Linked Life Data

17435113

Source:http://linkedlifedata.com/resource/pubmed/id/17435113

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2007-7-23
pubmed:abstractText
Activated coagulation factor XIII (FXIIIa) cross-links the gamma-chains of fibrin early in clot formation. Cross-linking of the alpha-chains occurs more slowly, leading to high molecular weight multimer formations that can also contain gamma-chains. To study the contribution of FXIIIa-induced gamma-chain cross-linking on fibrin structure and function, we created 2 recombinant fibrinogens (gammaQ398N/Q399N/K406R and gammaK406R) that modify the gamma-chain cross-linking process. In gammaK406R, gamma-dimer cross-links were absent, but FXIIIa produced a cross-linking pattern similar to that observed in tissue transglutaminase cross-linked fibrin(ogen) with mainly alpha-gamma cross-links. In Q398N/Q399N/K406R, cross-links with any gamma-chain involvement were completely absent, and only alpha-chain cross-linking occurred. Upon cross-linking, recombinant normal fibrin yielded a 3.5-fold increase in stiffness, compared with a 2.5-fold increase by alpha-chain cross-linking alone (gammaQ398N/Q399N/K406R). gammaK406R fibrin showed a 1.5-fold increase in stiffness after cross-linking. No major differences in clot morphology, polymerization, and lysis rates were observed, although fiber diameter was slightly lower in cross-linked normal fibrin relative to the variants. Our results show that gamma-chain cross-linking contributes significantly to clot stiffness, in particular through gamma-dimer formation; alpha-gamma hybrid cross-links had the smallest impact on clot stiffness.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0006-4971
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
110
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
902-7
pubmed:dateRevised
2007-12-3
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Functional analysis of fibrin {gamma}-chain cross-linking by activated factor XIII: determination of a cross-linking pattern that maximizes clot stiffness.
pubmed:affiliation
Academic Unit of Molecular Vascular Medicine, Leeds Institute for Genetics, Health and Therapeutics, Clarendon Way, University of Leeds, UK.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural