Cited by 79Cell Adhesion Molecules ResearchCellular Mechanics and InteractionsBone and Dental Protein Studies

Integrins: cell adhesives and modulators of cell function

Bosman, Fred T.·1993·The Histochemical Journal

Abstract

Integrins encompass a family of cell-surface molecules which play a crucial role in cell-cell and cell-extracellular matrix interaction. Of these heterodimeric transmembrane glycoproteins (consisting of an alpha and beta chain) as yet at least 20 different types have been described, all with a different pattern of reactivity with extracellular matrix components. In this review the cell and tissue distribution of the integrins is discussed, with special emphasis on immunohistochemical localization of the beta 1 integrins and the alpha 6 beta 4 integrin. The beta 1 integrins comprise a subfamily in which eight alpha chains combine with one beta (the beta 1) chain. The alpha 2 beta 1, alpha 3 beta 1 and alpha 6 beta 1 and the alpha 6 beta 4 integrins are expressed on a wide variety of epithelia on the basolateral surface or exclusively on the basal surface facing the basement membrane (e.g. alpha 6 beta 1 and alpha 6 beta 4). Leucocyte integrins, which share a common beta 2 chain, occur almost exclusively on white blood cells and their precursors. The vitronectin receptors, which share a common alpha v chain, occur in a wide variety of cell types. Integrins play a major role in the interaction of the cell with the extracellular matrix in order to create and maintain tissue architecture. It has become clear, however, that through integrin-ligand interaction cell function is also modulated. Furthermore, in pathological conditions integrins play a role of some significance. Integrins mediate leucocyte traffic in developing inflammatory processes and function in neoplastic growth when it comes to invasion and metastasis.

Integrity signals

Registry

Crossref · 10.1007/bf00159282

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  • Host ECM components and receptors preferentially localize to basolateral surface of polarized BBB endothelium.

    “Given that host ECM components and receptors preferentially localize to the basolateral surface of polarized BBB endothelium (16), we hypothesized that disruption of junctional protein complexes in brain endothelium is the first step leading to bacterial”

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Authors
Bosman, F. T.
Affiliations
Erasmus University Rotterdam (NL)
Corresponding author
Bosman, Fred T.
Venue
The Histochemical Journal
Published
1993-07
Volume
25
Issue
7
Pages
469-477
ISSN
  • 0018-2214 (ISSN-L)
  • 1573-6865
OpenAlex
W2013214344
Cited by
79
References
69
Citations by year
2024: 1 · 2021: 2 · 2019: 1 · 2018: 2 · 2015: 1 · 2014: 1
FWCI
0.72
Type
journal article
Language
en
Open access
closed
Locations
  • The Histochemical Journal (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
  • Health Sciences › Medicine › Rheumatology › Bone and Dental Protein Studies
Keywords
integrins, beta1 integrin, alpha2beta1 integrin, beta2 integrins, integrin αvβ3, cell-matrix interactions, cell adhesion, basement membrane, epithelium, inflammation, metastasis, tumor invasion, integrin-ligand interaction, immunolocalization
MeSH terms
Amino Acid Sequence, Animals, Cell Adhesion, Epithelial Cells, Epithelium, Humans, Immunohistochemistry, Leukocytes, Molecular Sequence Data, Neoplasms, Tissue Distribution, Tumor Cells, Cultured, Integrins

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