The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Evidence for Procollagen, a Biosynthetic Precursor of Collagen
Open accessAbstract
Incubation of rat calvaria for short times in the presence of a labeled amino acid revealed the existence of a collagen fraction (procollagen) that functions as a biosynthetic precursor of collagen. Procollagen contains an α1-like chain (pre-α1) that elutes earlier from CM-cellulose than does rat-bone α1 and has a molecular weight, estimated by acrylamide gel electrophoresis, of 120,000. A time-dependent conversion of pre-α1 to α1 was demonstrated by incubation of calvaria for periods varying from 9 to 60 min and by a pulse-chase experiment. Limited cleavage of procollagen with pepsin resulted in a molecule with a chain resembling α1 in chromatographic properties, molecular weight, and relative hydroxyproline and proline contents. Thus, conversion of procollagen to collagen is likely to occur in vivo by a proteolytic mechanism. The additional peptide sequences in procollagen may serve to initiate chain association in triple-helix formation, to facilitate molecular transport, and to inhibit intracellular fibrogenesis.
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Cites
Cross-linking of collagen and elastin. Properties of lysyl oxidase
Siegel, R. C., Pinnell, S. R., & Martin, G. R. (1970) · Biochemistry · doi:10.1021/bi00825a004 · Cited by 345
Cited by
Biochemical characteristics and biological significance of the genetically-distinct collagens
Miller, E. J. (1976) · Molecular and Cellular Biochemistry · doi:10.1007/bf01731779 · Cited by 462
Weinstock, M., & Leblond, C. P. (1974) · The Journal of Cell Biology · doi:10.1083/jcb.60.1.92 · Cited by 377
Collagen Made of Extended alpha-Chains, Procollagen, in Genetically-Defective Dermatosparaxic Calves
Lenaers, A., Nusgens, B. V., LapiERE, C. M., & Ansay, M. (1971) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1971.tb01651.x · Cited by 295
Ehlers–Danlos syndrome: A showcase of conditions that lead to understanding matrix biology
Byers, P. H., & Murray, M. L. (2014) · Matrix Biology · doi:10.1016/j.matbio.2013.07.005 · Cited by 68
“These studies occurred in parallel with others of collagens produced by rat calvaria (Bellamy and Bornstein, 1971) and cultured fibroblast (Layman et al., 1971) that provided the details of procollagen structure and established the existence of the amino-terminal and carboxylterminal propeptides…”
ResultSon, D. J., Jung, J. C., Choi, Y. M., Ryu, H. Y., Lee, S., & Davis, B. A. (2020) · Nutrients · doi:10.3390/nu12020300 · Cited by 26
Metadata
- Authors
- Bellamy, G., & Bornstein, P.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1971-06
- Volume
- 68
- Issue
- 6
- Pages
- 1138-1142
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2084287360
- Cited by
- 193
- References
- 1
- FWCI
- 33.03
- Type
- journal article
- Language
- en
- Open access
- green
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- Bellamy, G., & Bornstein, P. (1971). Evidence for Procollagen, a Biosynthetic Precursor of Collagen. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.68.6.1138
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
