Premium
Toxicant‐induced alterations in two‐dimensional electrophoretic patterns of hepatic and renal stress proteins
Author(s) -
Witzmann Frank A.,
Fultz Carla D.,
Lipscomb John C.
Publication year - 1996
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.1150170132
Subject(s) - toxicant , heat shock protein , hsp27 , hsp60 , hsp70 , polyacrylamide gel electrophoresis , chemistry , gel electrophoresis , biochemistry , protein disulfide isomerase , kidney , toxicity , in vivo , microbiology and biotechnology , biology , enzyme , endocrinology , genetics , gene , organic chemistry
Recent studies in this laboratory and by others suggest that two‐dimensional polyacrylamide gel electrophoresis of proteins (2‐DE) possesses significant utility in the detection of chemical toxicity and in providing information regarding toxic mechanism. After having identified a set of specific heat‐shock and glucose‐regulated proteins whose expression in rodent liver and kidney is highly conserved and constitutive, we compared the effect of in vivo exposure to perfluoro‐n‐octanoic acid and perfluoro‐ n ‐decanoic acid on their expression. The following stress proteins were identified, their x, y coordinate positions mapped, and abundance statistically analyzed and compared: hsp32, hsp60, hsc70, hsp70, hsp90, grp75, grp94, protein disulfide isomerase (PDI), and ER60. We report here that the stress response to perfluorocarboxylic acids is tissue‐, toxicant‐, and stress protein class‐specific and dose‐related. Furthermore, because nearly all of the proteins studied were constitutively expressed at detectable levels in both liver and kidney, the 2‐DE stress protein pattern may be suitable to future toxicologic screening applications.