An anti-apoptotic B-cell lymphoma-2 (BCL-2) from Channa striatus: Sequence analysis and delayed and advanced gene expression in response to fungal, bacterial and poly I: C induction

Molecular Immunology

Volumn 63, Issue 2, 2015, Pages 586-594

  Arockiaraj, Jesu ^a   Palanisamy, Rajesh ^a   Arasu, Abirami ^a,b   Sathyamoorthi, Akila ^a,b   Kumaresan, Venkatesh ^a   Bhatt, Prasanth ^a   Chaurasia, Mukesh Kumar ^a   Pasupuleti, Mukesh ^c   Gnanam, Annie J ^d  

^a SRM INSTITUTE OF SCIENCE AND TECHNOLOGY   (India)

^b SRM Arts and Science College Chennai   (India)

^c CENTRAL DRUG RESEARCH INSTITUTE   (India)

^d UNIVERSITY OF TEXAS AT AUSTIN   (United States)

Author keywords

B cell lymphoma; Bioinformatics; Channa striatus; Delayed response; Gene expression

Indexed keywords

AMINO ACID; ARGININE; BCL2 L1 PROTEIN; BETA 1,3 GLUCAN; BH1 PROTEIN; BH2 PROTEIN; BH3 PROTEIN; COMPLEMENTARY DNA; CSBCL2 PROTEIN; ESCHERICHIA COLI LIPOPOLYSACCHARIDE; GLYCINE; MEMBRANE PROTEIN; MESSENGER RNA; POLYINOSINIC POLYCYTIDYLIC ACID; PROTEIN BCL 2; SIGNAL PEPTIDE; TRYPTOPHAN; TUMOR SUPPRESSOR PROTEIN; UNCLASSIFIED DRUG;

AEROMONAS HYDROPHILA; ALPHA HELIX; AMINO TERMINAL SEQUENCE; ANIMAL EXPERIMENT; ANIMAL TISSUE; APHANOMYCES; APHANOMYCES INVADANS; APOPTOSIS; ARTICLE; BACTERIUM; CHANNA STRIATUS; CONTROLLED STUDY; DNA LIBRARY; DNA SEQUENCE; ESCHERICHIA COLI; FUNGUS; GENE EXPRESSION; IMMUNE SYSTEM; LAMINARIA; LAMINARIA DIGITATA; NONHUMAN; PHYLOGENY; PROTEIN DOMAIN; PROTEIN INDUCTION; PROTEIN MOTIF; PUFFER FISH; RECEPTOR UPREGULATION; SEQUENCE ANALYSIS; SPLEEN; TAKIFUGU RUBRIPES; AMINO ACID SEQUENCE; ANIMAL; BIOLOGY; CHEMISTRY; DRUG EFFECTS; GENE EXPRESSION REGULATION; GENETICS; METABOLISM; MICROBIOLOGY; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; PERCIFORMES; PHYSIOLOGY; REAL TIME POLYMERASE CHAIN REACTION; SEQUENCE ALIGNMENT;

BACTERIA (MICROORGANISMS); CHANNA STRIATA;

AEROMONAS HYDROPHILA; AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANIMALS; APHANOMYCES; APOPTOSIS; BASE SEQUENCE; COMPUTATIONAL BIOLOGY; GENE EXPRESSION REGULATION; MOLECULAR SEQUENCE DATA; PERCIFORMES; PHYLOGENY; POLY I-C; PROTO-ONCOGENE PROTEINS C-BCL-2; REAL-TIME POLYMERASE CHAIN REACTION; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS, PROTEIN;

EID: 84912143362     PISSN: 01615890     EISSN: 18729142     Source Type: Journal    
DOI: 10.1016/j.molimm.2014.07.018     Document Type: Article

References (35)

