The DOI matches its Crossref record; 40 of the 40 references it cites were found in a registry or an index.
Interaction of the 70,000-mol-wt amino-terminal fragment of fibronectin with the matrix-assembly receptor of fibroblasts.
Open accessAbstract
Plasma fibronectin binds saturably and reversibly to substrate-attached fibroblasts and is subsequently incorporated into the extracellular matrix (McKeown-Longo, P.J., and D. F. Mosher, 1983, J. Cell Biol., 97:466-472). We examined whether fragments of fibronectin are processed in a similar way. The amino-terminal 70,000-mol-wt catheptic D fragment of fibronectin bound reversibly to cell surfaces with the same affinity as intact fibronectin but did not become incorporated into extracellular matrix. The 70,000-mol-wt fragment blocked binding of intact fibronectin to cell surfaces and incorporation of intact fibronectin into extracellular matrix. Binding of the 70,000-mol-wt fragment to cells was partially abolished by cleavage into 27,000-mol-wt heparin-binding and 40,000-mol-wt gelatin-binding fragments and more completely abolished by reduction and alkylation of disulfide bonds. Binding of the 70,000-mol-wt fragment to cells was not blocked by gelatin or heparin. When coated onto plastic, the 70,000-mol-wt fragment did not mediate attachment and spreading of suspended fibroblasts. Conversely, fibronectin fragments that had attachment and spreading activity did not block binding of exogenous fibronectin to substrate-attached cells. These results indicate that there is a cell binding site in the 70,000-mol-wt fragment that is distinct from the previously described cell attachment site and is required for assembly of exogenous fibronectin into extracellular matrix.
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Cited by
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Structure and Biological Role of Vitronectin
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Metadata
- Authors
- McKeown-Longo, P. J., & Mosher, D. F.
- Venue
- The Journal of cell biology
- Publisher
- Rockefeller University Press
- Published
- 1985-02-01
- Volume
- 100
- Issue
- 2
- Pages
- 364-374
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- OpenAlex
- W2083216138
- Cited by
- 334
- References
- 40
- FWCI
- 9.20
- Type
- journal article
- Language
- en
- Open access
- bronze
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- McKeown-Longo, P. J., & Mosher, D. F. (1985). Interaction of the 70,000-mol-wt amino-terminal fragment of fibronectin with the matrix-assembly receptor of fibroblasts. The Journal of cell biology. https://doi.org/10.1083/jcb.100.2.364
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