Document Detail


Prostaglandins with antiproliferative activity induce the synthesis of a heat shock protein in human cells.
MedLine Citation:
PMID:  2813398     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Prostaglandins (PGs) A1 and J2 were found to potently suppress the proliferation of human K562 erythroleukemia cells and to induce the synthesis of a 74-kDa protein (p74) that was identified as a heat shock protein related to the major 70-kDa heat shock protein group. p74 synthesis was stimulated at doses of PGA1 and PGJ2 that inhibited cell replication, and its accumulation ceased upon removal of the PG-induced proliferation block. PGs that did not affect K562 cell replication did not induce p74 synthesis. p74 was found to be localized mainly in the cytoplasm of PG-treated cells, but moderate amounts were found also in dense areas of the nucleus after PGJ2 treatment. p74 synthesis was not necessarily associated with cytotoxicity or with inhibition of cell protein synthesis. The results described support the hypothesis that synthesis of the 70-kDa heat shock proteins is associated with changes in cell proliferation. The observation that PGs can induce the synthesis of heat shock proteins expands our understanding of the mechanism of action of these compounds whose regulatory role is well known in many physiological phenomena, including the control of fever production.
Authors:
M G Santoro; E Garaci; C Amici
Related Documents :
7517408 - Recovery of nuclear matrix ultrastructure of interphase cho cells after heat shock.
1639478 - Hsp70 synthesis in schwann cells in response to heat shock and infection with mycobacte...
16878978 - Targeting heat shock proteins on cancer cells: selection, characterization, and cell-pe...
22220628 - Signaling from lysosomes enhances mitochondria-mediated photodynamic therapy in cancer ...
1445848 - Cell-surface fucosylation and magnetic resonance spectroscopy characterization of human...
21983708 - Improvement of specific growth rate of pichia pastoris for effective porcine interferon...
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.    
Journal Detail:
Title:  Proceedings of the National Academy of Sciences of the United States of America     Volume:  86     ISSN:  0027-8424     ISO Abbreviation:  Proc. Natl. Acad. Sci. U.S.A.     Publication Date:  1989 Nov 
Date Detail:
Created Date:  1989-12-08     Completed Date:  1989-12-08     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  7505876     Medline TA:  Proc Natl Acad Sci U S A     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  8407-11     Citation Subset:  IM    
Affiliation:
Institute of Experimental Medicine, Consiglio Nazionale delle Ricerche, Rome, Italy.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Cell Line
Heat-Shock Proteins / biosynthesis*,  isolation & purification
Humans
Immunoblotting
Leukemia, Myelogenous, Chronic, BCR-ABL Positive
Methionine / metabolism
Molecular Weight
Neoplasm Proteins / biosynthesis,  isolation & purification
Prostaglandins / pharmacology*
Prostaglandins A / pharmacology
Tumor Cells, Cultured / cytology*,  drug effects,  metabolism
Chemical
Reg. No./Substance:
0/Heat-Shock Proteins; 0/Neoplasm Proteins; 0/Prostaglandins; 0/Prostaglandins A; 14152-28-4/prostaglandin A1; 63-68-3/Methionine
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Expression in transgenic plants of a viral gene product that mediates insect transmission of potyvir...
Next Document:  Role of platelets in smooth muscle cell proliferation and migration after vascular injury in rat car...