期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1971
卷号：68
期号：11
页码：2638-2642
DOI：10.1073/pnas.68.11.2638
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Sodium dodecyl sulfate-acrylamide gel electrophoresis and molecular-sieve chromatography on 8% agarose demonstrate the existence of a very high molecular weight (500,000-600,000), proline-rich protein in cultured 3T6 fibroblasts that appears to be the precursor molecule (procollagen) of collagen. The kinetics of [3H]-proline uptake indicate that this precursor is synthesized at a different rate than are other cell proteins and is secreted apparently unchanged into the medium, where it undergoes modification; it then precipitates around the cells as collagen fibrils that contain the characteristic tropocollagen polypeptide chains. The solubility of this precursor in hot 5% Cl3CCOOH, its hydroxyproline to proline ratio, and its sensitivity to highly-purified bacterial collagenase all indicate that this molecule is of collagenous nature, but that it has considerable regions of noncollagen peptide (about half of the molecule is collagenase sensitive, and it has half of the normal amount of hydroxylated proline residues). These results support the concept of a procollagen molecule, of molecular weight about 500,000-600,000, that contains large regions of noncollagen peptides, which might allow the collagen [α]-chain regions to associate in register and that also can provide the correct chain composition for tropocollagen. Upon secretion of the procollagen molecule, the intercollagen-peptide regions are cleaved and the finished tropocollagen molecule then polymerizes into typical intercellular fibrils.
关键词：fibroblasts ; isotopic tracers ; acrylamide gel electrophoresis ; gel filtration
