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Quantitative proteomic comparison of mouse peroxisomes from liver and kidney
Author(s) -
Mi Jia,
Kirchner Eva,
Cristobal Susana
Publication year - 2007
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200600638
Subject(s) - peroxisome , proteome , biology , endoplasmic reticulum , biochemistry , proteomics , organelle , catabolism , mitochondrion , microbiology and biotechnology , metabolism , receptor , gene
The peroxisome plays a central role in the catabolic and anabolic pathways that contribute to the lipid homeostasis. Besides this main function, this organelle has gained functional diversity. Although several approaches have been used for peroxisomal proteome analysis, a quantitative protein expression analysis of peroxisomes from different tissues has not been elucidated yet. Here, we applied a 2‐DE‐based method on mouse liver and kidney peroxisomal enriched fractions to study the tissue‐dependent protein expression. Ninety‐one spots were identified from the 2‐DE maps from pH 3.0–10.0 and 51 spots from the basic range corresponding to 31 peroxisomal proteins, 10 putative peroxisomal, 6 cytosolic, 17 mitochondrial and 1 protein from endoplasmic reticulum. Based on the identification and on the equivalent quality of both tissue preparations, the differences emerging from the comparison could be quantified. In liver, proteins involved in pathways such as α‐ and β‐oxidation, isoprenoid biosynthesis, amino acid metabolism and purine and pirimidine metabolism were more abundant whereas in kidney, proteins from the straight‐chain fatty acid β‐oxidation were highly expressed. These results indicate that tissue‐specific functional classes of peroxisomal proteins could be relevant to study peroxisomal cellular responses or pathologies. Finally, a web‐based peroxisomal proteomic database was built.