PMID- 12369901
OWN - NLM
STAT- MEDLINE
DCOM- 20021112
LR  - 20191025
IS  - 1389-2037 (Print)
IS  - 1389-2037 (Linking)
VI  - 2
IP  - 1
DP  - 2001 Mar
TI  - Protein thiol modification of glyceraldehyde-3-phosphate dehydrogenase and 
      caspase-3 by nitric oxide.
PG  - 61-72
AB  - The regulation of enzyme activity function is a major factor in the cellular 
      response to a changing environment. One mechanism of enzyme activity regulation 
      includes post-translational protein thiol modification by nitric oxide (NO) or 
      its redox species. Major routs used by NO to modify cysteine residues of proteins 
      include S-nitrosation, oxidation, mixed disulfide formation with glutathione, and 
      the covalent attachment of nucleotide cofactors, i.e NAD(+)/NADH. Critical thiol 
      centers serve as recognition sites for NO, thus channeling the NO signal through 
      post-translational modifications and oxidation into cellular functions. Here, we 
      summarize current knowledge on active site thiol modification of 
      glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and caspase-3 by nitric oxide. 
      Although very different in their cellular function, both enzymes contain highly 
      reactive cysteines which represent sensitive targets for NO. Our studies are 
      supportive of a potential role of S-nitrosation and mixed disulfide formation as 
      a general signaling mechanism that allows sensing of nitrosative stress. At the 
      same time, modification of GAPDH and caspase-3 by NO show the diversity of 
      mechanisms (S-nitrosation versus oxidations) that we are confronted with as a 
      result of NO delivery, especially comparing in vitro studies with cellular 
      systems. In the future it will be challenging to dissect how nitrosative and 
      oxidative signaling mechanisms overlap and how intracellular communication 
      systems allow their activation in a selective way.
FAU - Brune, B
AU  - Brune B
AD  - University of Erlangen-Nurnberg, Faculty of Medicine, Department of Medicine 
      IV-Experimental Division, Germany. bernhard.bruene@rzmil.uni-erlangen.de
FAU - Mohr, S
AU  - Mohr S
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Review
PL  - United Arab Emirates
TA  - Curr Protein Pept Sci
JT  - Current protein & peptide science
JID - 100960529
RN  - 0 (Sulfhydryl Compounds)
RN  - 0U46U6E8UK (NAD)
RN  - 31C4KY9ESH (Nitric Oxide)
RN  - EC 1.2.1.- (Glyceraldehyde-3-Phosphate Dehydrogenases)
RN  - EC 3.4.22.- (Caspase 3)
RN  - EC 3.4.22.- (Caspases)
RN  - GAN16C9B8O (Glutathione)
SB  - IM
MH  - Caspase 3
MH  - Caspases/*chemistry/*metabolism
MH  - Catalytic Domain
MH  - Glutathione/metabolism
MH  - Glyceraldehyde-3-Phosphate Dehydrogenases/*chemistry/*metabolism
MH  - NAD/metabolism
MH  - Nitric Oxide/*metabolism
MH  - Sulfhydryl Compounds/chemistry
RF  - 67
EDAT- 2002/10/09 04:00
MHDA- 2002/11/26 04:00
CRDT- 2002/10/09 04:00
PHST- 2002/10/09 04:00 [pubmed]
PHST- 2002/11/26 04:00 [medline]
PHST- 2002/10/09 04:00 [entrez]
AID - 10.2174/1389203013381206 [doi]
PST - ppublish
SO  - Curr Protein Pept Sci. 2001 Mar;2(1):61-72. doi: 10.2174/1389203013381206.