PMID- 10419473
OWN - NLM
STAT- MEDLINE
DCOM- 19990819
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 31
DP  - 1999 Jul 30
TI  - Identification of thioredoxin-binding protein-2/vitamin D(3) up-regulated protein
      1 as a negative regulator of thioredoxin function and expression.
PG  - 21645-50
AB  - Recent works have shown the importance of reduction/oxidation (redox) regulation 
      in various biological phenomena. Thioredoxin (TRX) is one of the major components
      of the thiol reducing system and plays multiple roles in cellular processes such 
      as proliferation, apoptosis, and gene expression. To investigate the molecular
      mechanism of TRX action, we used a yeast two-hybrid system to identify
      TRX-binding proteins. One of the candidates, designated as thioredoxin-binding
      protein-2 (TBP-2), was identical to vitamin D(3) up-regulated protein 1 (VDUP1). 
      The association of TRX with TBP-2/VDUP1 was observed in vitro and in vivo.
      TBP-2/VDUP1 bound to reduced TRX but not to oxidized TRX nor to mutant TRX, in
      which two redox active cysteine residues are substituted by serine. Thus, the
      catalytic center of TRX seems to be important for the interaction. Insulin
      reducing activity of TRX was inhibited by the addition of recombinant TBP-2/VDUP1
      protein in vitro. In COS-7 and HEK293 cells transiently transfected with
      TBP-2/VDUP1 expression vector, decrease of insulin reducing activity of TRX and
      diminishment of TRX expression was observed. These results suggested that
      TBP-2/VDUP1 serves as a negative regulator of the biological function and
      expression of TRX. Treatment of HL-60 cells with 1alpha, 25-dihydroxyvitamin D(3)
      caused an increase of TBP-2/VDUP1 expression and down-regulation of the
      expression and the reducing activity of TRX. Therefore, the TRX-TBP-2/VDUP1
      interaction may be an important redox regulatory mechanism in cellular processes,
      including differentiation of myeloid and macrophage lineages.
FAU - Nishiyama, A
AU  - Nishiyama A
AD  - Department of Biological Responses, Institute for Virus Research, Kyoto
      University, Sakyo-ku, Kyoto 606-8507, Japan.
FAU - Matsui, M
AU  - Matsui M
FAU - Iwata, S
AU  - Iwata S
FAU - Hirota, K
AU  - Hirota K
FAU - Masutani, H
AU  - Masutani H
FAU - Nakamura, H
AU  - Nakamura H
FAU - Takagi, Y
AU  - Takagi Y
FAU - Sono, H
AU  - Sono H
FAU - Gon, Y
AU  - Gon Y
FAU - Yodoi, J
AU  - Yodoi J
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Carrier Proteins)
RN  - 0 (Recombinant Proteins)
RN  - 0 (TXNIP protein, human)
RN  - 52500-60-4 (Thioredoxins)
RN  - FXC9231JVH (Calcitriol)
SB  - IM
MH  - Animals
MH  - B-Lymphocytes/metabolism
MH  - COS Cells
MH  - Calcitriol/pharmacology
MH  - Carrier Proteins/genetics/*metabolism
MH  - Cell Line
MH  - Cloning, Molecular
MH  - Female
MH  - *Gene Expression Regulation
MH  - Gene Library
MH  - HL-60 Cells
MH  - Humans
MH  - Kidney
MH  - Kinetics
MH  - Placenta/metabolism
MH  - Pregnancy
MH  - Recombinant Proteins/metabolism
MH  - Saccharomyces cerevisiae/metabolism
MH  - Thioredoxins/*genetics/*metabolism
MH  - Transfection
EDAT- 1999/07/27 00:00
MHDA- 1999/07/27 00:01
CRDT- 1999/07/27 00:00
PHST- 1999/07/27 00:00 [pubmed]
PHST- 1999/07/27 00:01 [medline]
PHST- 1999/07/27 00:00 [entrez]
AID - 10.1074/jbc.274.31.21645 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Jul 30;274(31):21645-50. doi: 10.1074/jbc.274.31.21645.