Linked Life Data

8396485

Source:http://linkedlifedata.com/resource/pubmed/id/8396485

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1993-10-8
pubmed:abstractText
The activity of calcium-independent, calcium-dependent and calcium + phospholipid-dependent (protein kinase C) kinases in cytosol fractions from rat brain glial cells in primary culture and from subcultured astrocytes and in oligodendrocyte-type 2 astrocyte lineage glia has been measured with histone Type IIIS as substrate. Accurate measurement of protein kinase C activity was achieved only after chromatography of glial cytosols on DE-52 anion exchange columns to remove an endogenous inhibitor, identified tentatively as a phosphatase possibly of the protein phosphatase 2A class. The specific activity of protein kinase C in glial cell cytosol increased from 7.5 +/- 0.8 to 37.9 +/- 0.9 nmol32P incorporated/mg protein/10 min with increasing culture age. Protein kinase C activity in glial cytosol was significantly higher when primary cultures were grown in a defined medium lacking serum. Astrocyte-conditioned medium and phorbol esters caused a rapid translocation of glial cell protein kinase C activity from cytosol to membrane compartments. Myelin basic protein and protamine have been compared with histone as substrates for measurement of calcium-independent, calcium-dependent and calcium + phospholipid-dependent kinase activities in glial cytosol.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0197-0186
pubmed:author
pubmed:issnType
Print
pubmed:volume
23
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
87-94
pubmed:dateRevised
2009-9-29
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
The protein kinase C, calcium-independent and calcium-dependent kinase activities of glial cells in primary culture and subculture.
pubmed:affiliation
Department of Biology, University of York, England.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't