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Proteomic Comparison of Heart and Liver Mitochondria in Diabetes
Author(s) -
Johnson D. Thor,
Harris Robert A,
Balaban Robert A
Publication year - 2006
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.20.4.a65-b
Subject(s) - proteome , mitochondrion , skeletal muscle , endoplasmic reticulum , proteomics , biology , aldh2 , heat shock protein , biochemistry , downregulation and upregulation , aldehyde dehydrogenase , endocrinology , enzyme , gene
We seek to understand the protein changes inherent to diabetes, especially with respect to those of the mitochondria. We have quantified the relative expression differences that exist between the mitochondria of heart and liver. As a second step we are quantifying differences between the proteome and phospho‐proteome of diabetic vs. control rats in the heart, liver, and skeletal muscle. We evaluated differences using 2‐demensional gel electrophoresis with Dige(Amersham biosciences), and Pro‐Q(Molecular Probes) labeling and mass‐spec analysis for protein ids. The mitochondrial proteome of heart and liver are markedly different. Only two proteins were within 50 % of each other across samples. In screens of diabetic animals across heart, liver, and skeletal muscle evidence was found for changes that are not demonstrated in the literature. These include up‐regulation of the pyruvate dehydrogenase kinase isoform 3 and D‐dopachrome tautomerase, downregulation of endoplasmic reticulum protein 72, heat shock protein 60, 14.5 kDa translational inhibitor protein, and calmodulin, down‐regulation of major urinary protein and up‐regulation of very‐long chain acyl‐CoA dehydrogenase. We also found probable covalent modification of alcohol dehydrogenase L1 and the glucokinase regulatory protein. This data should provide new avenues of exploration of diabetes pathogenesis. This research was funded by NHLBI intramural research funds