The biochemical mechanism accounting for the connective tissue abnormalities in homocystinuria was explored by examining the effects of various amino acids known to accumulate in the plasma of patients with this disease on cross-link formation in collagen. Neutral salt solutions of purified, rat skin collagen, rich in cross-link precursor aldehydes, were polymerized to native type fibrils by incubating at 37°C in the presence of homocysteine, homocystine, or methionine. After the polymerization was completed, each sample was examined for the formation of covalent intermolecular cross-links, assessed indirectly by solubility tests and directly by measuring the cross-link compounds after reduction with tritiated sodium borohydride and hydrolysis.
Andrew H. Kang, Robert L. Trelstad
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Title and authors | Publication | Year |
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Pulmonary surfactant: an immunological perspective
ZC Chroneos, Z Sever-Chroneos, VL Shepherd |
Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology | 2009 |
Collagen cross-links as a determinant of bone quality: a possible explanation for bone fragility in aging, osteoporosis, and diabetes mellitus
M Saito, K Marumo |
Osteoporosis International | 2009 |
Raloxifene ameliorates detrimental enzymatic and nonenzymatic collagen cross-links and bone strength in rabbits with hyperhomocysteinemia
M Saito, K Marumo, S Soshi, Y Kida, C Ushiku, A Shinohara |
Osteoporosis International | 2009 |
The relation of plasma homocysteine to radiographic knee osteoarthritis
M Fayfman, J Niu, YQ Zhang, DT Felson, B Sack, P Aliabadi, J Selhub, DJ Hunter |
Osteoarthritis and Cartilage | 2009 |