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Integrin expression in human bone
Author(s) -
Hughes D.E.,
Salter D.M.,
Dedhar S.,
Simpson R.
Publication year - 1993
Publication title -
journal of bone and mineral research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.882
H-Index - 241
eISSN - 1523-4681
pISSN - 0884-0431
DOI - 10.1002/jbmr.5650080503
Subject(s) - integrin , vitronectin , fibronectin , osteoclast , microbiology and biotechnology , collagen receptor , osteoblast , osteocyte , alpha (finance) , extracellular matrix , biology , alpha v beta 3 , cell , receptor , medicine , genetics , in vitro , construct validity , nursing , patient satisfaction
Integrins are a family of heterodimeric transmembrane glycoproteins that are known to mediate cell‐cell and cell‐matrix interactions. Members of the VLA (very late activation) family, which consists of β 1 integrin in association with the VLA α chains (α 1–6 ), mediate adhesion of a wide range of cells to matrix proteins, such as fibronectin, collagen, and laminin, and may therefore be important for cell‐matrix interactions in bone. Integrin expression in human bone was studied immunohistochemically using cryostat sections of fracture callus, tumor‐associated reactive bone, and neonatal costochondral junctions, with a panel of well‐characterized antibodies against β 1–4 integrins, α 1–6 and αv integrins, and the αvβ 3 dimer (the classic vitronectin receptor). All cell types present in bone expressed β 1 and α 5 integrins; a subpopulation of osteoblastic cells expressed α 4 . The αv was uniformly expressed by osteoblasts but was heterogeneously expressed by osteocytes. Osteoclasts also expressed α 2 , αv, and αvβ 3 . These results demonstrate differential expression of a restricted range of integrins in bone. This supports the possibility that integrins may mediate the differing interactions of cells of the osteoblast and osteoclast lineages with the matrix of bone.