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Submitted on November 23, 2004
Revised on May 20, 2005
Accepted on June 22, 2005

Proteomics analysis of cellular response to osmotic stress in TALH-cells

Hassan Dihazi, Asif Abdul Rahman, Nitin K. Agarwal, Yuliana Doncheva, and Gerhard A. Müller

Nephrology and Rheumatology, Georg-August University Goettingen, Göttingen 37075

Corresponding Author: dihazi{at}med.uni-goettingen.de

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. In order 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. 2D-gel analysis showed a total number of 40 proteins which were differentially expressed in TALH-cells under osmotic stress. Twenty five proteins were overexpressed, whereas fifteen proteins showed a down-regulation. Besides the sorbitol pathway enzyme aldose reducatase, whose expression was 15 times increased, many other metabolic enzymes like glutathione-S-transferase, malate dehydrogenase, lactate dehydrogenase, alpha enolase, GAPDH, and triose phosphate isomerase were upregulated. Among the cytoskeleton proteins and cytoskeleton associated proteins vimentin, cytokeratin tropomyosin 4 annexin I, II and V were upregulated, whereas tubulin, topomyosin 1, 2 and 3 were downregulated. The heat shock proteins alpha crystalin chain B, HSP70, and HSP90 were found to be overexpressed. In contrast to the results in oxidative stress the endoplasmic stress proteins like glucose regulated proteins (GRP78, GRP94, and GRP96), calreticulin, and protein disulphide isomerase were downregulated under hypertonic stress.


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