Am J Physiol Cell Physiol Fuel your research with LabChart
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Am J Physiol Cell Physiol 270: C903-C909, 1996;
0363-6143/96 $5.00
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Kegel, K. B.
Right arrow Articles by Goldman, J. E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kegel, K. B.
Right arrow Articles by Goldman, J. E.

AJP - Cell Physiology, Vol 270, Issue 3 C903-C909, Copyright © 1996 by American Physiological Society

ARTICLES

AlphaB-crystallin protects glial cells from hypertonic stress

K. B. Kegel, A. Iwaki, T. Iwaki and J. E. Goldman
Department of Pathology, Division of Neuropathology, Columbia University College of Physicians and Surgeons, New York, New York 10032, USA.

AlphaB-crystallin and the small stress protein, heat shock protein of 27 kDa (HSP27), share structural similarities and are coordinately induced by classical stress stimuli. We have recently observed that hypertonic stress produced by high NaCl concentrations selectively induces alphaB-crystallin in glial cells. To examine divergence of the functional properties of these two related proteins, we have constructed stable alphaB-crystallin-expressing glial cell lines from the U-251 MG glioma cells, which are normally deficient in alphaB-crystallin expression but constitutively express HSP27. These transfected cells lines are more resistant to acute hypertonic stress than the parental line from which they were derived. Moreover, the parental line acclimates to stepwise increases in hypertonicity and upregulates endogenous alphaB-crystallin in the process but not HSP27. The overexpression of HSP27 and alphaB-crystallin in NIH/3T3 fibroblasts, a cell line that normally expresses little alphaB-crystallin and no HSP27, does not result in increased survival. This suggests that alphaB-crystallin interacts with cell-type specific mechanisms to aid in protection from hypertonic stress.


This article has been cited by other articles:


Home page
 Am. J. Physiol. Cell Physiol.Home page
S. T. Lamitina and K. Strange
Transcriptional targets of DAF-16 insulin signaling pathway protect C. elegans from extreme hypertonic stress
Am J Physiol Cell Physiol, February 1, 2005; 288(2): C467 - C474.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Renal Physiol.Home page
F.-X. Beck, W. Neuhofer, and E. Muller
Molecular chaperones in the kidney: distribution, putative roles, and regulation
Am J Physiol Renal Physiol, August 1, 2000; 279(2): F203 - F215.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Pathol.Home page
Y. Koyama and J. E. Goldman
Formation of GFAP Cytoplasmic Inclusions in Astrocytes and Their Disaggregation by {alpha}B-Crystallin
Am. J. Pathol., May 1, 1999; 154(5): 1563 - 1572.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Visit Other APS Journals Online