Effect of prevention of procollagen triple-helix formation on proline 3-hydroxylation in freshly isolated chick-embryo tendon cells
- 15 April 1981
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 196 (1), 203-206
- https://doi.org/10.1042/bj1960203
Abstract
Inhibition of procollagen triple-helix formation by the addition of cis-hydroxyproline or azetidine-2-carboxylic acid increased the synthesis of 3-hydroxy[14C]proline 1.7-1.8-fold in pulse-chase experiments with freshly isolated chick embryo tendon cells. The amount of 3-hydroxy[14C]proline, expressed as a percentage of the total 14C radioactivity in hydroxyproline, reached 8.4%. Control experiments indicated that the 2 analogs had no effect on the prolyl 3-hydroxylase activity of these cells. Apparently, the time available before triple-helix formation in part regulates the extent of the 3-hydroxylation of proline in the biosynthesis of collagen in intact cells.This publication has 29 references indexed in Scilit:
- Partial purification and characterization of chick-embryo prolyl 3-hydroxylaseBiochemical Journal, 1979
- Formation of interchain disulfide bonds and helical structure during biosynthesis of procollagen by embryonic tendon cellsBiochemistry, 1974
- Prolyl HydroxylasePublished by Wiley ,1974
- Rate of helix formation by intracellular procollagen and protocollagen. Evidence for a role for disulfide bonsBiochemical and Biophysical Research Communications, 1973
- The biosynthesis of basement membrane collagen in embryonic chick lens. 3. Intracellular formation of the triple helix and the formation of aggregates through disulfide bonds.1973
- Biosynthesis of Cartilage ProcollagenEuropean Journal of Biochemistry, 1973
- Incorporation of cis-hydroxyproline into collagen by tendon cells. Failure of the intracellular collagen to assume a triple-helical conformationBiochimica et Biophysica Acta (BBA) - Protein Structure, 1972
- The biosynthesis of basement membrane collagen in embryonic chick lens. I. Delay between the synthesis of polypeptide chains and the secretion of collagen by matrix-free cells.1972
- Time lag in the secretion of collagen by matrix-free tendon cells and inhibition of the secretory process by colchicine and vinblastineBiochimica et Biophysica Acta (BBA) - General Subjects, 1972
- Biosynthesis of abnormal collagens with amino acid analogues: I. Incorporation of l-azetidine-2-carboxylic acid and cis-4-fluoro-l-proline into protocollagen and collagenBiochimica et Biophysica Acta (BBA) - Protein Structure, 1969