Toxicant‐induced alterations in two‐dimensional electrophoretic patterns of hepatic and renal stress proteins
- 1 January 1996
- journal article
- two dimensional-electrophoresis
- Published by Wiley in Electrophoresis
- Vol. 17 (1) , 198-202
- https://doi.org/10.1002/elps.1150170132
Abstract
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.Keywords
This publication has 20 references indexed in Scilit:
- The Hepatocarcinogen Methapyrilene but Not the Analog Pyrilamine Induces Sustained Hepatocellular Replication and Protein Alterations in F344 Rats in a 13-Week Feed StudyToxicology and Applied Pharmacology, 1995
- Two‐dimensional electrophoretic mapping of hepatic and renal stress proteinsElectrophoresis, 1995
- Modification of Hepatic Immunoglobulin Heavy Chain Binding Protein (BiP/Grp78) Following Exposure to Structurally Diverse Peroxisome ProliferatorsFundamental and Applied Toxicology, 1994
- Dose-responses in rat hepatic protein modification and expression following exposure to the rat hepatocarcinogen methapyrileneCarcinogenesis: Integrative Cancer Research, 1994
- THE FUNCTION OF HEAT-SHOCK PROTEINS IN STRESS TOLERANCE: DEGRADATION AND REACTIVATION OF DAMAGED PROTEINSAnnual Review of Genetics, 1993
- The E. coli dnaK gene product, the hsp70 homolog, can reactivate heat-inactivated RNA polymerase in an ATP hydrolysis-dependent mannerCell, 1990
- Protein Translocation Across MembranesScience, 1988
- Hsp108, a novel heat shock inducible protein of chickenBiochemistry, 1986
- Toxic effects of nonadecafluoro-n-decanoic acid in ratsToxicology and Applied Pharmacology, 1986
- Speculations on the functions of the major heat shock and glucose-regulated proteinsCell, 1986