Linked Life Data

12391176

Source:http://linkedlifedata.com/resource/pubmed/id/12391176

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
2002-10-22
pubmed:abstractText
Incidents of hemolytic uremic syndrome (HUS) include a subset of patients that exhibit mutations in C factor H. These mutations cluster in the C-terminal domains of factor H where previous reports have identified polyanion and C3b-binding sites. In this study, we show that recombinant human factor H with deletions at the C-terminal end of the protein loses the ability to control the spontaneous activation of the alternative C pathway on host-like surfaces. For the pathology of HUS, the findings imply that mutations that disrupt the normal functions of the C-terminal domains prevent host polyanion recognition. The resulting uncontrolled activation of complement on susceptible host tissues appears to be the initiating event behind the acute renal failure of familial HUS patients.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0022-1767
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
169
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4702-6
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Cutting edge: localization of the host recognition functions of complement factor H at the carboxyl-terminal: implications for hemolytic uremic syndrome.
pubmed:affiliation
Department of Biochemistry, University of Texas Health Science Center, Tyler 75708, USA. michael.pangburn@uthct.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.