Linked Life Data

10823824

Source:http://linkedlifedata.com/resource/pubmed/id/10823824

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
33
pubmed:dateCreated
2000-9-21
pubmed:abstractText
We have reported that prothrombin (1 microm) is able to replace high molecular weight kininogen (45 nm) as a cofactor for the specific binding of factor XI to the platelet (Baglia, F. A., and Walsh, P. N. (1998) Biochemistry 37, 2271-2281). We have also determined that prothrombin fragment 2 binds to the Apple 1 domain of factor XI at or near the site where high molecular weight kininogen binds. A region of 31 amino acids derived from high molecular weight kininogen (HK31-mer) can also bind to factor XI (Tait, J. F., and Fujikawa, K. (1987) J. Biol. Chem. 262, 11651-11656). We therefore investigated the role of prothrombin fragment 2 and HK31-mer as cofactors in the binding of factor XI to activated platelets. Our experiments demonstrated that prothrombin fragment 2 (1 microm) or the HK31-mer (8 microm) are able to replace high molecular weight kininogen (45 nm) or prothrombin (1 microm) as cofactors for the binding of factor XI to the platelet. To localize the platelet binding site on factor XI, we used mutant full-length recombinant factor XI molecules in which the platelet binding site in the Apple 3 domain was altered by alanine scanning mutagenesis. The recombinant factor XI with alanine substitutions at positions Ser(248), Arg(250), Lys(255), Leu(257), Phe(260), or Gln(263) were defective in their ability to bind to activated platelets. Thus, the interaction of factor XI with platelets is mediated by the amino acid residues Ser(248), Arg(250), Lys(255), Leu(257), Phe(260), and Gln(263) within the Apple 3 domain.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
275
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
25139-45
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:10823824-Amino Acids, pubmed-meshheading:10823824-Arginine, pubmed-meshheading:10823824-Binding Sites, pubmed-meshheading:10823824-Blood Platelets, pubmed-meshheading:10823824-Cell Membrane, pubmed-meshheading:10823824-Dose-Response Relationship, Drug, pubmed-meshheading:10823824-Factor XI, pubmed-meshheading:10823824-Glutamine, pubmed-meshheading:10823824-Humans, pubmed-meshheading:10823824-Kinetics, pubmed-meshheading:10823824-Kininogens, pubmed-meshheading:10823824-Lysine, pubmed-meshheading:10823824-Models, Biological, pubmed-meshheading:10823824-Mutagenesis, Site-Directed, pubmed-meshheading:10823824-Peptide Fragments, pubmed-meshheading:10823824-Phenylalanine, pubmed-meshheading:10823824-Platelet Aggregation, pubmed-meshheading:10823824-Protein Binding, pubmed-meshheading:10823824-Protein Conformation, pubmed-meshheading:10823824-Protein Structure, Tertiary, pubmed-meshheading:10823824-Prothrombin, pubmed-meshheading:10823824-Recombinant Proteins, pubmed-meshheading:10823824-Surface Plasmon Resonance
pubmed:year
2000
pubmed:articleTitle
The role of high molecular weight kininogen and prothrombin as cofactors in the binding of factor XI A3 domain to the platelet surface.
pubmed:affiliation
Sol Sherry Thrombosis Research Center, Departments of Medicine and Biochemistry, Temple University School of Medicine, Philadelphia, PA 19140, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.