Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1992-3-26
pubmed:abstractText
The in vitro degradation of individual neurofilament proteins by calpain and the effects of calmodulin on this proteolysis were studied. Two major results are reported. First, in the presence of calcium, calmodulin binds to the 200-kD neurofilament protein, but only weakly associates with the 150-kD neurofilament protein. The 70-kD neurofilament protein shows no specific calmodulin-binding. Second, calmodulin inhibits the calpain-mediated degradation of the 200-kD neurofilament protein, but does not alter the hydrolysis of the 150-kD and 70-kD neurofilament proteins. In addition, calmodulin is able to bind to the 200-kD neurofilament protein in the presence of other neurofilament subunits, indicating that calmodulin may play a role in the regulation of the metabolism of the 200-kD neurofilament protein in vivo.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0364-3190
pubmed:author
pubmed:issnType
Print
pubmed:volume
16
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
869-73
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
The regulatory role of calmodulin in the proteolysis of individual neurofilament proteins by calpain.
pubmed:affiliation
Department of Psychiatry and Behavioral Neurobiology, University of Alabama, Birmingham 35294.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't