Journal Article10.1002/JBMR.5650080503
Integrin expression in human bone
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TL;DR: In this article, 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 beta 1-4 integrins, alpha 1-6, and alpha V beta 3 dimer.
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Abstract: 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 beta 1 integrin in association with the VLA alpha chains (alpha 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 beta 1-4 integrins, alpha 1-6 and alpha V integrins, and the alpha V beta 3 dimer (the classic vitronectin receptor). All cell types present in bone expressed beta 1 and alpha 5 integrins; a subpopulation of osteoblastic cells expressed alpha 4. The alpha V was uniformly expressed by osteoblasts but was heterogeneously expressed by osteocytes. Osteoclasts also expressed alpha 2, alpha V, and alpha V beta 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.
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References
VCAM-1 on activated endothelium interacts with the leukocyte integrin VLA-4 at a site distinct from the VLA-4/Fibronectin binding site
Mariano J. Elices,Laurelee Osborn,Yoshikazu Takada,Carol Crouse,Stefan Luhowskyj,Martin E. Hemler,Roy R. Lobb +6 more
TL;DR: The VCAM-1/VLA-4 ligand-receptor pair may play a major role in the recruitment of mononuclear leukocytes to inflammatory sites in vivo.
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Osteopontin--a possible anchor of osteoclasts to bone.
TL;DR: The results thus support the hypothesis that osteoclasts when resorbing bone are anchored by osteopontin bound both to the mineral of bone matrix and to a vitronectin receptor on the osteoclast plasma membrane.
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The membrane glycoprotein Ia-IIa (VLA-2) complex mediates the Mg++-dependent adhesion of platelets to collagen.
TL;DR: Findings provide additional evidence that the platelet membrane Ia-IIa complex is the mediator of Mg++-dependent platelet adhesion to collagen and suggest that the VLA-2 complex may also function as an Mg+-dependent collagen receptor in other cells.
A human lymphocyte‐associated antigen involved in cell‐mediated lympholysis
TL;DR: It is concluded that HLFA is likely to be involved in the nonspecific adherence or lytic functions of killer cells rather than specific antigen recognition.
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