Linked Life Data

1337690

Source:http://linkedlifedata.com/resource/pubmed/id/1337690

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1993-3-15
pubmed:abstractText
Calpain, an inactive proenzyme, translocates from the cytosol to the membrane upon binding calcium, and is activated at the membrane in the presence of calcium and PIP2. Activated calpain is very unstable and presumably used only once. Thus the primary targets of calpain are considered to be membrane or membrane-associated proteins. Activation of protein kinase C (PKC) occurs concomitantly with calpain at the membrane. Calpain hydrolyzes only the active PKC species leading to downregulation. Calpain participates in the transcriptional regulation by controlling the levels of transcription factors, c-Jun and c-Fos. The calpain gene is a TPA-responsive gene and its expression is stimulated by activation of PKC. Modulation of cellular signal transduction by controlling the levels of the component proteins, such as PKC, c-Jun and c-Fos is one of the important physiological roles of calpain.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0077-8923
pubmed:author
pubmed:issnType
Print
pubmed:day
31
pubmed:volume
674
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
218-27
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Modulation of cellular signals by calpain.
pubmed:affiliation
Institute of Applied Microbiology, University of Tokyo, Japan.
pubmed:publicationType
Journal Article, Review