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(Received for publication, March 6, 1997, and in revised form, May 1, 1997)
From the Departments of ABSTRACT There is compelling evidence that members of the
caspase (interleukin-1 INTRODUCTION Apoptosis is a form of cell death that is essential for
morphogenesis, tissue homeostasis, and host defense (for review see Ref. 1). There is accumulating evidence that defects in apoptosis may
lead to several pathologies including some neurodegenerative disorders,
ischemic injury, and cancer (2). The discovery that CED-3, the product
of a gene necessary for programmed cell death in the nematode
Caenorhabditis elegans, is related to the cysteine protease
interleukin-1 EXPERIMENTAL PROCEDURES The method used for
production of caspases 1, 2, 3, 4, 5, 7, 8, and 9 involves folding of
active enzymes from their constituent large and small subunits, which
are expressed separately in Escherichia coli. The details of
the methods used for preparation of caspases 1 and 3 are described
elsewhere (6, 7). The other homologs were engineered in a similar
manner by polymerase chain reaction-directed template modification to
generate the following constructs: caspase-2 as a
MetAsn150-Asp316 large subunit with a
MetSerGly332-Thr435 small subunit; caspase-4 as
a MetSerGly95-Asp270 large subunit with a
MetSerVal291-Asn377 small subunit; caspase-5 as
a MetSerGly136-Asp311 large subunit with a
MetSer331-Asn418 small subunit; caspase-6 as a
MetSerAla34-Asp179 large subunit with a
MetSerGln181-Asn293 small subunit; caspase-7 as
a MetSerLys25-Asp198 large subunit with a
MetSer199-Gln303 small subunit; caspase-8 as a
MetSer217-Asp374 large subunit with a
MetSer375-Asp479 small subunit; and caspase-9
as a MetSerGly140-Asp305 large subunit with a
MetSerIle332-Ser416 small subunit. To obtain
active enzyme, the individual subunits from purified inclusion bodies
were solubilized in 6 M guanidine HCl and then rapidly
diluted to a final concentration of 100 µg/ml at room temperature
under conditions determined to be optimal for each enzyme. Caspase-2
was folded in 100 mM Hepes, 10 mM DTT, pH 7.5. Caspase-4 and caspase-5 were folded in 100 mM Hepes, 10% sucrose, 1% Triton X-100, 10 mM DTT, pH 7.5. Caspase-7 and
caspase-8 were folded in 100 mM Hepes, 10% sucrose, 10 mM DTT, pH 7.5. Caspase-9 was folded in 100 mM
Hepes, 20% sucrose, 1% Triton X-100, 10 mM DTT, pH 7.5. Active, recombinant CED-3 and caspase-6 were prepared by expressing a
construct encoding the entire proenzyme, minus the N-terminal peptide,
in E. coli, under conditions where a portion of the protein
produced is cytosolic and undergoes self-maturation (C. elegans CED-3 was engineered for expression as a
MetAla222-Val503 prodomainless construct and
caspase-6 as a MetSerPhe25-Asn293 prodomainless
construct).
To prepare homogeneous,
human granzyme B, granules were isolated from cultured human natural
killer leukemia YT cells and extracted with NaCl as described
previously (8, 9) except that calcium was omitted. The resulting
extract was diluted then loaded onto a Mono-S cation exchange column
(0.5 × 5 cm; Pharmacia Biotech Inc.) that had been
pre-equilibrated in 50 mM MES, pH 6.1, 25 mM
NaCl. After washing with 12 volumes of equilibration buffer, proteins
were eluted with a linear gradient up to 1 M NaCl (in 50 mM MES, pH 6.1) over 40 column volumes. Granzyme B eluted
at approximately 0.6 M NaCl and was homogeneous as judged by SDS-polyacrylamide gel electrophoresis.
The preparation of
the PS-SCL is described elsewhere (6). Each of the 60 samples (20 amino
acids × 3 sublibraries) of the PS-SCL was prepared as a stock of
approximately 10 mM in Me2SO. To determine
protease specificity, enzyme was added to reaction mixtures containing
100 µM substrate mix, 100 mM Hepes, 10 mM DTT, pH 7.5, in a total volume of 100 µl. Under these
conditions the final concentration of each individual compound is
approximately 0.25 µM. Production of AMC was monitored
continuously at room temperature in a Tecan Fluostar 96-well plate
reader using an excitation wavelength of 380 nm and an emission
wavelength of 460 nm.
