PMID- 10529400
OWN - NLM
STAT- MEDLINE
DCOM- 19991207
LR  - 20061115
IS  - 0006-291X (Print)
IS  - 0006-291X (Linking)
VI  - 264
IP  - 2
DP  - 1999 Oct 22
TI  - Akt phosphorylation site found in human caspase-9 is absent in mouse caspase-9.
PG  - 550-5
AB  - Caspase-9 is one caspase upstream of caspase-3 and its activation is stimulated
      by Apaf-1/cytochrome c and inhibited by Akt signals. BAD phosphorylation by Akt
      is an essential step for growth factor-mediated inhibition of caspase activation.
      Recently, it was shown that human caspase-9 is phosphorylated by Akt and that its
      protease activity is reduced. To clarify the molecular mechanism of regulation of
      caspase-9 activation in neuronal apoptosis, we isolated two alternative splicing 
      products of mouse caspase-9, caspase-9L and caspase-9S, from a P19 embryonal
      carcinoma cell cDNA library. Curiously, the Akt phosphorylation sites and motifs 
      found in human caspase-9 were absent in both mouse caspase-9L and -9S. Mouse
      caspase-9 was not phosphorylated by activated Akt in vitro. Reverse transcription
      polymerase chain reaction analysis showed that the absent Akt motif is not
      limited to caspase-9 expressed in P19 embryonal carcinoma cells but also occurs
      in caspase-9 expressed in mouse, rat, and monkey. These results suggest that
      inhibition of caspase-9 activation by Akt-dependent phosphorylation is not
      generalized across species.
CI  - Copyright 1999 Academic Press.
FAU - Fujita, E
AU  - Fujita E
AD  - Division of Development and Differentiation, National Institute of Neuroscience, 
      NCNP, Kodaira, Tokyo, 187-8502, Japan.
FAU - Jinbo, A
AU  - Jinbo A
FAU - Matuzaki, H
AU  - Matuzaki H
FAU - Konishi, H
AU  - Konishi H
FAU - Kikkawa, U
AU  - Kikkawa U
FAU - Momoi, T
AU  - Momoi T
LA  - eng
SI  - GENBANK/AB019600
SI  - GENBANK/AB019601
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Biochem Biophys Res Commun
JT  - Biochemical and biophysical research communications
JID - 0372516
RN  - EC 3.4.22.- (Caspases)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Binding Sites
MH  - Caspases/chemistry/*genetics/metabolism
MH  - Cell Differentiation
MH  - Enzyme Activation
MH  - Gene Library
MH  - Humans
MH  - Mice
MH  - Molecular Sequence Data
MH  - Phosphorylation
MH  - Tumor Cells, Cultured
EDAT- 1999/10/26 00:00
MHDA- 1999/10/26 00:01
CRDT- 1999/10/26 00:00
PHST- 1999/10/26 00:00 [pubmed]
PHST- 1999/10/26 00:01 [medline]
PHST- 1999/10/26 00:00 [entrez]
AID - 10.1006/bbrc.1999.1387 [doi]
AID - S0006-291X(99)91387-6 [pii]
PST - ppublish
SO  - Biochem Biophys Res Commun. 1999 Oct 22;264(2):550-5. doi:
      10.1006/bbrc.1999.1387.