Linked Life Data

11806996

Source:http://linkedlifedata.com/resource/pubmed/id/11806996

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2002-1-24
pubmed:abstractText
Alpha(IIb)beta(3) and alpha(v)beta(3) belong to the beta(3) integrin subfamily. Although the beta(3) subunit is a key regulator for the biosynthesis of beta(3) integrins, it remains obscure whether missense mutations in beta(3) may induce the same defects in both alpha(IIb)beta(3) and alpha(v)beta(3). In this study, it is revealed that thrombasthenic platelets with a His280Pro mutation in beta(3), which is prevalent in Japanese patients with Glanzmann thrombasthenia, did contain significant amounts of alpha(v)beta(3) (about 50% of control) using sensitive enzyme-linked immunosorbent assay. Expression studies showed that the His280Probeta(3) mutation impaired alpha(IIb)beta(3) expression but not alpha(v)beta(3) expression in 293 cells. To extend these findings, the effects of several beta(3) missense mutations leading to an impaired alpha(IIb)beta(3) expression on alpha(v)beta(3) function as well as expression was examined: Leu117Trp, Ser162Leu, Arg216Gln, Cys374Tyr, and a newly created Arg216Gln/Leu292Ser mutation. Leu117Trp and Cys374Tyr beta(3) mutations did impair alpha(v)beta(3) expression, while Ser162Leu, Arg216Gln, and Arg216Gln/Leu292Ser mutations did not. With regard to ligand binding function, Ser162Leu mutation induced especially distinct effects between 2 beta(3) integrins: it markedly impaired ligand binding to alpha(IIb)beta(3) but not to alpha(v)beta(3) at all. These data clearly demonstrate that the biosynthesis and the ligand binding function of alpha(IIb)beta(3) and those of alpha(v)beta(3) are regulated in part by different mechanisms. Present data would be a clue to elucidate the regulatory mechanism of expression and function of beta(3) integrins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0006-4971
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
99
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
931-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:11806996-Adult, pubmed-meshheading:11806996-Amino Acid Sequence, pubmed-meshheading:11806996-Antigens, CD, pubmed-meshheading:11806996-Blood Platelets, pubmed-meshheading:11806996-Cell Line, pubmed-meshheading:11806996-DNA Mutational Analysis, pubmed-meshheading:11806996-Female, pubmed-meshheading:11806996-Fibrinogen, pubmed-meshheading:11806996-Gene Expression, pubmed-meshheading:11806996-Humans, pubmed-meshheading:11806996-Integrin beta3, pubmed-meshheading:11806996-Molecular Sequence Data, pubmed-meshheading:11806996-Mutagenesis, Site-Directed, pubmed-meshheading:11806996-Mutation, Missense, pubmed-meshheading:11806996-Platelet Glycoprotein GPIIb-IIIa Complex, pubmed-meshheading:11806996-Platelet Membrane Glycoproteins, pubmed-meshheading:11806996-Protein Binding, pubmed-meshheading:11806996-Receptors, Vitronectin, pubmed-meshheading:11806996-Thrombasthenia, pubmed-meshheading:11806996-Transfection
pubmed:year
2002
pubmed:articleTitle
Missense mutations in the beta(3) subunit have a different impact on the expression and function between alpha(IIb)beta(3) and alpha(v)beta(3).
pubmed:affiliation
Department of Internal Medicine and Molecular Science, Graduate School of Medicine B5, Osaka University, 2-2 Yamadaoka, Suita Osaka 565-0871, Japan.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't