RESULTS AND DISCUSSION A PS-SCL with the general structure
Ac-X-X-X-Asp-AMC was synthesized to
determine the specificities of members of the caspase family and
granzyme B (Scheme 1). The design of this library was based on several catalytic properties of the caspases, including their
near absolute specificity for cleavage after aspartic acid and their
ability to utilize tetrapeptides terminating in Asp-AMC as efficient
fluorogenic substrates. Reports that granzyme B has a similar
preference for aspartic acid in P1 (10, 11) suggested that
this library would also be useful for defining the specificity of this
enzyme. This PS-SCL is composed of three separate sublibraries of 8,000 compounds each. In each sublibrary, one position is defined with one of
20 amino acids (Scheme 1, O) (excluding cysteine), whereas
the remaining two positions (Scheme 1, X) contain a mixture of amino acids present in approximately equimolar concentrations. Using
this strategy, analysis of the three sublibraries (20 samples each)
affords a complete understanding of the amino acid preferences across
S2, S3, and S4 subsites.
Scheme 1.
To validate this approach as providing a reliable measure of
specificity, we have used it to determine the amino acid preferences of
caspase-1/ICE (6). The results of these studies indicated that the
preferred recognition motif for ICE is WEHD and led to the synthesis of
a fluorogenic substrate, Ac-WEHD-AMC, that is cleaved 50-fold more
efficiently than that previously believed to be optimal for this
enzyme, with a second order rate constant (kcat/Km) of 3.3 × 106 M We have now extended this approach to determine the substrate
specificities for C. elegans CED-3, nine of the ten known
human caspase family members and granzyme B (Fig.
1). The results obtained with the caspases divide these
enzymes into three major groups. Surprisingly, the peptide preferences
within each group are remarkably similar. Members of Group I (caspases
1, 4, and 5) all prefer the tetrapeptide sequence WEHD. In contrast,
the optimal peptide recognition motif for Group II caspases (2, 3, and 7 and CED-3) is DEXD. The similarity between
caspase-3 and caspase-7 is particularly striking; their specificity
profiles are virtually indistinguishable. The caspases in Group III (6, 8, and 9) prefer the sequence (L/V)EXD.
A comparison of the specificities of these enzymes reveals the
following. First, aside from their stringent requirement for Asp in
P1, P4 is the most critical determinant of
specificity. Members of Group I can accommodate large
aromatic/hydrophobic amino acids in this position, whereas those in
Group II require Asp for efficient catalysis. The Group III caspases
tolerate many different amino acids in P4 but prefer those
with larger aliphatic side chains. Second, all of these enzymes prefer,
to varying degrees, Glu in P3. Finally, in general, liberal
substitutions are tolerated in P2. One notable exception is
caspase-9, which has a stringent specificity for His in P2.
The structural basis for the distinct specificities of these enzymes
can be inferred from the crystal structures of caspases 1 and 3 in
complex with tetrapeptide-based inhibitors (7, 12, 13).
The results obtained with granzyme B indicate that the preferred
recognition motif for this enzyme is (I/V)EPD. Interestingly, there are
several striking similarities between the specificities of granzyme B
and the caspases beyond what appears to be a common requirement for Asp
in the P1, including the importance of P4 and a
preference for Glu in P3. These results suggest that the active sites in this serine protease and the cysteine proteases of the
caspase family may be structurally similar, even though there is no
significant overall sequence homology between these proteins.
Several lines of evidence illustrate that the specificity observed with
tetrapeptide substrates extends to macromolecules. Most compelling is
the observation that the optimal tetrapeptide recognition motifs for
some of these enzymes are identical or closely related to the sequences
found in known macromolecular substrates (Fig. 2). In
addition, with caspases 1 and 3, we have found that tetrapeptide
substrates are cleaved just as efficiently or better than protein
substrates (data not shown). We have also found that incorporation of
the optimal tetrapeptide sequence into proteins that are not normally
good substrates results in a substantial improvement in the rate of
catalysis (data not shown). Clearly, other factors also influence the
hydrolysis rate of macromolecules, such as tertiary structure. However,
it appears that with these proteases primary sequence recognition is a
necessary requirement for catalysis and that the results obtained with
the PS-SCL approach accurately reflect macromolecular specificity.
Accordingly, an intimate understanding of their specificities provides
important insights into their biological functions. First, the
observation that closely related caspases have similar and in some
cases identical specificities suggests either that these enzymes
represent tissue-specific isoforms or that they have related or
redundant functions within the same cell type. The similarities between
the specificities of granzyme B and the caspases suggest an intriguing
potential evolutionary link between these enzymes.
Second, the data presented here secure a functional relationship
between the nematode death enzyme CED-3 and its closely related Group
II human homologs. The optimal recognition motif for these enzymes
(DEXD) is similar or identical to the cleavage sites in several cell maintenance and/or repair proteins that are
proteolytically cleaved during apoptosis, including sterol regulatory
element-binding proteins (14), D4- GDI (15), poly(ADP-ribose)
polymerase (16), the 70-kDa subunit of the U1 small ribonucleoprotein
(17), the catalytic subunit of DNA-dependent protein kinase
(17), and protein kinase C Finally, the optimal recognition motif for Group III caspases and
granzyme B resembles activation sites within several effector caspase
proenzymes (Fig. 3), specifically caspases 3 and 7, implicating these enzymes as upstream components in a proteolytic
cascade that serves to amplify the death signal. This conclusion is
supported by the results from several independent lines of research
(21-32). For example, caspase-8 appears to be physically associated
with the signaling complex during Fas-mediated cell death, suggesting that it functions as a initiator, as opposed to an effector, of the
death pathway (30, 31). Notwithstanding this role, several of these
enzymes tolerate broad substitution in P4, leaving open the
possibility that they have multiple functions in apoptosis, consistent
with the proposed role for caspase-6 in cleavage of lamin A (27,
33).
