NDLI: Enhancement in amount of P1 (hsp60) in mutants of Chinese hamster ovary (CHO-K1) cells exhibiting increases in the A system of amino acid transport.

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Enhancement in amount of P1 (hsp60) in mutants of Chinese hamster ovary (CHO-K1) cells exhibiting increases in the A system of amino acid transport.

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Enhancement in amount of P1 (hsp60) in mutants of Chinese hamster ovary (CHO-K1) cells exhibiting increases in the A system of amino acid transport.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Englesberg, E. Jones, M. Gupta, R. S.
Description	Author Affiliation: Jones M ( University of California, Santa Barbara 93106.);
Abstract	Mutants of CHO-K1 cells with varied levels of A system activity, probably the result of increases in absolute amount of the A system transporter, have corresponding increases in levels of peptides banding at 62-66 and 29 kDa. Mutant alar4-H3.9, showing the highest increase of A system activity and of 62- to 66- and 29-kDa peptides, was selected for this study. The N terminus 16-amino acid sequence of the 62- to 66-kDa peptide(s) of this mutant showed between 80% and 100% identity with the mammalian mitochondrial 60-kDa heat shock protein P1 (hsp60). Two-dimensional gel electrophoresis of the 62- to 66-kDa band showed two major, a minor, and several smaller spots (of same mass but different pI values) for both wild type (WT) and mutant, with the two major spots being of greater density in the mutant. Immunoblots with antibody to P1 identified the two major and minor peptides as P1 related. Two-dimensional gels of whole cell extracts of the WT and alar4-H3.9 confirmed these findings and indicated that the two major bands of the mutant were 2.4 times as abundant as that found for the WT. A plasma membrane fraction of the mutant, exhibiting 4.8 times more A system activity than the WT, contained 3.6 times as much P1 as the WT. Immunoblots with antibodies to P1, mitochondrial malate dehydrogenase, and to the mitochondrial F1/F0-ATPase demonstrated that the increased amount of P1 observed in the mutant was not the result of increases in amount of mitochondrial protein. Northern blot analysis demonstrated that the mutant had 2.5 times as much mRNA for P1 as the WT. The close analogy with the relationship between A system and Na+,K(+)-ATPase suggests that there is a coordinate regulation of the A system of amino acid transport, Na+,K(+)-ATPase, and P1 protein, probably as a result of mutation in a shared regulatory element. The possible role of P1 in A system function is discussed.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	3
Volume Number	91
Language	English
Publisher	National Academy of Sciences
Publisher Date	1994-03-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Amino Acids Metabolism Heat-Shock Proteins Animals Biological Transport, Active Genetics CHO Cells Chaperonin 60 Cricetinae Mutation RNA, Messenger Sodium-Potassium-Exchanging ATPase Up-Regulation Comparative Study Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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