PMID- 10564664
OWN - NLM
STAT- MEDLINE
DCOM- 20000203
LR  - 20111117
IS  - 0021-9533 (Print)
IS  - 0021-9533 (Linking)
VI  - 112 ( Pt 23)
DP  - 1999 Dec
TI  - Caspase-3 and caspase-7 but not caspase-6 cleave Gas2 in vitro: implications for 
      microfilament reorganization during apoptosis.
PG  - 4475-82
AB  - Apoptosis is characterized by proteolysis of specific cellular proteins by a
      family of cystein proteases known as caspases. Gas2, a component of the
      microfilament system, is cleaved during apoptosis and the cleaved form
      specifically regulates microfilaments and cell shape changes. We now demonstrate 
      that Gas2 is a substrate of caspase-3 but not of caspase-6. Proteolytic
      processing both in vitro and in vivo is dependent on aspartic residue 279. Gas2
      cleavage was only partially impaired in apoptotic MCF-7 cells which lack
      caspase-3, thus indicating that different caspases can process Gas2 in vivo. In
      vitro Gas2 was processed, albeit with low affinity, by caspase-7 thus suggesting 
      that this caspase could be responsible for the incomplete Gas2 processing
      observed in UV treated MCF-7 cells. In vivo proteolysis of Gas2 was detected at
      an early stage of the apoptotic process when the cells are still adherent on the 
      substrate and it was coupled to the specific rearrangement of the microfilament
      characterizing cell death. Finally we also demonstrated that Gas2 in vitro binds 
      to F-actin, but this interaction was unaffected by the caspase-3 dependent
      proteolytic processing.
FAU - Sgorbissa, A
AU  - Sgorbissa A
AD  - Dipartimento di Scienze e Tecnologie Biomediche, Sezione di Biologia, Universita'
      di Udine, p.le Kolbe 4, Italy.
FAU - Benetti, R
AU  - Benetti R
FAU - Marzinotto, S
AU  - Marzinotto S
FAU - Schneider, C
AU  - Schneider C
FAU - Brancolini, C
AU  - Brancolini C
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - J Cell Sci
JT  - Journal of cell science
JID - 0052457
RN  - 0 (Actins)
RN  - 0 (GAS2 protein, human)
RN  - 0 (Gas2 protein, mouse)
RN  - 0 (Microfilament Proteins)
RN  - 0 (Recombinant Proteins)
RN  - EC 3.4.22.- (CASP3 protein, human)
RN  - EC 3.4.22.- (CASP6 protein, human)
RN  - EC 3.4.22.- (CASP7 protein, human)
RN  - EC 3.4.22.- (Casp3 protein, mouse)
RN  - EC 3.4.22.- (Casp6 protein, mouse)
RN  - EC 3.4.22.- (Casp7 protein, mouse)
RN  - EC 3.4.22.- (Caspase 3)
RN  - EC 3.4.22.- (Caspase 6)
RN  - EC 3.4.22.- (Caspase 7)
RN  - EC 3.4.22.- (Caspases)
SB  - IM
MH  - 3T3 Cells
MH  - Actin Cytoskeleton/*physiology/ultrastructure
MH  - Actins/metabolism
MH  - Animals
MH  - Apoptosis/*physiology
MH  - Breast Neoplasms
MH  - COS Cells
MH  - Caspase 3
MH  - Caspase 6
MH  - Caspase 7
MH  - Caspases/*metabolism
MH  - Female
MH  - Humans
MH  - Mice
MH  - Microfilament Proteins/*metabolism
MH  - Models, Biological
MH  - Recombinant Proteins/metabolism
MH  - Tumor Cells, Cultured
EDAT- 1999/11/24 00:00
MHDA- 1999/11/24 00:01
CRDT- 1999/11/24 00:00
PHST- 1999/11/24 00:00 [pubmed]
PHST- 1999/11/24 00:01 [medline]
PHST- 1999/11/24 00:00 [entrez]
PST - ppublish
SO  - J Cell Sci. 1999 Dec;112 ( Pt 23):4475-82.