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Two distinct 4-hydroxynonenal metabolizing glutathione S-transferase isozymes are differentially expressed in human tissues.
- Source :
-
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2001 Apr 20; Vol. 282 (5), pp. 1268-74. - Publication Year :
- 2001
-
Abstract
- The two previously reported human glutathione S-transferase isozymes, hGST5.8 and hGSTA4-4, have been suggested to be similar because of their comparable activities toward 4-hydroxynonenal-GSH conjugation. Here, we demonstrate that hGST5.8 and hGSTA4-4 are distinct. Antibodies raised against hGSTA4-4 did not recognize hGST5.8, and antibodies raised against mouse GSTA4-4 that cross-react with hGST5.8 did not recognize hGSTA4-4. The pI value of hGSTA4-4 was found to be 8.4, as opposed to the pI value of 5.8 for hGST5.8. The two isozymes are differentially expressed in human tissues and there are significant differences in their kinetic properties. While both isozymes showed a strong expression in liver and testis, hGSTA4-4 was not detected in brain where hGST5.8 was present. In the pancreas, a strong expression of hGST5.8 was observed while hGSTA4-4 was barely detectable in this tissue.<br /> (Copyright 2001 Academic Press.)
- Subjects :
- Antibody Specificity
Blotting, Western
Brain enzymology
Brain Chemistry
Cell Line
Electrophoresis, Polyacrylamide Gel
Glutathione Transferase chemistry
Humans
Isoelectric Focusing
Isoenzymes chemistry
Isoenzymes metabolism
K562 Cells chemistry
K562 Cells enzymology
Liver chemistry
Liver enzymology
Male
Organ Specificity physiology
Pancreas chemistry
Pancreas enzymology
Substrate Specificity
Testis chemistry
Testis enzymology
Aldehydes metabolism
Glutathione Transferase metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0006-291X
- Volume :
- 282
- Issue :
- 5
- Database :
- MEDLINE
- Journal :
- Biochemical and biophysical research communications
- Publication Type :
- Academic Journal
- Accession number :
- 11302754
- Full Text :
- https://doi.org/10.1006/bbrc.2001.4707