Regarding the mechanism of activation of family members other than
caspases 3 and 7, it is interesting to note that all of those with
relatively long N-terminal peptides (caspases 1, 2, 4, 5, 8, 9, and
CED-3) have specificities that are similar to their own activation
sequences (Fig. 3), suggesting that these enzymes may employ an
autocatalytic mechanism of activation. This observation implies that
the N-terminal peptide plays an essential role in autocatalysis,
perhaps in mediating dimerization between two proenzyme molecules. The
importance of the N-terminal peptide to caspase-1 activation has
recently been demonstrated (34). The fact that CED-3 falls into this
category suggests that this enzyme can both self-activate and perform
effector functions, consistent with the observation that it is the only
caspase known to be in nematodes.
The results presented here do not provide compelling evidence for a
role for the Group I caspases in apoptosis, because hydrophobic amino
acids are not observed in the P4 position of proteins so far known to be cleaved during cell death. In contrast, studies with
caspase-1-deficient mice have defined an important role for this enzyme
in inflammation, where it appears to process both pro-interleukin-1 In conclusion, the results presented here, which precisely define the
specificities of the caspases and granzyme B, suggest previously
unknown functional relationships between these important biological
mediators. This information can now be exploited to produce selective,
small molecule inhibitors that will not only help to further define the
biological roles of these enzymes but may have clinical utility.
Moreover, these specificity "fingerprints" can now be used to
identify caspases in different cell types and in other species, leading
to additional insights into the biochemical mechanisms that govern
apoptosis.
FOOTNOTES ACKNOWLEDGEMENTS We thank Robert W. Myers and Antony Rosen for
numerous helpful discussions and for critical evaluations of this
manuscript.
REFERENCES
Volume 272, Number 29,
Issue of July 18, 1997
pp. 17907-17911
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
FUNCTIONAL RELATIONSHIPS ESTABLISHED FOR KEY MEDIATORS OF
APOPTOSIS*
§,,
,,,,,,
Enzymology and
¶ Molecular Design and Diversity, Merck Research Laboratories,
Rahway, New Jersey 07065 and the 
Department of Biochemistry
and Molecular Biology, Merck Frosst Centre for Therapeutic
Research, Pointe Claire, Dorval, Quebec H9R 4P8, Canada
ABSTRACT
INTRODUCTION
EXPERIMENTAL PROCEDURES
RESULTS AND DISCUSSION
FOOTNOTES
ACKNOWLEDGEMENTS
REFERENCES
converting enzyme/CED-3) family of cysteine
proteases and the cytotoxic lymphocyte-derived serine protease granzyme B play essential roles in mammalian apoptosis. Here we use a novel method employing a positional scanning substrate combinatorial library
to rigorously define their individual specificities. The results divide
these proteases into three distinct groups and suggest that several
have redundant functions. The specificity of caspases 2, 3, and 7 and
Caenorhabditis elegans CED-3 (DEXD) suggests
that all of these enzymes function to incapacitate essential homeostatic pathways during the effector phase of apoptosis. In contrast, the optimal sequence for caspases 6, 8, and 9 and granzyme B
((I/L/V)EXD) resembles activation sites in effector caspase proenzymes, consistent with a role for these enzymes as upstream components in a proteolytic cascade that amplifies the death
signal.
converting enzyme (ICE,
caspase-1)1 established proteases to be key
mediators in this process (3). Although the precise biochemical
pathways involved in mammalian cell death remain ill-defined, it is now
clear that proteases play an essential role both in the initial
signaling events and in the downstream processes that result in the
apoptotic phenotype. Those that are known to be involved include
members of the ICE/CED-3 or caspase (4) family of cysteine proteases
and the cytotoxic lymphocyte-derived serine protease, granzyme B. The
identification of potential endogenous substrates has provided
important clues to their molecular role(s); however, the identities of
the enzymes involved and their relationships to each other remain
obscure. To better understand the roles of proteases in apoptosis, to
identify appropriate fluorogenic substrates, and to facilitate
inhibitor design, peptide substrate specificities for the caspases and
granzyme B were determined using a positional scanning synthetic
combinatorial library (PS-SCL) (5). The results from this study
establish new functional relationships between these important
biological mediators.
