Molecular chaperones in the kidney: distribution, putative roles, and regulation.

@article{Beck2000MolecularCI,
  title={Molecular chaperones in the kidney: distribution, putative roles, and regulation.},
  author={Franz-X. Beck and Wolfgang Neuhofer and Elisabetta Mueller},
  journal={American journal of physiology. Renal physiology},
  year={2000},
  volume={279 2},
  pages={F203-15}
}
Molecular chaperones are intracellular proteins that prevent inappropriate intra- and intermolecular interactions of polypetide chains. A specific group of highly conserved molecular chaperones are the heat shock proteins (HSPs), many of which are constitutively expressed but most of which are inducible by diverse (in some cases specific) stress factors. HSPs, either alone or in cooperation with "partner" chaperones, are involved in cellular processes as disparate as correct folding and… CONTINUE READING

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A specific group of highly conserved molecular chaperones are the heat shock proteins ( HSPs ) , many of which are constitutively expressed but most of which are inducible by diverse ( in some cases specific ) stress factors .
A specific group of highly conserved molecular chaperones are the heat shock proteins ( HSPs ) , many of which are constitutively expressed but most of which are inducible by diverse ( in some cases specific ) stress factors .
The characteristic distribution of individual HSPs in the kidney , and their response to different challenges , suggests that a number of HSPs may fulfill specific , kidney - related functions . HSP72 and the osmotic stress protein 94 ( Osp94 )
appear to participate in the adaptation of medullary cells to high extracellular salt and urea concentrations ; the small HSPs ( HSP25/27 and crystallins ) may be involved in the function of mesangial cells and podocytes and contribute to the volume - regulatory remodeling of the cytoskeleton in medullary cells during changes in extracellular tonicity .
appear to participate in the adaptation of medullary cells to high extracellular salt and urea concentrations ; the small HSPs ( HSP25/27 and crystallins ) may be involved in the function of mesangial cells and podocytes and contribute to the volume - regulatory remodeling of the cytoskeleton in medullary cells during changes in extracellular tonicity .
A specific group of highly conserved molecular chaperones are the heat shock proteins ( HSPs ) , many of which are constitutively expressed but most of which are inducible by diverse ( in some cases specific ) stress factors .
Molecular ChaperonesIs biochemical function of gene productHeat shock proteins
A specific group of highly conserved molecular chaperones are the heat shock proteins ( HSPs ) , many of which are constitutively expressed but most of which are inducible by diverse ( in some cases specific ) stress factors .
The characteristic distribution of individual HSPs in the kidney , and their response to different challenges , suggests that a number of HSPs may fulfill specific , kidney - related functions . HSP72 and the osmotic stress protein 94 ( Osp94 )
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