PMID- 10453075
OWN - NLM
STAT- MEDLINE
DCOM- 19991004
LR  - 20061115
IS  - 1350-9047 (Print)
IS  - 1350-9047 (Linking)
VI  - 6
IP  - 7
DP  - 1999 Jul
TI  - Caspases: their intracellular localization and translocation during apoptosis.
PG  - 644-51
AB  - The activation of the caspase family of proteases has been detected in numerous
      cell systems and appears to function as a common pathway through which apoptotic 
      mechanisms may operate. Caspases are synthesized as precursors (pro-caspases) and
      are converted into mature enzymes by apoptotic signals. The effects of caspases
      in apoptosis are accomplished by the cleavage of numerous proteins located in
      different intracellular compartments. In the present study we have addressed the 
      question of the subcellular localization of different pro- and active caspases as
      well as several other proteins, such as Apaf-1, calpain and DFF, which also play 
      important roles in the apoptotic process. We found that at least three
      pro-caspases (pro-caspases-2, -3 and -9) were present in both the mitochondrial
      and cytosolic fractions of untreated Jurkat T lymphocytes. Only pro-caspase-2 was
      found in the nuclear fraction. Pro-caspases-7 and -8 were found only in the
      cytosolic fraction. In apoptotic cells, caspases-3, -8 and -9 were present in the
      cytosolic fraction, whereas caspases-3 and -9 were also found in the
      mitochondrial fraction and caspase-7 in the microsomal fraction. Caspases-2 and
      -3 were present in the nuclear fraction. The selective localization of
      pro-caspases in different subcellular compartments may play an important, but yet
      unknown, role in their activation. The translocation of active caspases to other 
      subcellular compartments appears to be critical for the development of the
      apoptotic process.
FAU - Zhivotovsky, B
AU  - Zhivotovsky B
AD  - Division of Toxicology, Institute of Environmental Medicine, Karolinska
      Institutet, Box 210, S-171 77 Stockholm, Sweden.
FAU - Samali, A
AU  - Samali A
FAU - Gahm, A
AU  - Gahm A
FAU - Orrenius, S
AU  - Orrenius S
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Cell Death Differ
JT  - Cell death and differentiation
JID - 9437445
RN  - 0 (APAF1 protein, human)
RN  - 0 (Apoptotic Protease-Activating Factor 1)
RN  - 0 (DNA fragmentation factor, human)
RN  - 0 (Enzyme Precursors)
RN  - 0 (Proteins)
RN  - EC 3.4.22.- (Calpain)
RN  - EC 3.4.22.- (Caspases)
SB  - IM
MH  - Apoptosis/*physiology
MH  - Apoptotic Protease-Activating Factor 1
MH  - Biological Transport, Active
MH  - Calpain/metabolism
MH  - Caspases/*metabolism
MH  - Cell Compartmentation
MH  - Cell Nucleus/enzymology
MH  - Cytosol/enzymology
MH  - Enzyme Activation
MH  - Enzyme Precursors/metabolism
MH  - Humans
MH  - Jurkat Cells
MH  - Microsomes/enzymology
MH  - Mitochondria/enzymology
MH  - Proteins/metabolism
EDAT- 1999/08/24 00:00
MHDA- 1999/08/24 00:01
CRDT- 1999/08/24 00:00
PHST- 1999/08/24 00:00 [pubmed]
PHST- 1999/08/24 00:01 [medline]
PHST- 1999/08/24 00:00 [entrez]
AID - 10.1038/sj.cdd.4400536 [doi]
PST - ppublish
SO  - Cell Death Differ. 1999 Jul;6(7):644-51. doi: 10.1038/sj.cdd.4400536.