1. Abirami A., Venkatesh K., Akila S., Rajesh P., Prabha N., Prasanth B., et al. Fish lily type lectin-1 contains β-prism 2 architecture: immunological characterization. Mol. Immunol. 2013, 56:497-506.
2. Antonsson B., Martinou J.C. The Bcl-2 protein family. Exp. Cell Res. 2000, 256:50-57.
3. Aouacheria A., Brunet F., Gouy M. Phylogenomics of life-or-death switches in multicellular animals: Bcl-2, BH3-only, and BNip families of apoptotic regulators. Mol. Biol. Evol. 2005, 22:2395-2416.
4. Arockiaraj J., Annie J.G., Dhanaraj M., Mukesh P., Milton J., Arun S. An upstream initiator caspase 10 of snakehead murrel Channa striatus, containing DED, p20 and p10 subunits: molecular cloning, gene expression and proteolytic activity. Fish Shellfish Immunol. 2013, 34:505-513.
5. Arockiaraj J., Annie J.G., Venkatesh K., Rajesh P., Prasanth B., Thirumalai M.K. An unconventional antimicrobial protein histone from freshwater prawn Macrobrachium rosenbergii: analysis of immune properties. Fish Shellfish Immunol. 2013, 35:1511-1522.
6. Arockiaraj J., Muruganandam M., Marimuthu K., Haniffa M.A. Utilization of carbohydrates as a dietary energy source by striped murrel Channa striatus (Bloch) fingerlings. Acta Zool. Taiwan. 1999, 10:103-111.
7. Arockiaraj J., Sarasvathi E., Puganeshwaran V., Arun S., Rofina Y.O., Subha B. Molecular cloning, characterization and gene expression of an antioxidant enzyme catalase (MrCat) from Macrobrachium rosenbergii. Fish Shellfish Immunol. 2012, 32:670-682.
8. Arockiaraj J., Sarasvathi E., Puganeshwaran V., Arun S., Rofina Y.O., Subha B. Effect of infectious hypodermal and haematopoietic necrosis virus (IHHNV) infection on caspase 3c expression and activity in freshwater prawn Macrobrachium rosenbergii. Fish Shellfish Immunol. 2012, 32:161-169.
9. Boman H.G. Antibacterial peptides: basic facts and emerging concepts. J. Intern. Med. 2003, 254:197-215.
10. Carris L.M., Little C.R., Stiles C.M. Introduction to fungi. Plant Health Instructor 2012, 10.1094/PHI-I-2012-0426-01.
11. Craig R.W. MCL1 provides a window on the role of the BCL2 family in cell proliferation, differentiation and tumorigenesis. Leukemia 2002, 16:444-454.
12. Démoulins T., Baron M.L., Kettaf N., Abdallah A., Sharif-Askari E., Sékaly R.P. Poly (I:C) induced immune response in lymphoid tissues involves three sequential waves of type I IFN expression. Virology 2009, 386:225-236.
13. Dewson G., Ruth M.K. Bcl-2 family-regulated apoptosis in health and disease. Cell Health Cytoskelet. 2010, 2:9-22. (review).
14. Distelhorst C.W., Rong Y.P., Bultynck G., Aromolaran A.S., Zhong F., Parys J.B., et al. The BH4 domain of Bcl-2 inhibits ER calcium release and apoptosis by binding the regulatory and coupling domain of the IP3 receptor. PNAS 2009, 106:14397-14402.
15. Feng C.Y., Rise M.L. Characterization and expression analyses of anti-apoptotic Bcl-2-like genes NR-13, Mcl-1, Bcl-X1, and Bcl-X2 in Atlantic cod (Gadus morhua). Mol. Immunol. 2010, 47:763-784.
16. Fesik S.W., Andrew M.P., Olejniczak E.T. Structural biology of the Bcl-2 family of proteins. Biochim. Biophys. Acta 2004, 1644:83-94.
17. Green D.R., John C.R. Mitochondria and apoptosis. Science 1998, 281:28. (review).
