Linked Life Data

18572013

Source:http://linkedlifedata.com/resource/pubmed/id/18572013

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2008-7-22
pubmed:abstractText
Calpastatin is an endogenous inhibitor of calpain, which has been implicated in various physiological and pathological processes. In the present study we determined the molecular and inhibitory properties of HMWCaMBP, calpastatin I, and calpastatin II. Western blot analysis with antibodies raised against either full length HMWCaMBP or internal peptides that are common to all isoforms showed that all three homologs have common antigenic epitopes. However, additional Western blot analysis with N-terminal specific antibodies showed that all three proteins are different at the N-terminal end. HMWCaMBP is clearly different from two other homologues, calpastatin I and II, at the N-terminal end. In addition, HMWCaMBP also showed the same affinities for m-calpain as calpastatin I and calpastatin II. Our findings suggest that HMWCaMBP is the homolog of calpastatin and may be a CaM-binding form of calpastatin.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1090-2104
pubmed:author
pubmed:issnType
Electronic
pubmed:day
29
pubmed:volume
373
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
387-91
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Cardiac high molecular weight calmodulin-binding protein is homologous to calpastatin I and calpastatin II.
pubmed:affiliation
Department of Pathology and Laboratory Medicine, College of Medicine, University of Saskatchewan, 103 Hospital Drive, Saskatoon, Saskatchewan, Canada S7N 0W8.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't