| Proteoglycan synthesis is increased in cells with impaired clathrin-dependent endocytosis. | |
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MedLine Citation:
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PMID: 11148135 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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A Llorente; K Prydz; M Sprangers; G Skretting; S O Kolset; K Sandvig |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Journal of cell science Volume: 114 ISSN: 0021-9533 ISO Abbreviation: J. Cell. Sci. Publication Date: 2001 Jan |
Date Detail:
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Created Date: 2001-01-26 Completed Date: 2001-05-17 Revised Date: 2009-11-19 |
Medline Journal Info:
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Nlm Unique ID: 0052457 Medline TA: J Cell Sci Country: England |
Other Details:
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Languages: eng Pagination: 335-43 Citation Subset: IM |
Affiliation:
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Department of Biochemistry, The Norwegian Radium Hospital, Montebello, Norway. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Cell Line Chondroitin ABC Lyase Chromatography, Gel Chromatography, Ion Exchange Clathrin / genetics, metabolism* Cricetinae Cyclic AMP / metabolism Cyclic AMP-Dependent Protein Kinases / metabolism Dynamins Endocytosis / physiology* Fibroblast Growth Factor 1 / metabolism GTP Phosphohydrolases / genetics, metabolism Hela Cells Humans Leucine / metabolism Protein Kinase C / metabolism Proteoglycans / biosynthesis*, isolation & purification Sulfates / metabolism Sulfur Radioisotopes Transcription, Genetic Transfection Transferrin / metabolism Tritium |
| Chemical | |
Reg. No./Substance:
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0/Clathrin; 0/Proteoglycans; 0/Sulfates; 0/Sulfur Radioisotopes; 10028-17-8/Tritium; 104781-85-3/Fibroblast Growth Factor 1; 11096-37-0/Transferrin; 60-92-4/Cyclic AMP; 61-90-5/Leucine; EC 2.7.11.11/Cyclic AMP-Dependent Protein Kinases; EC 2.7.11.13/Protein Kinase C; EC 3.6.1.-/GTP Phosphohydrolases; EC 3.6.5.5/Dynamins; EC 4.2.2.20/Chondroitin ABC Lyase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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