Linked Life Data

12068019

Source:http://linkedlifedata.com/resource/pubmed/id/12068019

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
36
pubmed:dateCreated
2002-9-2
pubmed:abstractText
CD9, a member of the tetraspanin family of proteins, is characterized by four transmembrane domains and two extracellular loops. Surface expression of CD9 on Chinese hamster ovary (CHO) cells dramatically enhances spreading and motility on fibronectin. To elucidate the mechanistic basis of CD9-fibronectin interaction, binding to fibronectin was investigated using purified and recombinant forms of CD9. The affinity of fibronectin for CD9 in enzyme-linked immunosorbent assay was 81 +/- 25 nm. The binding of fibronectin to immobilized CD9 was enhanced by Ca(2+) ions. Protein binding and peptide competition studies demonstrated that peptide 6 derived from CD9 extracellular loop 2 (amino acids 168-192) contained part of the fibronectin-binding domain. Additionally, enhanced adhesion of CD9-CHO-B2 cells to fibronectin was significantly reduced by peptide 6. CD9-CHO cells had a 5-fold increase in motility to fibronectin as compared with mock-transfected controls, an effect that correlated with CD9 cell surface density. Truncation of CD9 extracellular loop 2 and peptide 6 caused inhibition of CD9-CHO cell motility to fibronectin. Deletion of CD9 extracellular loop 1 had no significant effect on CHO cell motility. These findings demonstrate a critical role for CD9 extracellular loop 2 in cell motility to fibronectin and clarify the mechanism by which CD9-fibronectin interaction modulates cell adhesion and motility.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
6
pubmed:volume
277
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
32445-52
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:12068019-Amino Acid Sequence, pubmed-meshheading:12068019-Animals, pubmed-meshheading:12068019-Antigens, CD, pubmed-meshheading:12068019-Antigens, CD9, pubmed-meshheading:12068019-Binding Sites, pubmed-meshheading:12068019-CHO Cells, pubmed-meshheading:12068019-Calcium, pubmed-meshheading:12068019-Cell Adhesion, pubmed-meshheading:12068019-Cell Movement, pubmed-meshheading:12068019-Cells, Cultured, pubmed-meshheading:12068019-Cricetinae, pubmed-meshheading:12068019-DNA, Complementary, pubmed-meshheading:12068019-Dose-Response Relationship, Drug, pubmed-meshheading:12068019-Enzyme-Linked Immunosorbent Assay, pubmed-meshheading:12068019-Fibronectins, pubmed-meshheading:12068019-Gene Deletion, pubmed-meshheading:12068019-Membrane Glycoproteins, pubmed-meshheading:12068019-Molecular Sequence Data, pubmed-meshheading:12068019-Mutagenesis, Site-Directed, pubmed-meshheading:12068019-Peptides, pubmed-meshheading:12068019-Phenotype, pubmed-meshheading:12068019-Protein Structure, Tertiary, pubmed-meshheading:12068019-Recombinant Proteins, pubmed-meshheading:12068019-Sequence Homology, Amino Acid, pubmed-meshheading:12068019-Transfection
pubmed:year
2002
pubmed:articleTitle
Chinese hamster ovary cell motility to fibronectin is modulated by the second extracellular loop of CD9. Identification of a putative fibronectin binding site.
pubmed:affiliation
Vascular Biology Center of Excellence and the Department of Pharmacology, University of Tennessee Health Science Center and the Veterans Administration Medical Center, Memphis, Tennessee 38163, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't