Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 2
pubmed:dateCreated
2001-1-26
pubmed:abstractText
Overexpression of a GTPase deficient dynamin mutant in HeLa dynK44A cells causes a block in clathrin-dependent endocytosis. When endocytosis is inhibited, these cells incorporate higher levels of [(35)S]sulfate into both cellular and secreted macromolecules and larger amounts of proteoglycans such as syndecan and perlecan are immunoprecipitated from [(35)S]sulfate-labelled lysates. Gel filtration and ion-exchange chromatography revealed that the increased [(35)S]sulfate incorporation into proteoglycans was not due to significant differences in size or density of negative charge of glycosaminoglycan chains attached to proteoglycan core proteins. On the other hand, measurements of the syndecan-1 mRNA level and of [(3)H]leucine-labelled perlecan after immunoprecipitation supported the idea that the increased [(35)S]sulfate incorporation into proteoglycans was due to a selective increase in the synthesis of proteoglycan core proteins. Interestingly, the activity of protein kinase C was increased in cells expressing mutant dynamin and inhibition of protein kinase C with BIM reduced the differences in [(35)S]sulfate incorporation between cells with normal and impaired clathrin-dependent endocytosis. Thus, the activation of protein kinase C observed upon inhibition of clathrin-dependent endocytosis may be responsible for the increased synthesis of proteoglycans.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Chondroitin ABC Lyase, http://linkedlifedata.com/resource/pubmed/chemical/Clathrin, http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP, http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP-Dependent Protein Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Dynamins, http://linkedlifedata.com/resource/pubmed/chemical/Fibroblast Growth Factor 1, http://linkedlifedata.com/resource/pubmed/chemical/GTP Phosphohydrolases, http://linkedlifedata.com/resource/pubmed/chemical/Leucine, http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C, http://linkedlifedata.com/resource/pubmed/chemical/Proteoglycans, http://linkedlifedata.com/resource/pubmed/chemical/Sulfates, http://linkedlifedata.com/resource/pubmed/chemical/Sulfur Radioisotopes, http://linkedlifedata.com/resource/pubmed/chemical/Transferrin, http://linkedlifedata.com/resource/pubmed/chemical/Tritium
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0021-9533
pubmed:author
pubmed:issnType
Print
pubmed:volume
114
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
335-43
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:11148135-Animals, pubmed-meshheading:11148135-Cell Line, pubmed-meshheading:11148135-Chondroitin ABC Lyase, pubmed-meshheading:11148135-Chromatography, Gel, pubmed-meshheading:11148135-Chromatography, Ion Exchange, pubmed-meshheading:11148135-Clathrin, pubmed-meshheading:11148135-Cricetinae, pubmed-meshheading:11148135-Cyclic AMP, pubmed-meshheading:11148135-Cyclic AMP-Dependent Protein Kinases, pubmed-meshheading:11148135-Dynamins, pubmed-meshheading:11148135-Endocytosis, pubmed-meshheading:11148135-Fibroblast Growth Factor 1, pubmed-meshheading:11148135-GTP Phosphohydrolases, pubmed-meshheading:11148135-HeLa Cells, pubmed-meshheading:11148135-Humans, pubmed-meshheading:11148135-Leucine, pubmed-meshheading:11148135-Protein Kinase C, pubmed-meshheading:11148135-Proteoglycans, pubmed-meshheading:11148135-Sulfates, pubmed-meshheading:11148135-Sulfur Radioisotopes, pubmed-meshheading:11148135-Transcription, Genetic, pubmed-meshheading:11148135-Transfection, pubmed-meshheading:11148135-Transferrin, pubmed-meshheading:11148135-Tritium
pubmed:year
2001
pubmed:articleTitle
Proteoglycan synthesis is increased in cells with impaired clathrin-dependent endocytosis.
pubmed:affiliation
Department of Biochemistry, The Norwegian Radium Hospital, Montebello, Norway.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't