1 s1. The
corresponding tetrapeptide aldehyde, Ac-WEHD-CHO, was found to have a
Ki for inhibition of caspase-1 of 56 pM,
making it the most potent reversible, small molecule inhibitor
described for any caspases. These results clearly demonstrated that
this novel method furnishes an accurate identification of primary
specificity that can be exploited to produce efficient substrates and
potent inhibitors.
Fig. 1.
Substrate specificities of the caspases and
granzyme B. Specificities were determined for nine of the ten
known human caspases and CED-3 and granzyme B.. The y axis
represents the rate of AMC production expressed as a percentage of the
maximum rate observed in each experiment. The x axis shows
the positionally defined amino acids. The results indicate that these
proteases fall into three major groups and suggest that several have
redundant functions. Aliases for the proteases are shown in
parentheses.
[View Larger Version of this Image (44K GIF file)]
Fig. 2.
Comparison of protease specificities with
cleavage site sequences within known substrates. These substrate
sequences have been published elsewhere (14-17, 19, 24, 33, 37, 41, 42). The optimal tetrapeptide recognition motifs for some of these
enzymes are identical or closely related to the sequences found in
known macromolecular substrates, indicating that the tetrapeptide
specificity determined in this study extends to macromolecules.
[View Larger Version of this Image (24K GIF file)]
(18). Several of these are known
endogenous substrates for caspase-3 (17, 19). It now appears that all members of this group function to cripple or destroy essential homeostatic pathways during the effector phase of apoptosis. The conclusion that these caspases have redundant effector functions is
supported by the phenotype of caspase-3-deficient mice, where cleavage
of poly(ADP)-ribose polymerase is observed in apoptotic thymocytes
(20).
Fig. 3.
Activation sites in caspases. Known and
putative activation sites in caspases (24, 38) are shown. Previous
studies have established that the first event in activation of these
proteases is cleavage at the C terminus of the large subunit (39,
40).
[View Larger Version of this Image (28K GIF file)]
and pro-interferon-
inducing factor (35-37). Interestingly,
although the cleavage site sequences in these proteins are consistent
with the tetrapeptide specificity of caspase-1, they are not optimal
(Fig. 3). This observation leaves open the possibility that this enzyme
may have additional biological functions, consistent with evidence
linking it to IL-1
production (35, 36).
§
To whom correspondence should be addressed: Dept. of Enzymology,
Merck Research Laboratories, R80W-250, P. O. Box 2000, Rahway, NJ
07065. E-mail: Nancy_Thornberry{at}merck.com.
1
The abbreviations used are: ICE,
interleukin-1 converting enzyme; PS-SCL, positional scanning
synthetic combinatorial library; DTT, dithiothreitol; MES,
4-morpholineethanesulfonic acid; AMC, aminomethylcoumarin.
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
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M. Wiens, M. Korzhev, S. Perovic-Ottstadt, B. Luthringer, D. Brandt, S. Klein, and W. E. G. Muller Toll-Like Receptors Are Part of the Innate Immune Defense System of Sponges (Demospongiae: Porifera) Mol. Biol. Evol., March 1, 2007; 24(3): 792 - 804. [Abstract] [Full Text] [PDF]
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M. E. Werner, F. Chen, J. V. Moyano, F. Yehiely, J. C. R. Jones, and V. L. Cryns Caspase Proteolysis of the Integrin beta4 Subunit Disrupts Hemidesmosome Assembly, Promotes Apoptosis, and Inhibits Cell Migration J. Biol. Chem., February 23, 2007; 282(8): 5560 - 5569. [Abstract] [Full Text] [PDF]
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L. Casciola-Rosen, M. Garcia-Calvo, H. G. Bull, J. W. Becker, T. Hines, N. A. Thornberry, and A. Rosen Mouse and Human Granzyme B Have Distinct Tetrapeptide Specificities and Abilities to Recruit the Bid Pathway J. Biol. Chem., February 16, 2007; 282(7): 4545 - 4552. [Abstract] [Full Text] [PDF]
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 A. Lu, M. Frink, M. A. Choudhry, W. J. Hubbard, L. W. Rue III, K. I. Bland, and I. H. Chaudry Mitochondria play an important role in 17beta-estradiol attenuation of H2O2-induced rat endothelial cell apoptosis Am J Physiol Endocrinol Metab, February 1, 2007; 292(2): E585 - E593. [Abstract] [Full Text] [PDF]
