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Deficiency of S‐nitrosoglutathione reductase compromises expression of the ER stress‐related proteins in LPS‐treated liver
Author(s) -
Ozawa Kentaro,
Tsumoto Hiroki,
Tsujimoto Gozoh
Publication year - 2012
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.26.1_supplement.573.3
Subject(s) - s nitrosylation , reductase , carcinogenesis , s nitrosoglutathione , protein disulfide isomerase , chemistry , nitrosylation , chaperone (clinical) , nitric oxide , microbiology and biotechnology , biochemistry , enzyme , biology , glutathione , gene , cysteine , medicine , organic chemistry , pathology
Nitric oxide (NO) promotes tumor formation by inflicting damage to DNA, which could lead to mutations or other genomic rearrangements. Recently, we discovered that S‐nitrosoglutathione reductase (GSNOR) deficient mice (GSNOR KO) are prone to spontaneous tumor formation, suggesting that S‐nitrosylation might be involved in tumorigenesis. To clarify the mechanism of tumorigenesis in GSNOR KO, we compared the protein expression profiles of wild‐type and GSNOR KO following LPS‐treatment. We identified 19 up‐regulated and 19 down‐regulated proteins in the GSNOR KO using Two‐dimensional difference gel electrophoresis analysis and following mass spectrometry. Further immunoblot analysis revealed that several members of the protein disulfide‐isomerase (PDI) family were expressed at lower levels in the GSNOR KO and that there were also differences in the expression patterns of the ER chaperone isoforms. These results suggest that S‐nitrosylation could potentially regulate the expression of many proteins, including those of the chaperones and folding catalysts in the ER, under inflammatory conditions some of which may promote carcinogenesis induced by NO.