HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) All Versions of this Article: M400184-MCP200v1 4/10/1445    most recent Submit a response Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Glossary Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Dihazi, H. Articles by Müller, G. A. Search for Related Content PubMed PubMed Citation Articles by Dihazi, H. Articles by Müller, G. A. Social Bookmarking                      What's this?

Molecular & Cellular Proteomics 4:1445-1458, 2005.
© 2005 by The American Society for Biochemistry and Molecular Biology, Inc.

---

Research

Proteomic Analysis of Cellular Response to Osmotic Stress in Thick Ascending Limb of Henle’s Loop (TALH) Cells^*

Hassan Dihazi^,,¶, Abdul R. Asif^,||, Nitin K. Agarwal, Yuliana Doncheva and Gerhard A. Müller

From the Departments of Nephrology and Rheumatology and ^|| Clinical Chemistry, Georg-August University Göttingen, Robert-Koch-Strasse 40, D-37075 Göttingen, Germany

Epithelial cells of the thick ascending limb of Henle’s loop (TALH cells) play a major role in the urinary concentrating mechanism. They are normally exposed to variable and often very high osmotic stress, which is particularly due to high sodium and chloride reabsorption and very low water permeability of the luminal membrane. It is already established that elevation of the activity of aldose reductase and hence an increase in intracellular sorbitol are indispensable for the osmotic adaptation and stability of the TALH cells. To identify new molecular factors potentially associated with the osmotic stress-resistant phenotype in kidney cells, TALH cells exhibiting low or high levels of resistance to osmotic stress were characterized using proteomic tools. Two-dimensional gel analysis showed a total number of 40 proteins that were differentially expressed in TALH cells under osmotic stress. Twenty-five proteins were overexpressed, whereas 15 proteins showed a down-regulation. Besides the sorbitol pathway enzyme aldose reductase, whose expression was 15 times increased, many other metabolic enzymes like glutathione S-transferase, malate dehydrogenase, lactate dehydrogenase, enolase, glyceraldehyde-3-phosphate dehydrogenase, and triose-phosphate isomerase were up-regulated. Among the cytoskeleton proteins and cytoskeleton-associated proteins vimentin, cytokeratin, tropomyosin 4, and annexins I, II, and V were up-regulated, whereas tubulin and tropomyosins 1, 2, and 3 were down-regulated. The heat shock proteins -crystallin chain B, HSP70, and HSP90 were found to be overexpressed. In contrast to the results in oxidative stress the endoplasmic reticulum stress proteins like glucose-regulated proteins (GRP78, GRP94, and GRP96), calreticulin, and protein-disulfide isomerase were down-regulated under hypertonic stress.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				V. Thongboonkerd Current status of renal and urinary proteomics: ready for routine clinical application? Nephrol. Dial. Transplant., January 1, 2010; 25(1): 11 - 16. [Full Text] [PDF]

				M. B. Burg, J. D. Ferraris, and N. I. Dmitrieva Cellular Response to Hyperosmotic Stresses Physiol Rev, October 1, 2007; 87(4): 1441 - 1474. [Abstract] [Full Text] [PDF]

				H. Dihazi, G. A. Muller, S. Lindner, M. Meyer, A. R. Asif, M. Oellerich, and F. Strutz Characterization of Diabetic Nephropathy by Urinary Proteomic Analysis: Identification of a Processed Ubiquitin Form as a Differentially Excreted Protein in Diabetic Nephropathy Patients Clin. Chem., September 1, 2007; 53(9): 1636 - 1645. [Abstract] [Full Text] [PDF]

				S. P. R. Rao, R. Wassell, M. A. Shaw, and K. Sharma Profiling of human mesangial cell subproteomes reveals a role for calmodulin in glucose uptake Am J Physiol Renal Physiol, April 1, 2007; 292(4): F1182 - F1189. [Abstract] [Full Text] [PDF]

				B. A. Burkhart, S. B. Kennett, and T. K. Archer Osmotic Stress-dependent Repression Is Mediated by Histone H3 Phosphorylation and Chromatin Structure J. Biol. Chem., February 16, 2007; 282(7): 4400 - 4407. [Abstract] [Full Text] [PDF]

				M. G. Janech, J. R. Raymond, and J. M. Arthur Proteomics in renal research Am J Physiol Renal Physiol, February 1, 2007; 292(2): F501 - F512. [Abstract] [Full Text] [PDF]

				J. D. Hoffert, T. Pisitkun, G. Wang, R.-F. Shen, and M. A. Knepper Quantitative phosphoproteomics of vasopressin-sensitive renal cells: Regulation of aquaporin-2 phosphorylation at two sites PNAS, May 2, 2006; 103(18): 7159 - 7164. [Abstract] [Full Text] [PDF]

				L. Tomanek HENLE'S LOOP AND THE OSMOTIC STRESS PROTEOME J. Exp. Biol., April 1, 2006; 209(7): vi - vi. [Full Text] [PDF]