Linked Life Data

9716268

Source:http://linkedlifedata.com/resource/pubmed/id/9716268

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1998-11-13
pubmed:abstractText
In muscle protein phosphatase 1 (PP1) is involved in growth factor signal transduction and metabolic regulations. Three isoforms of the catalytic subunit are found in mammalian cells (PP1alpha, PP1gamma1 and PP1delta), with potentially different functions. We investigated the changes in the PP1 isoforms in differentiating C2C12 myoblasts. Few hours after differentiation induction the soluble PP1 activity was reversibly increased, displaying a peak at 6h. This was due to activation mainly of PP1alpha, with no change in the immunodetected protein. A further indication of PP1alpha involvement came from the observation that electroporation of inactive PP1alpha into myoblasts induced a differentiation delay of at least 24h. Subsequently, starting from 9-12 h, the activities and protein levels of all the three soluble PP1 isoforms decreased, reaching a minimum around 48 h. By this time the cells had undergone morphological changes and myosin became immunodetectable. We conclude that PP1 may be involved in myoblast differentiation, based on: 1) its higher activity in myoblasts than in myocytes, 2) the reversible activation of soluble PP1alpha during the first 6h from differentiation induction, 3) the delay in differentiation onset following electroporation of inactive PP1alpha into myoblasts.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0171-9335
pubmed:author
pubmed:issnType
Print
pubmed:volume
76
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
212-9
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Protein phosphatase 1 isoforms in differentiating C2C12 myocytes.
pubmed:affiliation
Department of Biomedicine, University of Pisa, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't