PMID- 10843779
OWN - NLM
STAT- MEDLINE
DCOM- 20000717
LR  - 20131121
IS  - 0014-4835 (Print)
IS  - 0014-4835 (Linking)
VI  - 70
IP  - 6
DP  - 2000 Jun
TI  - Modulation of lens glycolytic pathway by thioltransferase.
PG  - 745-53
AB  - The observation that the level of S-thiolated proteins (protein-thiol mixed 
      disulfides) was transiently increased in the lens epithelial cells correlation 
      with the transient inactivation of glyceraldehyde-3-phosphate dehydrogenase 
      (G-3PD), a key glycolytic enzyme, when the cells were treated with a bolus of 
      hydrogen peroxide, prompted our speculation that G-3PD may have been transiently 
      thiolated at the SH sensitive active center. In the meantime, thioltransferase 
      (TTase), a thiol regulating enzyme, whose activity remained constant under the 
      same condition, may be regulating G-3PD and other sulfhydryl-sensitive glycolytic 
      enzymes through thiol-disulfide exchange reactions ( Lou et al., 1998 ). To prove 
      this hypothesis, several purified glycolytic enzymes from a commercial source, 
      including hexokinase (HK), G-3PD, pyruvate kinase (PK) and fructose 
      1,6-bisphosphatase (FBPase), an enzyme in gluconeogenesis, were made into 
      protein-thiol mixed disulfide and used for this study. Glycolytic enzymes in 
      cultured rabbit lens epithelial cells pre-exposed to H(2)O(2)(0.5 m M for 15 min) 
      were also studied for this purpose. Recombinant human lens thioltransferase 
      (RHLT), which was isolated and purified previously in this laboratory, 
      reactivated these pure glycolytic enzymes inactivated by forming 
      protein-S-S-gluthathione (PSSG), protein-S-S-cysteine (PSSC) or, 
      protein-S-S-cysteamine after thiolating with oxidized glutathione, cystine or 
      cystamine respectively. RHLT also reactivated these enzymes in the cell extract 
      of cultured rabbit lens epithelial cells after being briefly exposed to 0.5 m M 
      H(2)O(2). The S-thiolation and dethiolation of FBPase however, showed an opposite 
      effect to that of glycolytic enzymes. These results suggest that TTase may 
      participate in the repair process of glycolytic enzymes during oxidative stress 
      and restore their activities in situ.
CI  - Copyright 2000 Academic Press.
FAU - Qiao, F
AU  - Qiao F
AD  - Center for Biotechnology and Department of Veterinary and Biomedical Sciences, 
      University of Nebraska-Lincoln, Lincoln, NE 68583-0905, USA.
FAU - Xing, K
AU  - Xing K
FAU - Lou, M F
AU  - Lou MF
LA  - eng
GR  - R0110595/PHS HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - England
TA  - Exp Eye Res
JT  - Experimental eye research
JID - 0370707
RN  - 0 (Glutaredoxins)
RN  - 0 (Recombinant Proteins)
RN  - 33X04XA5AT (Lactic Acid)
RN  - 8L70Q75FXE (Adenosine Triphosphate)
RN  - BBX060AN9V (Hydrogen Peroxide)
RN  - EC 1.- (Oxidoreductases)
RN  - EC 1.2.1.- (Glyceraldehyde-3-Phosphate Dehydrogenases)
RN  - EC 1.8.4.2 (Protein Disulfide Reductase (Glutathione))
RN  - EC 2.7.1.1 (Hexokinase)
RN  - EC 2.7.1.11 (Phosphofructokinase-1)
RN  - EC 2.7.1.40 (Pyruvate Kinase)
RN  - EC 3.1.3.11 (Fructose-Bisphosphatase)
RN  - K848JZ4886 (Cysteine)
SB  - IM
MH  - Adenosine Triphosphate/biosynthesis
MH  - Animals
MH  - Cells, Cultured
MH  - Cysteine/metabolism
MH  - Enzyme Activation
MH  - Epithelial Cells/metabolism
MH  - Fructose-Bisphosphatase/metabolism
MH  - Glutaredoxins
MH  - Glyceraldehyde-3-Phosphate Dehydrogenases/*metabolism
MH  - Glycolysis
MH  - Hexokinase/metabolism
MH  - Humans
MH  - Hydrogen Peroxide/pharmacology
MH  - Lactic Acid/biosynthesis
MH  - Lens, Crystalline/*metabolism
MH  - Oxidative Stress
MH  - Oxidoreductases/*pharmacology
MH  - Phosphofructokinase-1/metabolism
MH  - *Protein Disulfide Reductase (Glutathione)
MH  - Pyruvate Kinase/metabolism
MH  - Rabbits
MH  - Recombinant Proteins/metabolism
EDAT- 2000/06/14 09:00
MHDA- 2000/07/25 11:00
CRDT- 2000/06/14 09:00
PHST- 2000/06/14 09:00 [pubmed]
PHST- 2000/07/25 11:00 [medline]
PHST- 2000/06/14 09:00 [entrez]
AID - S0014-4835(00)90836-4 [pii]
AID - 10.1006/exer.2000.0836 [doi]
PST - ppublish
SO  - Exp Eye Res. 2000 Jun;70(6):745-53. doi: 10.1006/exer.2000.0836.