Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2012:2012:185641.
doi: 10.6064/2012/185641. Epub 2012 Oct 9.

Pathology-dependent effects linked to small heat shock proteins expression: an update

A-P Arrigo  1
Affiliations
Review

Pathology-dependent effects linked to small heat shock proteins expression: an update

A-P Arrigo. Scientifica (Cairo). 2012.

Abstract

Small heat shock proteins (small Hsps) are stress-induced molecular chaperones that act as holdases towards polypeptides that have lost their folding in stress conditions or consequently of mutations in their coding sequence. A cellular protection against the deleterious effects mediated by damaged proteins is thus provided to cells. These chaperones are also highly expressed in response to protein conformational and inflammatory diseases and cancer pathologies. Through specific and reversible modifications in their phospho-oligomeric organization, small Hsps can chaperone appropriate client proteins in order to provide cells with resistance to different types of injuries or pathological conditions. By helping cells to better cope with their pathological status, their expression can be either beneficial, such as in diseases characterized by pathological cell degeneration, or deleterious when they are required for tumor cell survival. Moreover, small Hsps are actively released by cells and can act as immunogenic molecules that have dual effects depending on the pathology. The cellular consequences linked to their expression levels and relationships with other Hsps as well as therapeutic strategies are discussed in view of their dynamic structural organization required to interact with specific client polypeptides.

PubMed Disclaimer

Figures

Figure 1
Figure 1
Small Hsps. (a) Organization of human HspB1 (Hsp27) and HspB5 (αB-crystallin) protein sequences. N-terminal gray box: WD/EPF domain; N-terminal white box: conserved sequence; black box: alpha crystallin domain; C-terminal gray box: IXI/V motif; the C-terminal flexible domain is also indicated. P: phosphorylated serine residues. Amino acids number is indicated. (b) Description of the members of the human small heat shock family of proteins. The distant Hsp16.2 polypeptide contains only a fraction of the alpha-crystallin domain. Chaperone activity and inducibility by heat shock are indicated. (c) Tissue-specific expression of constitutive small Hsps (compilation of murine as well as some human data).
See this image and copyright information in PMC

Similar articles

See all similar articles

Cited by

See all "Cited by" articles

References

    1. Ritossa FM. Experimental activation of specific loci in polytene chromosomes of Drosophila. Experimental Cell Research. 1964;35(3):601–607. - PubMed
    1. Ritossa F. Discovery of the heat shock response. Cell Stress & Chaperones. 1996;1(2):97–98. - PMC - PubMed
    1. Tissiéres A, Mitchell HK, Tracy UM. Protein synthesis in salivary glands of Drosophila melanogaster: relation to chromosome puffs. Journal of Molecular Biology. 1974;84(3):389–398. - PubMed
    1. Craig EA. The stress response: changes in eukaryotic gene expression in response to environmental stress. Science. 1985;230(4727):800–801. - PubMed
    1. Craig EA. The heat shock response. CRC Critical Reviews in Biochemistry. 1985;18(3):239–280. - PubMed

LinkOut - more resources

  NODES
twitter 2