Two distinct 4-hydroxynonenal metabolizing glutathione S-transferase isozymes are differentially expressed in human tissues.
Biochem Biophys Res Commun
; 282(5): 1268-74, 2001 Apr 20.
Article
em En
| MEDLINE
| ID: mdl-11302754
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.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Aldeídos
/
Glutationa Transferase
Limite:
Humans
/
Male
Idioma:
En
Ano de publicação:
2001
Tipo de documento:
Article