Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
5 Pt 1
|
| pubmed:dateCreated |
1998-12-14
|
| pubmed:abstractText |
The platelet GPIIb-GPIIIa heterodimer (integrin alphaIIbbeta3) binds fibrinogen with high affinity in response to activation by agonists, leading to platelet aggregation and formation of a hemostatic plug. The 326GRV motif in GPIIb is highly conserved in the alpha-subunit of other integrins, suggesting that it might play an important functional role. Moreover, Arg327-->His substitution in GPIIb has been associated with defective platelet surface expression of GPIIb-IIIa and thrombasthenic phenotype. This work aimed at elucidating whether the absence of Arg327 or its substitution by His was responsible for the impaired surface expression of GPIIb-IIIa complexes. Transfection of cDNA encoding [Ala327]GPIIb, [Gln327]GPIIb, or [Phe327]GPIIb into Chinese hamster ovary cells inherently expressing GPIIIa permitted surface exposure of GPIIb-IIIa complexes, whereas [Glu327]GPIIb did not. These observations indicate that it is not the loss of [Arg327]GPIIb but the presence of His327 or a negatively charged residue like Glu at position 327 of GPIIb that prevents the surface exposure of GPIIb-IIIa heterodimers. In contrast, changing Gln344, the homologue to Arg327 in the alpha-subunit of the vitronectin receptor, to His did not prevent the surface expression of alphav-GPIIIa complexes. Thus the conformational constraint imposed by His327 seems to be rather specific for the heterodimerization and/or processing of GPIIb-IIIa complexes.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Arginine,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/Histidine,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Platelet Glycoprotein GPIIb-IIIa...,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Vitronectin,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Nov
|
| pubmed:issn |
0002-9513
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
275
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
C1239-46
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:9814972-Amino Acid Sequence,
pubmed-meshheading:9814972-Amino Acid Substitution,
pubmed-meshheading:9814972-Animals,
pubmed-meshheading:9814972-Arginine,
pubmed-meshheading:9814972-Base Sequence,
pubmed-meshheading:9814972-CHO Cells,
pubmed-meshheading:9814972-Cell Membrane,
pubmed-meshheading:9814972-Cricetinae,
pubmed-meshheading:9814972-DNA Primers,
pubmed-meshheading:9814972-Gene Expression Regulation,
pubmed-meshheading:9814972-Histidine,
pubmed-meshheading:9814972-Humans,
pubmed-meshheading:9814972-Macromolecular Substances,
pubmed-meshheading:9814972-Mice,
pubmed-meshheading:9814972-Molecular Sequence Data,
pubmed-meshheading:9814972-Mutagenesis, Site-Directed,
pubmed-meshheading:9814972-Platelet Glycoprotein GPIIb-IIIa Complex,
pubmed-meshheading:9814972-Point Mutation,
pubmed-meshheading:9814972-Polymerase Chain Reaction,
pubmed-meshheading:9814972-Receptors, Vitronectin,
pubmed-meshheading:9814972-Recombinant Proteins,
pubmed-meshheading:9814972-Sequence Alignment,
pubmed-meshheading:9814972-Sequence Homology, Amino Acid,
pubmed-meshheading:9814972-Transfection
|
| pubmed:year |
1998
|
| pubmed:articleTitle |
Role of the alpha-subunit 326GRV sequence in the surface expression of fibrinogen and vitronectin receptors.
|
| pubmed:affiliation |
Department of Pathophysiology and Human Molecular Genetics, Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas, Velázquez 144, 28006-Madrid, Spain.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|