Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1989-9-11
pubmed:abstractText
Distinct sets of cellular proteins were labeled with [3H]myristic and [3H]palmitic acids in primary (rat neurons and astroglia) and continuous (murine N1E-115 neuroblastoma and rat C6 glioma) cell cultures derived from the nervous system. Both soluble and membrane proteins were modified by myristate in a hydroxylamine-stable (amide) linkage, while palmitoylated proteins were ester-linked and almost exclusively membrane bound. Chain elongation of both labeled fatty acids prior to acylation was observed, but no protein amide-linked [3H]myristate originating from [3H]palmitate was detected. Fatty acylation profiles differed considerably among most of the cell lines, except for rat astroglial and glioma cells in which myristoylated proteins appeared to be almost identical based on SDS gel electrophoresis. An unidentified 47 kDa myristoylated protein was labeled to a significantly greater extent in astroglial than in glioma cells; the expression of this protein could be related to transformation or development in cells of glial origin.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0364-3190
pubmed:author
pubmed:issnType
Print
pubmed:volume
14
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
503-9
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:2548106-Acylation, pubmed-meshheading:2548106-Animals, pubmed-meshheading:2548106-Calcineurin, pubmed-meshheading:2548106-Calmodulin-Binding Proteins, pubmed-meshheading:2548106-Cells, Cultured, pubmed-meshheading:2548106-Detergents, pubmed-meshheading:2548106-Membrane Proteins, pubmed-meshheading:2548106-Molecular Weight, pubmed-meshheading:2548106-Myristic Acid, pubmed-meshheading:2548106-Myristic Acids, pubmed-meshheading:2548106-Nerve Tissue Proteins, pubmed-meshheading:2548106-Neuroglia, pubmed-meshheading:2548106-Neurons, pubmed-meshheading:2548106-Palmitic Acid, pubmed-meshheading:2548106-Palmitic Acids, pubmed-meshheading:2548106-Phosphoprotein Phosphatases, pubmed-meshheading:2548106-Precipitin Tests, pubmed-meshheading:2548106-Protein Processing, Post-Translational, pubmed-meshheading:2548106-Rats, pubmed-meshheading:2548106-Tumor Cells, Cultured
pubmed:year
1989
pubmed:articleTitle
Cell-specific fatty acylation of proteins in cultured cells of neuronal and glial origin.
pubmed:affiliation
Department of Pediatrics, Dalhousie University, Halifax, Nova Scotia, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't