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Y. Ganor, V. I. Teichberg, and M. Levite TCR Activation Eliminates Glutamate Receptor GluR3 from the Cell Surface of Normal Human T Cells, via an Autocrine/Paracrine Granzyme B-Mediated Proteolytic Cleavage J. Immunol., January 15, 2007; 178(2): 683 - 692. [Abstract] [Full Text] [PDF]
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 W.-Z. Ying, H.-G. Zhang, and P. W. Sanders EGF Receptor Activity Modulates Apoptosis Induced by Inhibition of the Proteasome of Vascular Smooth Muscle Cells J. Am. Soc. Nephrol., January 1, 2007; 18(1): 131 - 142. [Abstract] [Full Text] [PDF]
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 A. K. Samraj, D. Sohn, K. Schulze-Osthoff, and I. Schmitz Loss of Caspase-9 Reveals Its Essential Role for Caspase-2 Activation and Mitochondrial Membrane Depolarization Mol. Biol. Cell, January 1, 2007; 18(1): 84 - 93. [Abstract] [Full Text] [PDF]
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D. Kaiserman, C. H. Bird, J. Sun, A. Matthews, K. Ung, J. C. Whisstock, P. E. Thompson, J. A. Trapani, and P. I. Bird The major human and mouse granzymes are structurally and functionally divergent J. Cell Biol., November 20, 2006; 175(4): 619 - 630. [Abstract] [Full Text] [PDF]
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 S. Ying, S. F. Fischer, M. Pettengill, D. Conte, S. A. Paschen, D. M. Ojcius, and G. Hacker Characterization of Host Cell Death Induced by Chlamydia trachomatis Infect. Immun., November 1, 2006; 74(11): 6057 - 6066. [Abstract] [Full Text] [PDF]
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S. Sipione, K. C. Simmen, S. J. Lord, B. Motyka, C. Ewen, I. Shostak, G. R. Rayat, J. M. Dufour, G. S. Korbutt, R. V. Rajotte, et al. Identification of a Novel Human Granzyme B Inhibitor Secreted by Cultured Sertoli Cells J. Immunol., October 15, 2006; 177(8): 5051 - 5058. [Abstract] [Full Text] [PDF]
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 V. Raz, F. Carlotti, B. J. Vermolen, E. van der Poel, W. C. R. Sloos, S. Knaan-Shanzer, A. A. F. de Vries, R. C. Hoeben, I. T. Young, H. J. Tanke, et al. Changes in lamina structure are followed by spatial reorganization of heterochromatic regions in caspase-8-activated human mesenchymal stem cells J. Cell Sci., October 15, 2006; 119(20): 4247 - 4256. [Abstract] [Full Text] [PDF]
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C. R. K. Loeb, J. L. Harris, and C. S. Craik Granzyme B Proteolyzes Receptors Important to Proliferation and Survival, Tipping the Balance toward Apoptosis J. Biol. Chem., September 22, 2006; 281(38): 28326 - 28335. [Abstract] [Full Text] [PDF]
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S. Cathelin, C. Rebe, L. Haddaoui, N. Simioni, F. Verdier, M. Fontenay, S. Launay, P. Mayeux, and E. Solary Identification of Proteins Cleaved Downstream of Caspase Activation in Monocytes Undergoing Macrophage Differentiation J. Biol. Chem., June 30, 2006; 281(26): 17779 - 17788. [Abstract] [Full Text] [PDF]
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 A Higuchi, S Shimmura, T Takeuchi, M Suematsu, and K Tsubota Elucidation of apoptosis induced by serum deprivation in cultured conjunctival epithelial cells Br. J. Ophthalmol., June 1, 2006; 90(6): 760 - 764. [Abstract] [Full Text] [PDF]
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Z. Liu, H. Li, M. Derouet, A. Berezkin, T. Sasazuki, S. Shirasawa, and K. Rosen Oncogenic Ras Inhibits Anoikis of Intestinal Epithelial Cells by Preventing the Release of a Mitochondrial Pro-apoptotic Protein Omi/HtrA2 into the Cytoplasm J. Biol. Chem., May 26, 2006; 281(21): 14738 - 14747. [Abstract] [Full Text] [PDF]
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J. M. Scheer, M. J. Romanowski, and J. A. Wells A common allosteric site and mechanism in caspases PNAS, May 16, 2006; 103(20): 7595 - 7600. [Abstract] [Full Text] [PDF]
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Y. Choe, F. Leonetti, D. C. Greenbaum, F. Lecaille, M. Bogyo, D. Bromme, J. A. Ellman, and C. S. Craik Substrate Profiling of Cysteine Proteases Using a Combinatorial Peptide Library Identifies Functionally Unique Specificities J. Biol. Chem., May 5, 2006; 281(18): 12824 - 12832. [Abstract] [Full Text] [PDF]
