Linked Life Data

9657448

Source:http://linkedlifedata.com/resource/pubmed/id/9657448

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1998-10-16
pubmed:databankReference
pubmed:abstractText
The entire cDNA sequences of a novel snake venom platelet glycoprotein (GP) Ib-binding protein (BP) composed of an alpha/beta heterodimeric structure, termed mamushigin, from Agkistrodon halys blomhoffii were determined, that include the leader peptides (21/23 amino acid residues) and mature subunits (136/123 amino acid residues). The mature subunits of mamushigin are 37.5% identical, and showed a high degree of similarity (37.7-67.5% identity) with the respective subunits of group VII C-type lectins (19). The sequences of the leader peptides of the mamusigin subunits showed the highest similarity (alpha-73.9/beta-82.6%) with those of factor IX/X-BP from Trimeresurus flavoviridis, and the cleavage site residue in both proteins was the same Ala(-1). The GPIb-binding specificity of mamushigin is strongly supported by several lines of evidence, but mamushigin can directly aggregate normal platelets, similar to alboaggregin-B (AL-B) (1). This differs from other GPIb-BP's. In mamushigin-treated platelets, serotonin was not released, and flow cytometric analysis using a monoclonal antibody PAC-1 totally excluded platelet GPIIb/IIIa activation. Mamushigin enhanced platelet aggregation at low-shear stress, and this effect totally disappeared in the presence of GPIb-receptor blockers specific for von Willebrand factor binding, but not by GPIIb/IIIa-receptor blockers. At high-shear stress, mamushigin blocked platelet aggregation in a dose-dependent manner, as seen with other GPIb-BP's. This paper, therefore, describes the cDNA cloning and molecular characterization of mamushigin which has a different effect on platelet aggregation under different shear stress.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0340-6245
pubmed:author
pubmed:issnType
Print
pubmed:volume
79
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1199-207
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:9657448-Agkistrodon, pubmed-meshheading:9657448-Amino Acid Sequence, pubmed-meshheading:9657448-Animals, pubmed-meshheading:9657448-Base Sequence, pubmed-meshheading:9657448-Binding Sites, pubmed-meshheading:9657448-Blood Platelets, pubmed-meshheading:9657448-Carrier Proteins, pubmed-meshheading:9657448-Cloning, Molecular, pubmed-meshheading:9657448-Crotalid Venoms, pubmed-meshheading:9657448-DNA, Complementary, pubmed-meshheading:9657448-Dimerization, pubmed-meshheading:9657448-Molecular Sequence Data, pubmed-meshheading:9657448-Platelet Aggregation, pubmed-meshheading:9657448-Platelet Glycoprotein GPIb-IX Complex, pubmed-meshheading:9657448-Protein Binding, pubmed-meshheading:9657448-Protein Conformation, pubmed-meshheading:9657448-Protein Precursors, pubmed-meshheading:9657448-Protein Sorting Signals, pubmed-meshheading:9657448-Ristocetin, pubmed-meshheading:9657448-Sequence Alignment, pubmed-meshheading:9657448-Sequence Homology, Amino Acid, pubmed-meshheading:9657448-Species Specificity, pubmed-meshheading:9657448-Stress, Mechanical, pubmed-meshheading:9657448-Structure-Activity Relationship, pubmed-meshheading:9657448-Thrombasthenia
pubmed:year
1998
pubmed:articleTitle
The cDNA cloning and molecular characterization of a snake venom platelet glycoprotein Ib-binding protein, mamushigin, from Agkistrodon halys blomhoffii venom.
pubmed:affiliation
Department of Pediatrics and Blood Transfusion Medicine, Nara Medical University, Kashihara, Japan.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't