Literature DB >> 1720122

Vitronectin receptor has a role in bone resorption but does not mediate tight sealing zone attachment of osteoclasts to the bone surface.

P T Lakkakorpi1, M A Horton, M H Helfrich, E K Karhukorpi, H K Väänänen.   

Abstract

During bone resorption, osteoclasts form a tight attachment, the sealing zone, around resorption lacunae. Vitronectin receptor has previously been shown to be expressed in osteoclasts and it has been suggested that it mediates the tight attachment at the sealing zone. In this study we have shown that glycine-arginine-glycine-aspartic acid-serine pentapeptide inhibits bone resorption by isolated osteoclasts and drastically changes the morphology of the osteoclasts. When the vitronectin receptor was localized by immunofluorescence in rat and chicken osteoclasts cultured on bone slices, it was found to be distributed throughout the osteoclast cell membrane except in the sealing zone areas. Immunoperoxidase staining of rat bone sections at the light microscopical level also revealed intense staining of the cell membrane with occasional small unstained areas, probably corresponding to the sealing zones. Immunoelectron microscopy confirmed the results obtained by light microscopy showing specific labeling only at the ruffled borders and basolateral membranes (0.82 and 2.43 gold particles/microns of membrane, respectively), but not at the sealing zone areas (0.06 gold particles/microns of membrane). Both alpha v and beta 3 subunits of the vitronectin receptor were similarly localized. These results strongly suggest that, although the vitronectin receptor is important in the function of osteoclasts, it is not mediating the final sealing zone attachment of the osteoclasts to the mineralized bone surface.

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Year:  1991        PMID: 1720122      PMCID: PMC2289948          DOI: 10.1083/jcb.115.4.1179

Source DB:  PubMed          Journal:  J Cell Biol        ISSN: 0021-9525            Impact factor:   10.539


  33 in total

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5.  Arginine-glycine-aspartic acid- and fibrinogen gamma-chain carboxyterminal peptides inhibit platelet adherence to arterial subendothelium at high wall shear rates. An effect dissociable from interference with adhesive protein binding.

Authors:  J B Lawrence; W S Kramer; L P McKeown; S B Williams; H R Gralnick
Journal:  J Clin Invest       Date:  1990-11       Impact factor: 14.808

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Authors:  M D Pierschbacher; E Ruoslahti
Journal:  J Biol Chem       Date:  1987-12-25       Impact factor: 5.157

7.  A novel integrin beta subunit is associated with the vitronectin receptor alpha subunit (alpha v) in a human osteosarcoma cell line and is a substrate for protein kinase C.

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Journal:  EMBO J       Date:  1989-10       Impact factor: 11.598

8.  Echistatin is a potent inhibitor of bone resorption in culture.

Authors:  M Sato; M K Sardana; W A Grasser; V M Garsky; J M Murray; R J Gould
Journal:  J Cell Biol       Date:  1990-10       Impact factor: 10.539

9.  The function of multiple extracellular matrix receptors in mediating cell adhesion to extracellular matrix: preparation of monoclonal antibodies to the fibronectin receptor that specifically inhibit cell adhesion to fibronectin and react with platelet glycoproteins Ic-IIa.

Authors:  E A Wayner; W G Carter; R S Piotrowicz; T J Kunicki
Journal:  J Cell Biol       Date:  1988-11       Impact factor: 10.539

10.  The osteoclast functional antigen, implicated in the regulation of bone resorption, is biochemically related to the vitronectin receptor.

Authors:  J Davies; J Warwick; N Totty; R Philp; M Helfrich; M Horton
Journal:  J Cell Biol       Date:  1989-10       Impact factor: 10.539

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  21 in total

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7.  PYK2 in osteoclasts is an adhesion kinase, localized in the sealing zone, activated by ligation of alpha(v)beta3 integrin, and phosphorylated by src kinase.

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8.  Localization of CD44, the hyaluronate receptor, on the plasma membrane of osteocytes and osteoclasts in rat tibiae.

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9.  Bone is not essential for osteoclast activation.

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