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C. Bonzon, L. Bouchier-Hayes, L. J. Pagliari, D. R. Green, and D. D. Newmeyer Caspase-2-induced Apoptosis Requires Bid Cleavage: A Physiological Role for Bid in Heat Shock-induced Death Mol. Biol. Cell, May 1, 2006; 17(5): 2150 - 2157. [Abstract] [Full Text] [PDF]
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A. Sarkar, M. Duncan, J. Hart, E. Hertlein, D. C. Guttridge, and M. D. Wewers ASC Directs NF-{kappa}B Activation by Regulating Receptor Interacting Protein-2 (RIP2) Caspase-1 Interactions. J. Immunol., April 15, 2006; 176(8): 4979 - 4986. [Abstract] [Full Text] [PDF]
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 M. Fennell, H. Chan, and A. Wood Multiparameter Measurement of Caspase 3 Activation and Apoptotic Cell Death in NT2 Neuronal Precursor Cells Using High-Content Analysis J Biomol Screen, April 1, 2006; 11(3): 296 - 302. [Abstract] [PDF]
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R. L. Dusek, S. Getsios, F. Chen, J. K. Park, E. V. Amargo, V. L. Cryns, and K. J. Green The Differentiation-dependent Desmosomal Cadherin Desmoglein 1 Is a Novel Caspase-3 Target That Regulates Apoptosis in Keratinocytes J. Biol. Chem., February 10, 2006; 281(6): 3614 - 3624. [Abstract] [Full Text] [PDF]
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 W. Zhu, J. Chen, X. Cong, S. Hu, and X. Chen Hypoxia and Serum Deprivation-Induced Apoptosis in Mesenchymal Stem Cells Stem Cells, February 1, 2006; 24(2): 416 - 425. [Abstract] [Full Text] [PDF]
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M. S. Bulmer and R. H. Crozier Variation in Positive Selection in Termite GNBPs and Relish Mol. Biol. Evol., February 1, 2006; 23(2): 317 - 326. [Abstract] [Full Text] [PDF]
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 D. Gilot, A.-L. Serandour, G. P. Ilyin, D. Lagadic-Gossmann, P. Loyer, A. Corlu, A. Coutant, G. Baffet, M. E. Peter, O. Fardel, et al. A role for caspase-8 and c-FLIPL in proliferation and cell-cycle progression of primary hepatocytes Carcinogenesis, December 1, 2005; 26(12): 2086 - 2094. [Abstract] [Full Text] [PDF]
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 S. Kamada, U. Kikkawa, Y. Tsujimoto, and T. Hunter A-Kinase-Anchoring Protein 95 Functions as a Potential Carrier for the Nuclear Translocation of Active Caspase 3 through an Enzyme-Substrate-Like Association Mol. Cell. Biol., November 1, 2005; 25(21): 9469 - 9477. [Abstract] [Full Text] [PDF]
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L. Eckhart, C. Ballaun, A. Uthman, C. Kittel, M. Stichenwirth, M. Buchberger, H. Fischer, W. Sipos, and E. Tschachler Identification and Characterization of a Novel Mammalian Caspase with Proapoptotic Activity J. Biol. Chem., October 21, 2005; 280(42): 35077 - 35080. [Abstract] [Full Text] [PDF]
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C. A. L. Clarke, L. N. Bennett, and P. R. Clarke Cleavage of Claspin by Caspase-7 during Apoptosis Inhibits the Chk1 Pathway J. Biol. Chem., October 21, 2005; 280(42): 35337 - 35345. [Abstract] [Full Text] [PDF]
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S. W. Hicks and C. E. Machamer Isoform-specific Interaction of Golgin-160 with the Golgi-associated Protein PIST J. Biol. Chem., August 12, 2005; 280(32): 28944 - 28951. [Abstract] [Full Text] [PDF]
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N. Comtesse, A. Zippel, S. Walle, D. Monz, C. Backes, U. Fischer, J. Mayer, N. Ludwig, A. Hildebrandt, A. Keller, et al. Complex humoral immune response against a benign tumor: Frequent antibody response against specific antigens as diagnostic targets PNAS, July 5, 2005; 102(27): 9601 - 9606. [Abstract] [Full Text] [PDF]
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 C.-J. Lee, C.-L. Liao, and Y.-L. Lin Flavivirus Activates Phosphatidylinositol 3-Kinase Signaling To Block Caspase-Dependent Apoptotic Cell Death at the Early Stage of Virus Infection J. Virol., July 1, 2005; 79(13): 8388 - 8399. [Abstract] [Full Text] [PDF]
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C. Backes, J. Kuentzer, H.-P. Lenhof, N. Comtesse, and E. Meese GraBCas: a bioinformatics tool for score-based prediction of Caspase- and Granzyme B-cleavage sites in protein sequences Nucleic Acids Res., July 1, 2005; 33(suppl_2): W208 - W213. [Abstract] [Full Text] [PDF]
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 S. Gupta, C. Reutelingsperger, and J. Narula Mortals Turn Me On... J. Nucl. Med., June 1, 2005; 46(6): 906 - 908. [Full Text] [PDF]
