The DOI matches its Crossref record; 129 of the 129 references it cites were found in a registry or an index.
Still More Complexity in Mammalian Basement Membranes
Abstract
At the epithelial/mesenchymal interface of most tissues lies the basement membrane (BM). These thin sheets of highly specialized extracellular matrix vary in composition in a tissue-specific manner, and during development and repair. For about two decades it has been apparent that all BMs contain laminins, entactin-1/nidogen-1, Type IV collagen, and proteoglycans. However, within the past few years this complexity has increased as new components are described. The entactin/nidogen (E/N) family has expanded with the recent description of a new isoform, E/N-2/osteonidogen. Agrin and Type XVIII collagen have been reclassified as heparan sulfate proteoglycans (HSPGs), expanding the repertoire of HSPGs in the BM. The laminin family has become more diverse as new α-chains have been characterized, increasing the number of laminin isoforms. Interactions between BM components are now appreciated to be regulated through multiple, mostly domain-specific mechanisms. Understanding the functions of individual BM components and their assembly into macromolecular complexes is a considerable challenge that may increase as further BM and cell surface ligands are discovered for these proteins.
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Cites
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Cited by
Matrigel: A complex protein mixture required for optimal growth of cell culture
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Metadata
- Authors
- Erickson, A. C., & Couchman, J. R.
- Venue
- Journal of Histochemistry & Cytochemistry
- Publisher
- SAGE Publications
- Published
- 2000-10
- Volume
- 48
- Issue
- 10
- Pages
- 1291-1306
- ISSN
- 0022-1554 (ISSN-L)
- 1551-5044
- OpenAlex
- W1971325550
- Cited by
- 303
- References
- 129
- FWCI
- 7.95
- Type
- journal article
- Language
- en
- Open access
- closed
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