CO2 impairs peroxynitrite-mediated inhibition of human caspase-3

2006 ◽  
Vol 349 (1) ◽  
pp. 367-371 ◽  
Author(s):  
Paolo Ascenzi ◽  
Maria Marino ◽  
Enea Menegatti
Keyword(s):  
Caspase 3 ◽  
Human Caspase

scholarly journals Biochemical and Genetic Interactions betweenDrosophila Caspases and the Proapoptotic Genesrpr, hid, and grim

2000 ◽  
Vol 20 (8) ◽  
pp. 2907-2914 ◽  
Author(s):  
Zhiwei Song ◽  
Bo Guan ◽  
Andreas Bergman ◽  
Donald W. Nicholson ◽  
Nancy A. Thornberry ◽  
...  
Keyword(s):  
Caspase 3 ◽  
Cultured Cells ◽  
Ectopic Expression ◽  
Full Length ◽  
Truncated Form ◽  
Effector Caspase ◽  
Death Effector ◽  
Human Caspase

ABSTRACT In Drosophila melanogaster, the induction of apoptosis requires three closely linked genes, reaper(rpr), head involution defective(hid), and grim. The products of these genes induce apoptosis by activating a caspase pathway. Two very similarDrosophila caspases, DCP-1 and drICE, have been previously identified. We now show that DCP-1 has a substrate specificity that is remarkably similar to those of human caspase 3 and Caenorhabditis elegans CED-3, suggesting that DCP-1 is a death effector caspase. drICE and DCP-1 have similar yet different enzymatic specificities. Although expression of either in cultured cells induces apoptosis, neither protein was able to induce DNA fragmentation inDrosophila SL2 cells. Ectopic expression of a truncated form of dcp-1 (ΔN-dcp-1) in the developingDrosophila retina under an eye-specific promoter resulted in a small and rough eye phenotype, whereas expression of the full-length dcp-1 (fl-dcp-1) had little effect. On the other hand, expression of either full-length drICE(fl-drICE) or truncated drICE(ΔN-drICE) in the retina showed no obvious eye phenotype. Although active DCP-1 protein cleaves full-length DCP-1 and full-length drICE in vitro, GMR-ΔN-dcp-1 did not enhance the eye phenotype of GMR-fl-dcp-1 or GMR-fl-drICEflies. Significantly, GMR-rpr and GMR-grim, but not GMR-hid, dramatically enhanced the eye phenotype of GMR-fl-dcp-1 flies. These results indicate that Reaper and Grim, but not HID, can activate DCP-1 in vivo.

scholarly journals Functional Analysis of the Inhibitor of Apoptosis (iap) Gene Carried by the Entomopoxvirus of Amsacta moorei

2005 ◽  
Vol 79 (4) ◽  
pp. 2335-2345 ◽  
Author(s):  
Qianjun Li ◽  
Peter Liston ◽  
Richard W. Moyer
Keyword(s):  
Caspase 3 ◽  
Autographa Californica ◽  
Inhibitor Of Apoptosis ◽  
Intrinsic Pathway ◽  
Abortive Infection ◽  
Caspase 9 ◽  
Rapid Induction ◽  
Human Caspase ◽  
Proapoptotic Gene

ABSTRACT The entomopoxvirus from Amsacta moorei (AmEPV) contains none of the commonly recognized vertebrate poxvirus apoptotic suppressor genes. However, AmEPV carries a single inhibitor of apoptosis (iap) gene (AMViap) not present in vertebrate poxviruses. The AMViap gene was active when coexpressed with the Drosophila proapoptotic gene hid in Ld652 cells and can rescue cells from apoptosis as shown by increased number of surviving cells and reduced levels of caspase-3-like activity. We also showed that expression of the AMViap gene rescued polyhedron production in Autographa californica M nucleopolyhedrovirus (AcMNPV)Δp35-infected Sf9 cells during an otherwise abortive infection induced by apoptosis. Surprisingly, deletion of the AMViap gene from the AmEPV genome led to only a modest (10-fold) loss of virion production in infected Ld652 cells, indicating that the AMViap gene is nonessential for virus replication under these conditions. However, infection of Ld652 cells by AmEPV lacking a functional iap gene led to a more rapid induction of cytotoxicity and increased levels of caspase-3-like activity. Similar results were observed and were more pronounced in infected Sf9 and S2 cells. The purified AMVIAP protein also inhibits the enzymatic activities of human caspase-9 and caspase-3 in vitro. Our results indicate that while the AMViap gene was active in controlling apoptosis through the intrinsic pathway, the virus likely encodes additional proteins that also regulate apoptosis.

Human caspase-3 inhibition by Z-tLeu-Asp-H: tLeu(P2) counterbalances Asp(P4) and Glu(P3) specific inhibitor truncation

2008 ◽  
Vol 377 (3) ◽  
pp. 757-762 ◽  
Author(s):  
Patrizia Colantonio ◽  
Loris Leboffe ◽  
Alessandro Bolli ◽  
Maria Marino ◽  
Paolo Ascenzi ◽  
...  
Keyword(s):  
Caspase 3 ◽  
Specific Inhibitor ◽  
Human Caspase

Conformational restrictions in the active site of unliganded human caspase-3

2003 ◽  
Vol 16 (3) ◽  
pp. 121-124 ◽  
Author(s):  
Chao-Zhou Ni ◽  
Chenglong Li ◽  
Joe C. Wu ◽  
Alfred P. Spada ◽  
Kathryn R. Ely
Keyword(s):  
Active Site ◽  
Caspase 3 ◽  
Human Caspase ◽  
Conformational Restrictions

A18 NICOTINE REVERSES THE WORKING MEMORY DEFICIT OBSERVED IN MICE OVEREXPRESSING HUMAN CASPASE-3

2005 ◽  
Vol 16 (Supplement 1) ◽  
pp. S29
Author(s):  
J. Young ◽  
J. Sharkey ◽  
J. McCulloch ◽  
K. Finlayson
Keyword(s):  
Working Memory ◽  
Caspase 3 ◽  
Memory Deficit ◽  
Human Caspase

scholarly journals Selective and Rapid Cell-Permeable Inhibitor of Human Caspase-3

2019 ◽  
Vol 14 (11) ◽  
pp. 2463-2470 ◽  
Author(s):  
Angelo Solania ◽  
Gonzalo E. González-Páez ◽  
Dennis W. Wolan
Keyword(s):  
Caspase 3 ◽  
Human Caspase

Ac-tLeu-Asp-H is the minimal and highly effective human caspase-3 inhibitor: biological and in silico studies

Amino Acids ◽  
2014 ◽  
Vol 47 (1) ◽  
pp. 153-162 ◽  
Author(s):  
Anna Ferrucci ◽  
Loris Leboffe ◽  
Mariangela Agamennone ◽  
Antonella Di Pizio ◽  
Marco Fiocchetti ◽  
...  
Keyword(s):  
In Silico ◽  
Caspase 3 ◽  
In Silico Studies ◽  
Highly Effective ◽  
Human Caspase

scholarly journals Sp1-like sequences mediate human caspase-3 promoter activation by p73 and cisplatin

FEBS Journal ◽  
2008 ◽  
Vol 275 (9) ◽  
pp. 2200-2213 ◽  
Author(s):  
Cherukuri Sudhakar ◽  
Nishant Jain ◽  
Ghanshyam Swarup
Keyword(s):  
Caspase 3 ◽  
Promoter Activation ◽  
Human Caspase
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