007/BF02509548
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DOI: https://doi.org/10.1007/BF02509548