Caspase 3 from rock bream (Oplegnathus fasciatus): genomic characterization and transcriptional profiling upon bacterial and viral inductions

Fish & Shellfish Immunology
Don Anushka Sandaruwan ElvitigalaJehee Lee

Abstract

Caspase 3 is a prominent mediator of apoptosis and participates in the cell death signaling cascade. In this study, caspase 3 was identified (Rbcasp3) and characterized from rock bream (Oplegnathus fasciatus). The full-length cDNA of Rbcasp3 is 2683 bp and contains an open reading frame of 849 bp, which encodes a 283 amino acid protein with a calculated molecular mass of 31.2 kDa and isoelectric point of 6.31. The amino acid sequence resembles the conventional caspase 3 domain architecture, including crucial amino acid residues in the catalytic site and binding pocket. The genomic length of Rbcasp3 is 7529 bp, and encompasses six exons interrupted by five introns. Phylogenetic analysis affirmed that Rbcasp3 represents a complex group in fish that has been shaped by gene duplication and diversification. Many putative transcription factor binding sites were identified in the predicted promoter region of Rbcasp3, including immune factor- and cancer signal-inducible sites. Rbcasp3, excluding the pro-domain, was expressed in Escherichia coli. The recombinant protein showed a detectable activity against the mammalian caspase 3/7-specific substrate DEVD-pNA, indicating a functional role in physiology. Quantitative real time PCR assay ...Continue Reading

References

Jul 1, 1996·Nature Structural Biology·J RotondaJ W Becker
Aug 1, 1997·Trends in Biochemical Sciences·D W Nicholson, N A Thornberry
Aug 15, 1997·The Biochemical Journal·G M Cohen
Aug 28, 1998·Science·N A Thornberry, Y Lazebnik
Feb 17, 1999·Genes & Development·Q L Deveraux, J C Reed
Apr 28, 1999·Trends in Microbiology·H Everett, G McFadden
Jul 10, 1999·The Journal of Biological Chemistry·B B Wolf, D R Green
Jul 27, 1999·Hepatology : Official Journal of the American Association for the Study of Liver Diseases·H DobashiI Sekine
Dec 1, 1999·Cell Death and Differentiation·D W Nicholson
Feb 24, 2000·Biology of Reproduction·A L Johnson, J T Bridgham
Jun 29, 2000·Annual Review of Biochemistry·W C EarnshawS H Kaufmann
Dec 6, 2000·Microbiology and Molecular Biology Reviews : MMBR·H Y Chang, X Yang
Dec 15, 2000·Current Opinion in Structural Biology·M G Grütter
Mar 21, 2001·Cellular Signalling·M Guha, N Mackman
May 25, 2001·Current Opinion in Critical Care·K Sheth, P Bankey
Aug 16, 2001·Journal of Toxicology and Environmental Health. Part B, Critical Reviews·A W Abu-Qare, M B Abou-Donia
Jan 5, 2002·The Journal of Biological Chemistry·Wenfang LiuAlexander G Yakovlev
Feb 16, 2002·Methods : a Companion to Methods in Enzymology·K J Livak, T D Schmittgen
Mar 28, 2002·Pharmacology & Therapeutics·E W Sun, Y F Shi
Dec 3, 2003·Cell Death and Differentiation·M BoyceJ Yuan
Sep 29, 2004·The Biochemical Journal·Pablo Fuentes-Prior, Guy S Salvesen
Oct 4, 2005·The Journal of Clinical Investigation·Inna N LavrikPeter H Krammer
Nov 3, 2005·The FEBS Journal·Po-ki Ho, Christine J Hawkins
Apr 1, 2006·Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology·Harald TakleOivind Andersen
Jun 20, 2006·Molecular Immunology·Marta I R ReisNuno M S dos Santos
Jun 22, 2006·Journal of Molecular Biology·Rajkumar GanesanMarkus G Grütter
Apr 17, 2007·Fish & Shellfish Immunology·Diana S NascimentoNuno M S dos Santos
May 10, 2007·Molecular Biology and Evolution·Koichiro TamuraSudhir Kumar
Jan 25, 2008·BMC Bioinformatics·Yang Zhang
Jul 22, 2008·Archives of Virology·Kosuke Zenke, Ki Hong Kim
May 9, 2013·ACS Synthetic Biology·Rajni VermaDanilo Roccatano

❮ Previous
Next ❯

Citations

Oct 24, 2015·Virus Research·Latif ReshiJiann-Ruey Hong
Jun 2, 2016·Fish & Shellfish Immunology·Yina ShaoQiongfen Qiu

❮ Previous
Next ❯

Related Concepts

Related Feeds

Apoptotic Caspases

Apoptotic caspases belong to the protease enzyme family and are known to play an essential role in inflammation and programmed cell death. Here is the latest research.

Apoptosis

Apoptosis is a specific process that leads to programmed cell death through the activation of an evolutionary conserved intracellular pathway leading to pathognomic cellular changes distinct from cellular necrosis