The DOI matches its Crossref record; 31 of the 31 references it cites were found in a registry or an index.
Interaction of a 59-kDa Connective Tissue Matrix Protein with Collagen I and Collagen II
Open accessAbstract
We have studied binding to collagen of the 59-kDa protein present in most connective tissues. Collagen fibril formation, measured as increasing turbidity, was markedly retarded and reduced by the presence of small amounts of this protein. This was true for both collagen I and collagen II. The effect was also observed when pepsin-treated collagens were used, indicating that interaction with the telopeptides is not involved. The proportion of collagen precipitated in the assay was not or only marginally reduced. Thus, the altered optical properties indicate that structurally different fibrils are formed in the presence of the 59-kDa protein. The 59-kDa protein bound to collagen I or collagen II that had been insolubilized on polystyrene 96-well microtiter plates, as measured by enzyme-linked immunosorbent assay. Analogously, binding to the collagens was demonstrated for the PG-S2 low Mr proteoglycan, previously shown only to inhibit collagen fibrillogenesis. The two matrix components showed similar strength of binding, i.e. Kd 35 nM for the 59-kDa protein and 16 nM for PG-S2 at 20 degrees C. The results do not reveal if the collagen interaction site of the 59-kDa protein is different from that of PG-S2. Our observations do, however, suggest that the 59-kDa protein, as well as PG-S2, have functions related to the regulation of collagen organization in tissues.
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Self-citationCollagen fibril formation. Optimal in vitro conditions and preliminary kinetic results.
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The Heat Precipitation of Collagen from Neutral Salt Solutions: Some Rate-Regulating Factors
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The regulatory roles of small leucine‐rich proteoglycans in extracellular matrix assembly
Chen, S., & Birk, D. E. (2013) · The FEBS Journal · doi:10.1111/febs.12136 · Cited by 378
Binding of the proteoglycan decorin to collagen type VI.
Bidanset, D. J., Guidry, C., Rosenberg, L. C., Choi, H. U., Timpl, R., & Hook, M. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42759-7 · Cited by 339
Chondroitin Sulfate Perlecan Enhances Collagen Fibril Formation
Kvist, A. J., Johnson, A. E., Mörgelin, M., Gustafsson, E., Bengtsson, E., Lindblom, K., Aszódi, A., Fässler, R., Sasaki, T., Timpl, R., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m607892200 · Cited by 102
Madamanchi, A., Santoro, S. A., & Zutter, M. M. (2014) · Advances in Experimental Medicine and Biology · doi:10.1007/978-94-017-9153-3_3 · Cited by 87
Metadata
- Authors
- Hedbom, E., & Heinegård, D.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1989-04
- Volume
- 264
- Issue
- 12
- Pages
- 6898-6905
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1748510480
- Cited by
- 332
- References
- 31
- FWCI
- 16.49
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Hedbom, E., & Heinegård, D. (1989). Interaction of a 59-kDa Connective Tissue Matrix Protein with Collagen I and Collagen II. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)83516-5
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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).
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