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A. Krippner-Heidenreich, G. Walsemann, M. J. Beyrouthy, S. Speckgens, R. Kraft, H. Thole, R. V. Talanian, M. M. Hurt, and B. Luscher Caspase-Dependent Regulation and Subcellular Redistribution of the Transcriptional Modulator YY1 during Apoptosis Mol. Cell. Biol., May 1, 2005; 25(9): 3704 - 3714. [Abstract] [Full Text] [PDF]
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 W. Wang, S. Faubel, D. Ljubanovic, A. Mitra, S. A. Falk, J. Kim, Y. Tao, A. Soloviev, L. L. Reznikov, C. A. Dinarello, et al. Endotoxemic acute renal failure is attenuated in caspase-1-deficient mice Am J Physiol Renal Physiol, May 1, 2005; 288(5): F997 - F1004. [Abstract] [Full Text] [PDF]
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S. L. Fink and B. T. Cookson Apoptosis, Pyroptosis, and Necrosis: Mechanistic Description of Dead and Dying Eukaryotic Cells Infect. Immun., April 1, 2005; 73(4): 1907 - 1916. [Full Text] [PDF]
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M. A. O'Brien, W. J. Daily, P. E. Hesselberth, R. A. Moravec, M. A. Scurria, D. H. Klaubert, R. F. Bulleit, and K. V. Wood Homogeneous, Bioluminescent Protease Assays: Caspase-3 as a Model J Biomol Screen, March 1, 2005; 10(2): 137 - 148. [Abstract] [PDF]
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 K. Steigerwald, G. K. Behbehani, K. A. Combs, M. C. Barton, and J. Groden The APC Tumor Suppressor Promotes Transcription-Independent Apoptosis In vitro Mol. Cancer Res., February 1, 2005; 3(2): 78 - 89. [Abstract] [Full Text] [PDF]
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S. Kamada, U. Kikkawa, Y. Tsujimoto, and T. Hunter Nuclear Translocation of Caspase-3 Is Dependent on Its Proteolytic Activation and Recognition of a Substrate-like Protein(s) J. Biol. Chem., January 14, 2005; 280(2): 857 - 860. [Abstract] [Full Text] [PDF]
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S. Mahrus, W. Kisiel, and C. S. Craik Granzyme M Is a Regulatory Protease That Inactivates Proteinase Inhibitor 9, an Endogenous Inhibitor of Granzyme B J. Biol. Chem., December 24, 2004; 279(52): 54275 - 54282. [Abstract] [Full Text] [PDF]
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 Z. Roth and P.J. Hansen Involvement of Apoptosis in Disruption of Developmental Competence of Bovine Oocytes by Heat Shock During Maturation Biol Reprod, December 1, 2004; 71(6): 1898 - 1906. [Abstract] [Full Text] [PDF]
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 C. Houde, K. G. Banks, N. Coulombe, D. Rasper, E. Grimm, S. Roy, E. M. Simpson, and D. W. Nicholson Caspase-7 Expanded Function and Intrinsic Expression Level Underlies Strain-Specific Brain Phenotype of Caspase-3-Null Mice J. Neurosci., November 3, 2004; 24(44): 9977 - 9984. [Abstract] [Full Text] [PDF]
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 L. J. Schmidt, H. Murillo, and D. J. Tindall Gene Expression in Prostate Cancer Cells Treated With the Dual 5 Alpha-Reductase Inhibitor Dutasteride J Androl, November 1, 2004; 25(6): 944 - 953. [Abstract] [Full Text] [PDF]
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 Y. Kotone-Miyahara, K. Yamashita, K.-K. Lee, S. Yonehara, T. Uchiyama, M. Sasada, and A. Takahashi Short-term delay of Fas-stimulated apoptosis by GM-CSF as a result of temporary suppression of FADD recruitment in neutrophils: evidence implicating phosphatidylinositol 3-kinase and MEK1-ERK1/2 pathways downstream of classical protein kinase C J. Leukoc. Biol., November 1, 2004; 76(5): 1047 - 1056. [Abstract] [Full Text] [PDF]
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M. P. Biju, A. K. Neumann, S. J. Bensinger, R. S. Johnson, L. A. Turka, and V. H. Haase Vhlh Gene Deletion Induces Hif-1-Mediated Cell Death in Thymocytes Mol. Cell. Biol., October 15, 2004; 24(20): 9038 - 9047. [Abstract] [Full Text] [PDF]
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 K. Izeradjene, L. Douglas, A. Delaney, and J. A. Houghton Influence of Casein Kinase II in Tumor Necrosis Factor-Related Apoptosis-Inducing Ligand-Induced Apoptosis in Human Rhabdomyosarcoma Cells Clin. Cancer Res., October 1, 2004; 10(19): 6650 - 6660. [Abstract] [Full Text] [PDF]
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P. M. Horowitz, K. R. Patterson, A. L. Guillozet-Bongaarts, M. R. Reynolds, C. A. Carroll, S. T. Weintraub, D. A. Bennett, V. L. Cryns, R. W. Berry, and L. I. Binder Early N-Terminal Changes and Caspase-6 Cleavage of Tau in Alzheimer's Disease J. Neurosci., September 8, 2004; 24(36): 7895 - 7902. [Abstract] [Full Text] [PDF]
