Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2004-3-8
pubmed:abstractText
Transglutaminases (TGs) posttranslationally modify proteins by transamidation of specific polypeptide bond glutamines. This reaction results in deamination, polyamine incorporation or the formation of isopeptide bonds. Transglutaminase activity in the brain is increased in several neurodegenerative diseases. Because insoluble inclusions occur in these neurodegenerative diseases, it has been hypothesized that transglutaminase contributes to the formation of the inclusions by catalyzing the formation of isopeptide bonds resulting in crosslinked, insoluble protein aggregates. To demonstrate a role for transglutaminase in the formation of these inclusions, the primary approach has been to show increased immunoreactivity with antibodies that recognize the isopeptide bonds. However, the specificity of these antibodies for isopeptide crosslinks within or between proteins has not been clearly established. In this report we demonstrate that the two most commonly used isopeptide antibodies do not specifically recognize the isopeptide bonds formed by transglutaminase when they are within or between proteins.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0165-0270
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
134
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
151-8
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Immunoblot analysis reveals that isopeptide antibodies do not specifically recognize the epsilon-(gamma-glutamyl)lysine bonds formed by transglutaminase activity.
pubmed:affiliation
Department of Psychiatry, School of Medicine 1720, University of Alabama at Birmingham, 7th Avenue South, SC1061, Birmingham, AL 35294-0017, USA. gvwj@uab.edu
pubmed:publicationType
Journal Article, Comparative Study, In Vitro, Research Support, U.S. Gov't, P.H.S.