Phosphorylation of αB-Crystallin and HSP27 Is Induced by Similar Stressors in HeLa Cells

Three members of the small heat shock protein family, αA-, αB-crystallin, and HSP27, confer thermoresistance upon their overexpression in mammalian cells. Phosphorylation, in conjunction with the molecular chaperone-like activity of these small HSPs, is believed to be important for thisin situfuncti...

Full description

Saved in:
Bibliographic Details
Published in:Biochemical and biophysical research communications 1998-06, Vol.247 (2), p.518-523
Main Authors: van den IJssel, Paul R.L.A., Overkamp, Perry, Bloemendal, Hans, de Jong, Wilfried W.
Format: Article
Language:English
Subjects:
heat shock protein
phosphorylation
stress
αA-crystallin
αB-crystallin
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Three members of the small heat shock protein family, αA-, αB-crystallin, and HSP27, confer thermoresistance upon their overexpression in mammalian cells. Phosphorylation, in conjunction with the molecular chaperone-like activity of these small HSPs, is believed to be important for thisin situfunctional property. We here report the influence of heat shock and other kinds of stress on the phosphorylation of αA-, αB-crystallin, and HSP27 in stably transfected HeLa cells. It is observed that αB-crystallin becomes phosphorylated upon exposure to the same inducers as is HSP27, although to a lesser extent. In contrast, phosphorylation of αA-crystallin is very low upon heat stress and even absent when other stressors are used. This indicates that phosphorylation is not in all instances essential for the stress protective functioning of the various small HSPs.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.1998.8699