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 M. Alikhani, Z. Alikhani, and D.T. Graves Apoptotic Effects of LPS on Fibroblasts are Indirectly Mediated through TNFR1 Journal of Dental Research, September 1, 2004; 83(9): 671 - 676. [Abstract] [Full Text] [PDF]
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J. A. Hardy, J. Lam, J. T. Nguyen, T. O'Brien, and J. A. Wells Discovery of an allosteric site in the caspases PNAS, August 24, 2004; 101(34): 12461 - 12466. [Abstract] [Full Text] [PDF]
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A. J. Bredemeyer, R. M. Lewis, J. P. Malone, A. E. Davis, J. Gross, R. R. Townsend, and T. J. Ley A proteomic approach for the discovery of protease substrates PNAS, August 10, 2004; 101(32): 11785 - 11790. [Abstract] [Full Text] [PDF]
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O. R. Kunduzova, G. Escourrou, F. De La Farge, R. Salvayre, M.-H. Seguelas, N. Leducq, F. Bono, J.-M. Herbert, and A. Parini Involvement of Peripheral Benzodiazepine Receptor in the Oxidative Stress, Death-Signaling Pathways, and Renal Injury Induced by Ischemia-Reperfusion J. Am. Soc. Nephrol., August 1, 2004; 15(8): 2152 - 2160. [Abstract] [Full Text] [PDF]
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J. D. Foley, H. Rosenbaum, and A. E. Griep Temporal Regulation of VEID-7-amino-4-trifluoromethylcoumarin Cleavage Activity and Caspase-6 Correlates with Organelle Loss during Lens Development J. Biol. Chem., July 30, 2004; 279(31): 32142 - 32150. [Abstract] [Full Text] [PDF]
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S. W. Ruggles, R. J. Fletterick, and C. S. Craik Characterization of Structural Determinants of Granzyme B Reveals Potent Mediators of Extended Substrate Specificity J. Biol. Chem., July 16, 2004; 279(29): 30751 - 30759. [Abstract] [Full Text] [PDF]
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B. D. Poole, Y. V. Karetnyi, and S. J. Naides Parvovirus B19-Induced Apoptosis of Hepatocytes J. Virol., July 15, 2004; 78(14): 7775 - 7783. [Abstract] [Full Text] [PDF]
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J. C. Reed, K. S. Doctor, and A. Godzik The Domains of Apoptosis: A Genomics Perspective Sci. Signal., June 29, 2004; 2004(239): re9 - re9. [Abstract] [Full Text] [PDF]
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F. Chen, O. K. Arseven, and V. L. Cryns Proteolysis of the Mismatch Repair Protein MLH1 by Caspase-3 Promotes DNA Damage-induced Apoptosis J. Biol. Chem., June 25, 2004; 279(26): 27542 - 27548. [Abstract] [Full Text] [PDF]
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 G. Tomiyoshi, Y. Horita, M. Nishita, K. Ohashi, and K. Mizuno Caspase-mediated cleavage and activation of LIM-kinase 1 and its role in apoptotic membrane blebbing Genes Cells, June 1, 2004; 9(6): 591 - 600. [Abstract] [Full Text] [PDF]
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 K. M. Kim, Y. Zhang, B.-Y. Kim, S. J. Jeong, S. A. Lee, G.-D. Kim, A. Dritschilo, and M. Jung The p65 subunit of nuclear factor-{kappa}B is a molecular target for radiation sensitization of human squamous carcinoma cells Mol. Cancer Ther., June 1, 2004; 3(6): 693 - 698. [Abstract] [Full Text] [PDF]
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 L. He, X. Wu, F. Meylan, D. P. Olson, J. Simone, D. Hewgill, R. Siegel, and P. E. Lipsky Monitoring Caspase Activity in Living Cells Using Fluorescent Proteins and Flow Cytometry Am. J. Pathol., June 1, 2004; 164(6): 1901 - 1913. [Abstract] [Full Text] [PDF]
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N. A. Maianski, D. Roos, and T. W. Kuijpers Bid Truncation, Bid/Bax Targeting to the Mitochondria, and Caspase Activation Associated with Neutrophil Apoptosis Are Inhibited by Granulocyte Colony-Stimulating Factor J. Immunol., June 1, 2004; 172(11): 7024 - 7030. [Abstract] [Full Text] [PDF]
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G. Paroni, M. Mizzau, C. Henderson, G. Del Sal, C. Schneider, and C. Brancolini Caspase-dependent Regulation of Histone Deacetylase 4 Nuclear-Cytoplasmic Shuttling Promotes Apoptosis Mol. Biol. Cell, June 1, 2004; 15(6): 2804 - 2818. [Abstract] [Full Text] [PDF]
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