pubmed-article:2071672 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2071672 | lifeskim:mentions | umls-concept:C0018850 | lld:lifeskim |
pubmed-article:2071672 | lifeskim:mentions | umls-concept:C0026385 | lld:lifeskim |
pubmed-article:2071672 | lifeskim:mentions | umls-concept:C1999216 | lld:lifeskim |
pubmed-article:2071672 | lifeskim:mentions | umls-concept:C2244412 | lld:lifeskim |
pubmed-article:2071672 | lifeskim:mentions | umls-concept:C0205251 | lld:lifeskim |
pubmed-article:2071672 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:2071672 | pubmed:dateCreated | 1991-8-19 | lld:pubmed |
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pubmed-article:2071672 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2071672 | pubmed:abstractText | The 25-kD inhibitor of actin polymerization (25-kD IAP), isolated from turkey smooth muscle (Miron, T., M. Wilchek, and B. Geiger, 1988. Eur. J. Biochem. 178:543-553), is shown here to be a low molecular mass heat shock protein (HSP). Direct sequence analysis of the purified protein, as well as cloning and sequencing of the respective cDNA, disclosed a high degree of homology (67% identity, 80% similarity) to the human 27-kD HSP. Southern blot of chicken genomic DNA disclosed one band, suggesting the presence of a single gene, and Northern blot analysis revealed abundant transcript of approximately 1 kb in gizzard and heart tissues and lower amounts in total 18-d chick embryo RNA and in cultured fibroblasts. Exposure of the latter cells to 45 degrees C resulted in over 15-fold increase in the apparent level of the 25-kD IAP protein, confirming that its expression is regulated by heat shock. Immunofluorescent microscopic localization indicated that after heat treatment, the levels of the 25-kD IAP were markedly increased and the protein was apparently associated with cytoplasmic granules. Heat shock also had a transient, yet prominent, effect on the microfilament system in cultured fibroblasts: stress fibers disintegrated within 10-15 min after incubation at 45 degrees C, yet upon further incubation at the elevated temperature, conspicuous actin bundles were apparently reformed. | lld:pubmed |
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pubmed-article:2071672 | pubmed:language | eng | lld:pubmed |
pubmed-article:2071672 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2071672 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:2071672 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2071672 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:2071672 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2071672 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2071672 | pubmed:month | Jul | lld:pubmed |
pubmed-article:2071672 | pubmed:issn | 0021-9525 | lld:pubmed |
pubmed-article:2071672 | pubmed:author | pubmed-author:GeigerBB | lld:pubmed |
pubmed-article:2071672 | pubmed:author | pubmed-author:Vandekerckhov... | lld:pubmed |
pubmed-article:2071672 | pubmed:author | pubmed-author:WilchekMM | lld:pubmed |
pubmed-article:2071672 | pubmed:author | pubmed-author:MironTT | lld:pubmed |
pubmed-article:2071672 | pubmed:author | pubmed-author:Vancompernoll... | lld:pubmed |
pubmed-article:2071672 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2071672 | pubmed:volume | 114 | lld:pubmed |
pubmed-article:2071672 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2071672 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2071672 | pubmed:pagination | 255-61 | lld:pubmed |
pubmed-article:2071672 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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