PMID- 10469173
OWN - NLM
STAT- MEDLINE
DCOM- 19991012
LR  - 20171116
IS  - 1356-9597 (Print)
IS  - 1356-9597 (Linking)
VI  - 4
IP  - 7
DP  - 1999 Jul
TI  - Changes in nuclear morphology during apoptosis correlate with vimentin cleavage
      by different caspases located either upstream or downstream of Bcl-2 action.
PG  - 401-14
AB  - BACKGROUND: Upon Fas stimulation, procaspase-8 is recruited to the death-inducing
      signalling complex where autoactivation of caspase-8 occurs. Active caspase-8 can
      directly activate downstream caspases (e.g. caspase-3, 6, and 7) for the
      execution of apoptosis (mitochondria-independent pathway), while caspase-8 can
      also lead to executioner caspase activation through mitochondrial damage
      (mitochondria-dependent pathway). Caspase activation results in the dismantling
      of intracellular structure through specific proteolysis. RESULTS: We have found
      that an intermediate filament protein, vimentin, is cleaved at multiple sites by 
      caspases at an early stage of apoptosis in Jurkat cells. The sequences of the two
      major cleavage sites in vimentin (IDVD/V and DSVD/F) suggested that these sites
      are cleaved by caspase-8 and caspase-3, respectively, or by close homologues of
      these proteases. The IDVD/V site can be cleaved by caspase-8 in vitro, and its
      cleavage is less sensitive to DEVD-CHO and Bcl-2 over-expression than that of the
      DSVD/F site in Jurkat cells. Over-expression of a mutant vimentin which was
      insensitive to caspase cleavage at these sites delayed the appearance of
      apoptotic nuclei in Jurkat cells. CONCLUSION: The specific cleavage of vimentin
      can be used as an apoptotic marker of both apical- and mitochondria-dependent
      caspase activation. Apoptotic cleavage of vimentin most likely results in
      disruption of its filamentous structure, which may facilitate nuclear
      condensation and subsequent fragmentation through disruption of the cytoskeletal 
      network.
FAU - Morishima, N
AU  - Morishima N
AD  - Biodesign Research Group, RIKEN (the Institute of Physical and Chemical
      Research), 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.
      morishim@postman.riken.go.jp
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Genes Cells
JT  - Genes to cells : devoted to molecular & cellular mechanisms
JID - 9607379
RN  - 0 (Caspase Inhibitors)
RN  - 0 (Cysteine Proteinase Inhibitors)
RN  - 0 (Lamins)
RN  - 0 (Nuclear Proteins)
RN  - 0 (Proto-Oncogene Proteins c-bcl-2)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (Vimentin)
RN  - 0 (fas Receptor)
RN  - EC 2.4.2.30 (Poly(ADP-ribose) Polymerases)
RN  - EC 3.4.22.- (CASP3 protein, human)
RN  - EC 3.4.22.- (CASP8 protein, human)
RN  - EC 3.4.22.- (CASP9 protein, human)
RN  - EC 3.4.22.- (Calpain)
RN  - EC 3.4.22.- (Casp3 protein, mouse)
RN  - EC 3.4.22.- (Casp8 protein, mouse)
RN  - EC 3.4.22.- (Casp9 protein, mouse)
RN  - EC 3.4.22.- (Caspase 3)
RN  - EC 3.4.22.- (Caspase 8)
RN  - EC 3.4.22.- (Caspase 9)
RN  - EC 3.4.22.- (Caspases)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - *Apoptosis/drug effects
MH  - Calpain/antagonists & inhibitors/metabolism
MH  - Caspase 3
MH  - Caspase 8
MH  - Caspase 9
MH  - Caspase Inhibitors
MH  - Caspases/*metabolism
MH  - Cell Nucleus/drug effects/*metabolism
MH  - Cysteine Proteinase Inhibitors/pharmacology
MH  - HeLa Cells
MH  - Humans
MH  - Jurkat Cells
MH  - Lamins
MH  - Mice
MH  - Mutation
MH  - Nuclear Proteins/metabolism
MH  - Poly(ADP-ribose) Polymerases/metabolism
MH  - Proto-Oncogene Proteins c-bcl-2/genetics/*metabolism
MH  - Recombinant Fusion Proteins/chemistry/genetics/metabolism
MH  - Vimentin/chemistry/genetics/*metabolism
MH  - fas Receptor/*metabolism
EDAT- 1999/09/01 00:00
MHDA- 1999/09/01 00:01
CRDT- 1999/09/01 00:00
PHST- 1999/09/01 00:00 [pubmed]
PHST- 1999/09/01 00:01 [medline]
PHST- 1999/09/01 00:00 [entrez]
AID - gtc270 [pii]
PST - ppublish
SO  - Genes Cells. 1999 Jul;4(7):401-14.