18. Krajewski S., Tanaka S., Takayama S., Schibles M.J., Fenton W. Investigation of the subcellular distribution of the Bcl-2 onco-protein: residence in the nuclear envelope, endoplasmic reticulum and outer mitochondrial membrane. Cancer Res. 1993, 53:4701-4714.
19. Lee Y., Whang I., Lee S., Menike U., Oh C., Kang D.H., et al. Two molluscan BCL-2 family members from Manila clam, Ruditapes philippinarum: molecular characterization and immune responses. Fish Shellfish Immunol. 2013, 34:1628-1634.
20. Letai A., Joslyn K.B. Control of mitochondrial apoptosis by the Bcl-2 family. J. Cell Sci. 2009, 122:437-441.
21. Lin J., Ding J., Zhang Z., Andrews D.W., Roberts G.J., Falcone M., et al. Bcl-2 and Bax interact via the BH1-3 Groove-BH3 motif interface and a novel interface involving the BH4 motif. J. Biol. Chem. 2010, 285:28749-28763.
22. Lin X.K., Sun M., Zheng L.H., Wang Y.J., Sheng J., Wang F., et al. Antitumor peptides from marine organisms. Mar. Drugs 2011, 9:1840-1859.
23. Livak K.J., Schmittgenm T.D. Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method. Methods 2001, 25:402-408.
24. MacManus J.P., Mathew D.L. Gene expression induced by cerebral ischemia: an apoptotic perspective. J. Cereb. Blood Flow Metab. 1997, 17:815-832.
25. Michels J., Johnson P.W., Packham G. Mcl-1. Int. J. Biochem. Cell Biol. 2005, 37:267-271.
26. Nguyen S.M., Millar S.D.G., Yongll V.W. Targeting of Bcl-2 to the mitochondrial outer membrane by a COOH-terminal signal anchor sequence. J. Biol. Chem. 1993, 268:25265-25268.
27. Papagianni M. Ribosomally synthesized peptides with antimicrobial properties: biosynthesis, structure, function, and applications. Biotechnol. Adv. 2003, 21:465-499.
28. Peterson J.W. Bacterial pathogenesis. Medical Microbiology 1996, University of Texas Medical Branch at Galveston, Galveston, TX, (Chapter 7). 4th edition. S. Baron (Ed.).
29. Prasanth B., Venkatesh K., Rajesh P., Mukesh K.C., Annie J.G., Mukesh P., et al. Immunological role of C4 CC chemokine-1 from snakehead murrel Channa striatus. Mol. Immunol. 2013, 57:292-301.
30. Rajesh P., Prasanth B., Venkatesh K., Mukesh K.C., Annie J.G., Mukesh P., et al. A redox active site containing murrel cytosolic thioredoxin: analysis of immunological properties. Fish Shellfish Immunol. 2013, 36:141-150.
31. Steimer D.A., Boyd K., Takeuchi O., Fisher J.K., Zambetti G.P., Opferman J.T. Selective roles for antiapoptotic MCL-1 during granulocyte development and macrophage effector function. Blood 2009, 113:2805-2815.
32. Todar K. Colonization and invasion by bacterial pathogens. Web Review of Todar's Online Textbook of Bacteriology 2008, 1-4. University of Wisconsin, Department of Bacteriology, Madison, Wisconsin, USA, (Chapter 3). K. Today (Ed.).
33. Tschopp J., Borner C., Martinou I., Matthmann C., Irmber M., Scherer E., et al. The protein Bcl-2α does not require membrane attachment but two conserved domain to suppress apoptosis. J. Cell Biol. 2013, 4:1059-1068.
34. Venkatesh K., Prasanth B., Rajesh P., Annie J.G., Mukesh P., Arockiaraj J. A murrel cysteine protease, cathepsin L: bioinformatics characterization, gene expression and proteolytic activity. Biologia 2014, 69:395-406.
35. Wilson J.M., Laurent P. Fish gill morphology: inside out. J. Exp. Zool. 2002, 293:192-213.