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Cross-Linking of Collagen: Endogenous aldehydes in collagen react in several ways to form a variety of unique covalent cross-links.
Abstract
The formation of collagen cross-links is attributable to the presence of two aldehyde-containing amino acids which react with other amino acids in collagen to generate difunctional, trifunctional, and tetrafunctional cross-links. A necessary prerequisite for the development of these cross-links is that the collagen molecules be assembled in the naturally occurring fibrous polymer. Once this condition is met, cross-linking occurs in a spontaneous, progressive fashion. The chemical structures of the cross-links dictate that very precise intermolecular alignments must occur in the collagen polymer. This seems to be a function of each specific collagen because the relative abundance of the different cross-links varies markedly, depending upon the tissue of origin of the collagen.
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Cited by
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Levental, K. R., Yu, H., Kass, L., Lakins, J. N., Egeblad, M., Erler, J. T., Fong, S. F. T., Csiszar, K., Giaccia, A., Weninger, W., et al. (2009) · Cell · doi:10.1016/j.cell.2009.10.027 · Cited by 4,101
Hoffman, P. N., & Lasek, R. J. (1975) · The Journal of cell biology · doi:10.1083/jcb.66.2.351 · Cited by 937
Collagen: Molecular Diversity in the Body's Protein Scaffold
Eyre, D. R. (1980) · Science · doi:10.1126/science.7355290 · Cited by 451
Collagen type I and type V are present in the same fibril in the avian corneal stroma.
Birk, D. E., Fitch, J. M., Babiarz, J. P., & Linsenmayer, T. F. (1988) · The Journal of cell biology · doi:10.1083/jcb.106.3.999 · Cited by 391
Extracellular matrix regulation of fibroblast function: redefining our perspective on skin aging
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Metadata
- Authors
- Tanzer, M. L.
- Venue
- Science
- Published
- 1973-05-11
- Volume
- 180
- Issue
- 4086
- Pages
- 561-566
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2093434593
- Cited by
- 387
- References
- 0
- FWCI
- 20.63
- Type
- journal article
- Language
- en
- Open access
- closed
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- Tanzer, M. L. (1973). Cross-Linking of Collagen: Endogenous aldehydes in collagen react in several ways to form a variety of unique covalent cross-links. Science. https://doi.org/10.1126/science.180.4086.561
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
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.
