Linked Life Data

15174099

Source:http://linkedlifedata.com/resource/pubmed/id/15174099

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2004-6-2
pubmed:abstractText
In the present work, we have analyzed the expression and subcellular localization of all the members of inositide-specific phospholipase C (PLCbeta) family in muscle differentiation, given that nuclear PLCbeta1 has been shown to be related to the differentiative process. Cell cultures of C2C12 myoblasts were induced to differentiate towards the phenotype of myotubes, which are also indicated as differentiated C2C12 cells. By means of immunochemical and immunocytochemical analysis, the expression and subcellular localization of PLCbeta1, beta2, beta3, beta4 have been assessed. As further characterization, we investigated the localization of PLCbeta isoenzymes in C2C12 cells by fusing their cDNA to enhanced green fluorescent protein (GFP). In myoblast culture, PLCbeta4 was the most expressed isoform in the cytoplasm, whereas PLCbeta1 and beta3 exhibited a lesser expression in this cell compartment. In nuclei of differentiated myotube culture, PLCbeta1 isoform was expressed at the highest extent. A marked decrease of PLCbeta4 expression in the cytoplasm of differentiated C2C12 cells was detected as compared to myoblasts. No relevant differences were evidenced as regards the expression of PLCbeta3 at both cytoplasmatic and nuclear level, whilst PLCbeta2 expression was almost undetectable. Therefore, we propose that the different subcellular expression of these PLC isoforms, namely the increase of nuclear PLCbeta1 and the decrease of cytoplasmatic PLCbeta4, during the establishment of myotube differentiation, is related to a spatial-temporal signaling event, involved in myogenic differentiation. Once again the subcellular localization appears to be a key step for the diverse signaling activity of PLCbetas.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9541
pubmed:author
pubmed:copyrightInfo
Copyright 2004 Wiley-Liss, Inc.
pubmed:issnType
Print
pubmed:volume
200
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
291-6
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:15174099-Animals, pubmed-meshheading:15174099-Antibodies, Monoclonal, pubmed-meshheading:15174099-Blotting, Western, pubmed-meshheading:15174099-Cell Differentiation, pubmed-meshheading:15174099-Cell Line, pubmed-meshheading:15174099-Cell Nucleus, pubmed-meshheading:15174099-Cytoplasm, pubmed-meshheading:15174099-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:15174099-Fluorescent Antibody Technique, Direct, pubmed-meshheading:15174099-Green Fluorescent Proteins, pubmed-meshheading:15174099-Immunohistochemistry, pubmed-meshheading:15174099-Isoenzymes, pubmed-meshheading:15174099-Luminescent Proteins, pubmed-meshheading:15174099-Mice, pubmed-meshheading:15174099-Myoblasts, pubmed-meshheading:15174099-Phospholipase C beta, pubmed-meshheading:15174099-Recombinant Fusion Proteins, pubmed-meshheading:15174099-Subcellular Fractions, pubmed-meshheading:15174099-Type C Phospholipases
pubmed:year
2004
pubmed:articleTitle
Expression of phospholipase C beta family isoenzymes in C2C12 myoblasts during terminal differentiation.
pubmed:affiliation
Cellular Signalling Laboratory, Department of Anatomical Science, University of Bologna, Bologna, Italy.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't