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Science Forum Index » Life Extension Forum » More on thioredoxin
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| Tim |
 Posted: Fri Jan 09, 2004 2:40 pm |
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IUBMB Life. 2001 Jul;52(1-2):29-33. Related Articles, Links
Redox regulation by thioredoxin and thioredoxin-binding proteins.
Nishiyama A, Masutani H, Nakamura H, Nishinaka Y, Yodoi J.
Department of Biological Responses, Institute for Virus Research,
Kyoto University, Japan.
Recent works have shown the importance of reduction/oxidation (redox)
regulation in various biological phenomena. Thioredoxin is a 12-kDa
protein with redox-active dithiol in the active site -Cys-Gly-Pro-Cys-
and constitutes a major thiol reducing system, the thioredoxin system.
Thioredoxin plays multiple roles in cellular processes such as
proliferation or apoptosis. It also promotes DNA binding of
transcription factors such as NF-kappaB, AP-1, p53, and PEBP2.
Overexpression of thioredoxin suppresses the degradation of IkappaB
and the transactivation of NF-kappaB, whereas overexpression of
nuclear-targeted thioredoxin exhibits the enhancement of
NF-kappaB-dependent transactivation. ASK1, a MAP kinase kinase kinase
mediating the TNF-alpha signal has been identified as a thioredoxin
binding protein. Thioredoxin shows an inhibitory effect on the
TNF-alpha induced activation of ASK1 and p38 MAP kinase pathway. We
identified p40phox as the thioredoxin binding protein-1 (TBP-1) and
vitamin D3 up-regulated protein 1 (VDUP1) as the thioredoxin binding
protein-2 (TBP-2) by yeast two-hybrid system. TBP-2/VDUP1 negatively
regulates the expression and reducing activity of thioredoxin.
Thioredoxin interacting proteins may be involved in
thioredoxin-mediating redox regulation.
Publication Types:
Review
Review, Tutorial
PMID: 11795589 [PubMed - indexed for MEDLINE]
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