PMID- 10448534
OWN - NLM
STAT- MEDLINE
DCOM- 19991004
LR  - 20151119
IS  - 0199-9885 (Print)
IS  - 0199-9885 (Linking)
VI  - 19
DP  - 1999
TI  - Characterization of glycosylphosphatidylinositiol-anchored, secreted, and
      intracellular vertebrate mono-ADP-ribosyltransferases.
PG  - 485-509
AB  - Mono-ADP-ribosylation is a posttranslational modification of proteins in which
      the ADP-ribose moiety of nicotinamide adenine dinucleotide is transferred to an
      acceptor amino acid. Five mammalian ADP-ribosyltransferases (ART1--ART5) have
      been cloned and expression is restricted to tissues such as cardiac and skeletal 
      muscle, leukocytes, brain, and testis. ART1 and ART2 are
      glycosylphosphatidylinositol (GPI)-anchored ectoenzymes. ART5 appears not to be
      GPI-linked and may be secreted. In skeletal muscle and lymphocytes, ART1 modifies
      specific members of the integrin family of adhesion molecules, suggesting that
      ADP-ribosylation affects cell-matrix or cell-cell interactions. In lymphocytes,
      ADP-ribosylation of surface proteins is associated with changes in p56lck
      tyrosine kinase-mediated signaling. The catalytic sites of bacterial toxins and
      vertebrate transferases have conserved structural features, consistent with a
      common reaction mechanism. ADP-ribosylation can be reversed by
      ADP-ribosylarginine hydrolases, resulting in the regeneration of free arginine.
      Thus, an ADP-ribosylation cycle may play a regulatory role in vertebrate tissues.
FAU - Okazaki, I J
AU  - Okazaki IJ
AD  - Pulmonary-Critical Care Medicine Branch, National Heart, Lung, and Blood
      Institute, National Institutes of Health, Bethesda, Maryland 20892-1434, USA.
      Okazaki@gwgate.nhlbi.nih.gov
FAU - Moss, J
AU  - Moss J
LA  - eng
PT  - Journal Article
PT  - Review
PL  - United States
TA  - Annu Rev Nutr
JT  - Annual review of nutrition
JID - 8209988
RN  - 0 (Enzyme Inhibitors)
RN  - 0 (Glycosylphosphatidylinositols)
RN  - 0 (Poly(ADP-ribose) Polymerase Inhibitors)
RN  - EC 2.4.2.- (ADP Ribose Transferases)
RN  - EC 2.4.2.30 (Poly(ADP-ribose) Polymerases)
RN  - EC 3.2.1.- (Glycoside Hydrolases)
RN  - EC 3.2.2.- (N-Glycosyl Hydrolases)
RN  - EC 3.2.2.19 (ADP-ribosylarginine hydrolase)
SB  - IM
MH  - *ADP Ribose Transferases
MH  - Animals
MH  - Birds
MH  - Conserved Sequence
MH  - Enzyme Inhibitors
MH  - Glycoside Hydrolases/chemistry/metabolism
MH  - Glycosylphosphatidylinositols/*metabolism
MH  - Humans
MH  - Molecular Sequence Data
MH  - *N-Glycosyl Hydrolases
MH  - Poly(ADP-ribose) Polymerase Inhibitors
MH  - Poly(ADP-ribose) Polymerases/chemistry/*metabolism
RF  - 110
EDAT- 1999/08/17 00:00
MHDA- 1999/08/17 00:01
CRDT- 1999/08/17 00:00
PHST- 1999/08/17 00:00 [pubmed]
PHST- 1999/08/17 00:01 [medline]
PHST- 1999/08/17 00:00 [entrez]
AID - 10.1146/annurev.nutr.19.1.485 [doi]
PST - ppublish
SO  - Annu Rev Nutr. 1999;19:485-509. doi: 10.1146/annurev.nutr.19.1.485.