Linked Life Data

7513610

Source:http://linkedlifedata.com/resource/pubmed/id/7513610

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1994-6-6
pubmed:abstractText
Using whole viable human colon carcinoma HT29 cells as immunogen, we produced a monoclonal antibody (mAb) termed 69-6-5. The antibody was functionally selected on its anti-cell-spreading activity. By immunoprecipitation of surface radiolabeled cell lysates from HT29-D4 cells (an HT29 cell clone), mAb 69-6-5 recognized a molecular complex resembling integrin heterodimers. Sequential immunodepletions with mAb to the integrin alpha v subunit demonstrated that this complex was composed of alpha v-containing integrins. Accordingly, mAb 69-6-5 reacted with integrin alpha v beta 3 immunopurified from melanoma cells and integrins alpha v beta 5 and alpha v beta 6 immunopurified from pancreatic carcinoma cells. In cell adhesion assays, the 69-6-5 mAb was able to inhibit strongly in a dose-dependent manner arginine-glycine-aspartic acid-mediated adhesion of HT29-D4 cells to vitronectin, fibronectin, or ProNectin F but not to laminin or collagen. Immunoprecipitations with beta chain-specific antisera indicated that these cells express integrins alpha v beta 5 (receptor for vitronectin) and alpha v beta 6 (receptor for fibronectin) but neither alpha v beta 1 nor alpha v beta 3. In summary, these results indicated that mAb 69-6-5 reacts with several alpha v integrins and that it can effectively interfere with the adhesive functions of at least alpha v beta 5 and alpha v beta 6, which represent the major receptors on HT29-D4 cells responsible for their adhesion on vitronectin and fibronectin.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0008-5472
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
54
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2102-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:7513610-Amino Acid Sequence, pubmed-meshheading:7513610-Antibodies, Monoclonal, pubmed-meshheading:7513610-Antigens, Neoplasm, pubmed-meshheading:7513610-Cell Adhesion, pubmed-meshheading:7513610-Cell Line, pubmed-meshheading:7513610-Cell Movement, pubmed-meshheading:7513610-Colonic Neoplasms, pubmed-meshheading:7513610-Cross Reactions, pubmed-meshheading:7513610-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:7513610-Epitopes, pubmed-meshheading:7513610-Fibronectins, pubmed-meshheading:7513610-Glycoproteins, pubmed-meshheading:7513610-Humans, pubmed-meshheading:7513610-Integrins, pubmed-meshheading:7513610-Molecular Sequence Data, pubmed-meshheading:7513610-Molecular Weight, pubmed-meshheading:7513610-Receptors, Cytoadhesin, pubmed-meshheading:7513610-Receptors, Vitronectin, pubmed-meshheading:7513610-Tumor Cells, Cultured, pubmed-meshheading:7513610-Vitronectin
pubmed:year
1994
pubmed:articleTitle
A monoclonal antibody inhibits adhesion to fibronectin and vitronectin of a colon carcinoma cell line and recognizes the integrins alpha v beta 3, alpha v beta 5, and alpha v beta 6.
pubmed:affiliation
Institut de Chimie Biologique, ER CNRS 079, Université d'Aix-Marseille, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't