| pubmed-article:10375689 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10375689 | lifeskim:mentions | umls-concept:C0010453 | lld:lifeskim |
| pubmed-article:10375689 | lifeskim:mentions | umls-concept:C0042666 | lld:lifeskim |
| pubmed-article:10375689 | lifeskim:mentions | umls-concept:C0017626 | lld:lifeskim |
| pubmed-article:10375689 | lifeskim:mentions | umls-concept:C0004112 | lld:lifeskim |
| pubmed-article:10375689 | lifeskim:mentions | umls-concept:C0205101 | lld:lifeskim |
| pubmed-article:10375689 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:10375689 | lifeskim:mentions | umls-concept:C0018847 | lld:lifeskim |
| pubmed-article:10375689 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:10375689 | lifeskim:mentions | umls-concept:C0205369 | lld:lifeskim |
| pubmed-article:10375689 | lifeskim:mentions | umls-concept:C0596235 | lld:lifeskim |
| pubmed-article:10375689 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:10375689 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:10375689 | pubmed:dateCreated | 1999-8-13 | lld:pubmed |
| pubmed-article:10375689 | pubmed:abstractText | The effect of external Ca2+ ([Ca2+]e) on the incorporation of [32P] into total protein, cytoskeletal proteins and the heat shock protein HSP27, was studied in primary cultures of astrocytes from the rat hippocampus. Zero [Ca2+]e increased total 32P-incorporation into astrocyte protein and when this was normalized to 100%, incorporation was significantly increased into glial fibrillary acidic protein (GFAP), vimentin (VIM) and HSP27. The difference in total 32P-incorporation between zero [Ca2+]e and 1 mM [Ca2+]e was reversed by incubation of the cells with the protein phosphatase inhibitor okadaic acid in the range 1-10 nM; higher concentrations of okadaic acid (50-100 nM) further increased total 32P-incorporation. In zero [Ca2+]e the non-specific channel blocker Co2+ (1 mM) decreased total 32P-incorporation by approximately 30%. The results were compared with a previous study [S.T. Wofchuk, R. Rodnight, Age-dependent changes in the regulation by external calcium ions of the phosphorylation of glial fibrillary acidic protein in slices of rat hippocampus, Dev. Brain Res. 85 (1995) 181-186] in which it was shown that in immature hippocampal slices zero [Ca2+]e compared with 1 mM [Ca2+]e increased 32P-incorporation into GFAP without changing total incorporation. The difference between the results for total 32P-incorporation obtained in cultured astrocytes and immature brain tissue was found to be related to the concentration of [Ca2+]e in the medium since in slices concentrations of [Ca2+]e higher than 1 mM progressively decreased total incorporation. The difference may reflect a higher Ca2+-permeability of the plasma membrane in cultured astrocytes and/or to the complex structure of the slice tissue. In two-dimensional electrophoresis HSP27, in contrast to GFAP and VIM, was separated into 3 immunodetectable isoforms only two of which were normally phosphorylated. After labelling in the presence of okadaic acid both immunodetectable and phosphorylated HSP27 focussed as a single polypeptide. Phorbol dibutyrate (1 microM) and zero [Ca2+]e stimulated the phosphorylation of both isoforms, but in the case of zero [Ca2+]e the effect on the more acidic isoform was proportionally greater. | lld:pubmed |
| pubmed-article:10375689 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10375689 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10375689 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10375689 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10375689 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10375689 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10375689 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10375689 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10375689 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10375689 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10375689 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10375689 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10375689 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10375689 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10375689 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:10375689 | pubmed:issn | 0006-8993 | lld:pubmed |
| pubmed-article:10375689 | pubmed:author | pubmed-author:RodnightRR | lld:pubmed |
| pubmed-article:10375689 | pubmed:author | pubmed-author:ValentinMM | lld:pubmed |
| pubmed-article:10375689 | pubmed:author | pubmed-author:KarkUU | lld:pubmed |
| pubmed-article:10375689 | pubmed:author | pubmed-author:WofchukS TST | lld:pubmed |
| pubmed-article:10375689 | pubmed:author | pubmed-author:SalbegoCC | lld:pubmed |
| pubmed-article:10375689 | pubmed:author | pubmed-author:GottfriedCC | lld:pubmed |
| pubmed-article:10375689 | pubmed:copyrightInfo | Copyright 1999 Published by Elsevier Science B.V. | lld:pubmed |
| pubmed-article:10375689 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10375689 | pubmed:day | 3 | lld:pubmed |
| pubmed-article:10375689 | pubmed:volume | 833 | lld:pubmed |
| pubmed-article:10375689 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10375689 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10375689 | pubmed:pagination | 142-9 | lld:pubmed |
| pubmed-article:10375689 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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| pubmed-article:10375689 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10375689 | pubmed:articleTitle | Regulation of protein phosphorylation in astrocyte cultures by external calcium ions: specific effects on the phosphorylation of glial fibrillary acidic protein (GFAP), vimentin and heat shock protein 27 (HSP27). | lld:pubmed |
| pubmed-article:10375689 | pubmed:affiliation | Departamento de Bioquímica, UFRGS, Instituto de Ciências Básicas da Saúde, Rua Ramiro Barcelos 2600-Anexo, 90.035.003, Porto Alegre, RS, Brazil. | lld:pubmed |
| pubmed-article:10375689 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10375689 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
