Linked Life Data

7683273

Source:http://linkedlifedata.com/resource/pubmed/id/7683273

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1993-5-28
pubmed:abstractText
Integrins are a family of cell surface glycoproteins that promote cell adhesion. The integrin alpha V beta 3, vitronectin receptor, is a major integrin expressed by osteoclasts. To further investigate the role of alpha V beta 3 in cell adhesion, we generated and characterized monoclonal antibodies to alpha V beta 3 by immunizing BALB/c mice with purified alpha V beta 3 protein. Three monoclonal antibodies (mAbs), 9D4.9.1, 9G2.1.3, and 10C4.1.3, from a total of more than 1100 positive cultures which bound alpha V beta 3, were characterized extensively: mAbs 9G2.1.3 and 10C4.1.3 recognize the alpha V beta 3 complex whereas mAb 9D4.9.1 reacts with the beta 3-chain shared between the alpha V beta 3 complex and gpIIbIIIa. Further epitope mapping using flow microfluorometry analysis and histochemical staining of various tissues showed that 9D4.9.1 and 10C4.1.3 recognized distinct epitopes. Ligand-binding studies using cell-bound and purified alpha V beta 3 demonstrated that all three mAbs blocked fibrinogen binding. Vitronectin binding was blocked by mAb 9D4.9.1 and, less effectively, by mAb 10C4.1.3; mAb 9G2.1.3 was without effect. All three mAbs recognized osteoclasts from human tissues; mAb 9G2.1.3 also stained osteoclasts from a wide range of nonhuman species. Monoclonal antibodies 9D4.9.1 and 9G2.1.3 bound to a panel of cultured cell lines and various tissues. In contrast, mAb 10C4.1.3 bound only weakly or not at all to tissues expressing alpha V beta 3 with the exception of osteoclasts. Thus, mAb 10C4.1.3 showed a very narrow tissue specificity being restricted to high-level expression on human osteoclasts.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0014-4827
pubmed:author
pubmed:issnType
Print
pubmed:volume
205
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
345-52
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:7683273-Amino Acid Sequence, pubmed-meshheading:7683273-Animals, pubmed-meshheading:7683273-Antibodies, Monoclonal, pubmed-meshheading:7683273-Cell Adhesion, pubmed-meshheading:7683273-Epitopes, pubmed-meshheading:7683273-Fibrinogen, pubmed-meshheading:7683273-Flow Cytometry, pubmed-meshheading:7683273-Glycoproteins, pubmed-meshheading:7683273-Humans, pubmed-meshheading:7683273-Integrins, pubmed-meshheading:7683273-Molecular Sequence Data, pubmed-meshheading:7683273-Oligopeptides, pubmed-meshheading:7683273-Osteoclasts, pubmed-meshheading:7683273-Receptors, Cytoadhesin, pubmed-meshheading:7683273-Receptors, Vitronectin, pubmed-meshheading:7683273-Recombinant Proteins, pubmed-meshheading:7683273-Species Specificity, pubmed-meshheading:7683273-Transfection, pubmed-meshheading:7683273-Tumor Cells, Cultured, pubmed-meshheading:7683273-Vitronectin
pubmed:year
1993
pubmed:articleTitle
Blocking monoclonal antibodies to alpha V beta 3 integrin: a unique epitope of alpha V beta 3 integrin is present on human osteoclasts.
pubmed:affiliation
Genentech Inc., South San Francisco, California 94080.
pubmed:publicationType
Journal Article, Comparative Study