Chaperonin 60 | definition of Chaperonin 60 by Medical dictionary
chaperonin (redirected from Chaperonin 60)
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A molecular complex composed of multiple heat shock protein subunits that assemble into double ring structures. Chaperonins function within the cytoplasm to refold damaged proteins.
See also: heat shock proteins
[chaperon + -in]
Farlex Partner Medical Dictionary © Farlex 2012
Any of a family of large chaperone proteins that function chiefly to assist in the folding of newly synthesized proteins.
The American Heritage® Medical Dictionary Copyright © 2007, 2004 by Houghton Mifflin Company. Published by Houghton Mifflin Company. All rights reserved.Any of a group of 60 kD cytosolic chaperone proteins—e.g., heat shock protein 60, hsp60, GroEL—found in prokaryotes, the equivalent of the eukaryotic hsp60, mitochondria and plastids; chaparonins use energy from ATP hydrolysis to maintain proteins in the necessary folded configuration for proper function, thus having ‘foldase’ activity; other postulated roles for chaperonins include protein transport, oligomer assembly, DNA replication, mRNA turnover, and protection of the cell from various stresses; some chaperonins have auto-foldase activities
Segen's Medical Dictionary. © 2012 Farlex, Inc. All rights reserved.
References in periodicals archive
The chaperonin 60
encoding gene has been previously used for the identification of various Gram positive bacteria and a chaperonin sequence database containing a large collections of sequences including gene cpn60 of T.
Topics addressed in the 14 included presentations are the history of the understanding of cell stress; systems biology of molecular chaperone networks; unusual cellular disposition of the mitochondrial chaperones Hsp60, Hsp70, and Hsp10; cell surface molecular chaperones as endogenous modulators of innate immune response; cell stress proteins in extracellular fluids; Hsp60 and the immune system; novel immunotherapies from cell stress proteins; cell stress proteins as modulators of bacteria-host interactions; chaperonin 60
and microphage activation; extracellular functions of thioredoxin; Hsp27 as an anti-inflammatory and immunomodulatory stress protein acting to dampen immune function; and binding immunoglobulin protein as a potential new therapy for the treatment of rheumatoid arthritis.
A mitochondrial-like chaperonin 60
gene in Giardia lamblia: evidence that diplomonads once harbored an endosymbiont related to the progenitor of mitochondria.
Streptococcus iniae, a human and animal pathogen: specific identification by the chaperonin 60
gene identification method.