Divergence of intracellular and extracellular HSP72 in type 2 diabetes: does fat matter?

Title
Divergence of intracellular and extracellular HSP72 in type 2 diabetes: does fat matter?
Publication Date
2012
Author(s)
Rodrigues-Krause, Josianne
Krause, Mauricio
O'Hagan, Ciara
de Vito, Giuseppe
Boreham, Colin
Murphy, Colin
Newsholme, Philip
Colleran, Gerard
Type of document
Journal Article
Language
en
Entity Type
Publication
Publisher
Springer Netherlands
Place of publication
Netherlands
DOI
10.1007/s12192-011-0319-x
UNE publication id
une:16728
Abstract
Mammalian cells have developed a range of adaptations to survive against acute and prolonged (but not lethal) stresses (Beckmann et al. 1992). Among these adaptations, the heat shock response is the most conserved, being found in all prokaryotes and eukaryotes (Locke and Noble 1995). Heat shock proteins (HSPs) are considered part of a family of proteins known as "stress proteins" since their expression is induced by a wide range of stressors, such as oxidative stress (Krause et al. 2007), thermal stress (Yang et al. 1996), ischaemia (Richard et al. 1996), exercise (Krause et al. 2007), metabolic stress (Beckmann et al. 1992) and many others. The genes encoding Hsps are highly conserved, and many of these genes and their protein products can be assigned to different families on the basis of their typical molecular weight (kDa): HSP110 (or officially named HSPH), HSP90 (or HSPC), HSP70 (or HSPA), HSP60 (or HSPD1), HSP40 (or DNAJ) and small hsp families (HSPB) (Kampinga et al. 2009). In eukaryotes, many families comprise multiple members that differ in inducibility, intracellular localization and function (Feder and Hofmann 1999).
Link
Citation
Cell Stress and Chaperones, 17(3), p. 293-302
ISSN
1466-1268
1355-8145
Start page
293
End page
302

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