PMID- 10407139
OWN - NLM
STAT- MEDLINE
DCOM- 19990820
LR  - 20190610
IS  - 0006-3002 (Print)
IS  - 0006-3002 (Linking)
VI  - 1432
IP  - 2
DP  - 1999 Jul 13
TI  - New insights into an old protein: the functional diversity of mammalian 
      glyceraldehyde-3-phosphate dehydrogenase.
PG  - 159-84
AB  - Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was considered a classical 
      glycolytic protein examined for its pivotal role in energy production. It was 
      also used as a model protein for analysis of protein structure and enzyme 
      mechanisms. The GAPDH gene was utilized as a prototype for studies of genetic 
      organization, expression and regulation. However, recent evidence demonstrates 
      that mammalian GAPDH displays a number of diverse activities unrelated to its 
      glycolytic function. These include its role in membrane fusion, microtubule 
      bundling, phosphotransferase activity, nuclear RNA export, DNA replication and 
      DNA repair. These new activities may be related to the subcellular localization 
      and oligomeric structure of GAPDH in vivo. Furthermore, other investigations 
      suggest that GAPDH is involved in apoptosis, age-related neurodegenerative 
      disease, prostate cancer and viral pathogenesis. Intriguingly, GAPDH is also a 
      unique target of nitric oxide. This review discusses the functional diversity of 
      GAPDH in relation to its protein structure. The mechanisms through which 
      mammalian cells may utilize GAPDH amino acid sequences to provide these new 
      functions and to determine its intracellular localization are considered. The 
      interrelationship between new GAPDH activities and its role in cell pathologies 
      is addressed.
FAU - Sirover, M A
AU  - Sirover MA
AD  - Department of Pharmacology, Temple University School of Medicine, Philadelphia PA 
      19140, USA. msirover@astro.ocis.temple.edu
LA  - eng
GR  - AG14566/AG/NIA NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PT  - Review
PL  - Netherlands
TA  - Biochim Biophys Acta
JT  - Biochimica et biophysica acta
JID - 0217513
RN  - 0 (Tubulin)
RN  - 31C4KY9ESH (Nitric Oxide)
RN  - EC 1.2.1.- (Glyceraldehyde-3-Phosphate Dehydrogenases)
SB  - IM
MH  - Animals
MH  - Apoptosis
MH  - DNA Repair
MH  - Gene Expression
MH  - Glyceraldehyde-3-Phosphate Dehydrogenases/chemistry/genetics/*metabolism
MH  - Humans
MH  - Male
MH  - Membrane Fusion
MH  - Neurodegenerative Diseases/enzymology
MH  - Nitric Oxide/chemistry
MH  - Phosphorylation
MH  - Prostatic Neoplasms/enzymology
MH  - Structure-Activity Relationship
MH  - Tubulin/chemistry
RF  - 166
EDAT- 1999/07/17 00:00
MHDA- 1999/07/17 00:01
CRDT- 1999/07/17 00:00
PHST- 1999/07/17 00:00 [pubmed]
PHST- 1999/07/17 00:01 [medline]
PHST- 1999/07/17 00:00 [entrez]
AID - S0167-4838(99)00119-3 [pii]
AID - 10.1016/s0167-4838(99)00119-3 [doi]
PST - ppublish
SO  - Biochim Biophys Acta. 1999 Jul 13;1432(2):159-84. doi: 
      10.1016/s0167-4838(99)00119-3.