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A proteomics approach to the mammalian kidney as a model for hyperosmotic stress
Author(s) -
Gabert Beverly Joy,
Kültz Dietmar
Publication year - 2008
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.22.1_supplement.1162.2
Subject(s) - renal papilla , renal cortex , major duodenal papilla , proteome , cortex (anatomy) , proteomics , biology , western blot , gel electrophoresis , kidney , microbiology and biotechnology , biochemistry , chemistry , anatomy , gene , endocrinology , neuroscience
The papilla of the mammalian kidney must tolerate varying degrees of hyperosmotic stress during urine concentration. Though functionally distinct the papilla is in close physical proximity to the renal cortex, an isoosmotic region. Proteomic differences between the papilla and cortex of C57BL6 mice were investigated using two‐dimensional gel electrophoresis to generate a whole proteome map for each tissue region. Delta2D software was used to quantify (n = 6) two‐fold or greater expression changes between the regions leading to detection of 211 cortex spots and 70 papilla spots. MALDI‐TOF/TOF mass spectrometry was used to sequence and identify tryptic peptides from the spots identifying 34 different cortex proteins and 19 proteins overexpressed in the papilla. Region specificity was substantiated by Western Blot confirmation. Proteins overrepresented in the cortex include enoyl CoA hydratase and malate dehydrogenase. Protein identifications of the renal papilla include alpha B crystallin, HSP 90, 14‐3‐3 protein and aldose reductase, which indicates that an array of stress response proteins contributes to offset the hostile environment in the papilla. PANTHER analysis of protein identifications was used to determine cellular functions, biological processes and molecular pathways characteristic of renal cells exposed to the stressful environment found in the papilla. Supported by NIH grant DK 59470.

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