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Heat shock proteins within the mammalian cell cycle: Relationship to thermal sensitivity, thermal tolerance, and cell cycle progression
Author(s) -
Rice Glenn,
Laszlo Andrei,
Li Gloria,
Gray Joe,
Dewey William
Publication year - 1986
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1041260220
Subject(s) - heat shock protein , cell cycle , heat shock , gel electrophoresis , thermal shock , cell sorting , shock (circulatory) , chinese hamster ovary cell , biology , endogeny , chinese hamster , biophysics , microbiology and biotechnology , cell , flow cytometry , chemistry , biochemistry , dna , thermodynamics , gene , medicine , receptor , physics
Abstract We have measured endogenous and induced rates of 70‐kD, 89‐kD, and 110‐kD heat shock proteins in highly pure G1‐, S‐, or G2‐M phase fractions of Chinese hamster fibroblasts (CHO) separated by fluorescence‐activated cell sorting (FACS). Relative rates of synthesis of all three polypeptides as measured by two‐dimensional gel electrophoresis were similar throughout the cell cycle, and therefore, endogenous levels were unlikely to explain the thermal sensitivity of S‐phase cells. Distinct heterogeneity in induced rates of these polypeptides was noted in all phase fractions. Enhanced rates of 70‐kD polypeptide were measured in S and G2‐M as compared to G1 following heat shock. Little increase in either the 89‐kD or 110k‐kD heat shock proteins was observed in heated G1 cells. This heterogeneity in induced rates of synthesis was in contrast to the similarity in thermal tolerance expression kinetics between each phase. Finally, enhanced synthesis of these polypeptides appeared unrelated to regulation of either heat‐induced cell cycle delay or to the resumption of phase‐specific progression after heat shock as measured by simultaneous flow cytometric measurement of incorporated BrdUrd and DNA content.