Structure and expression of a shrimp prohormone convertase 2

General and Comparative Endocrinology

Volumn 178, Issue 2, 2012, Pages 185-193

  Tangprasittipap, Amornrat ^a,b,d   Chouwdee, Saisunee ^a,b   Phiwsaiya, Kornsunee ^b   Laiphrom, Seansook ^c   Senapin, Saengchan ^b   Flegel, Timothy W ^b   Sritunyalucksana, Kallaya ^a,b  

^a NATIONAL SCIENCE AND TECHNOLOGY DEVELOPMENT AGENCY   (Thailand)

^b Mahidol University   (Thailand)

^c Shrimp Genetic Improvement Center   (Thailand)

^d MAHIDOL UNIVERSITY   (Thailand)

Author keywords

Crustacean hyperglycemic hormone 1 (CHH 1); Neuroendocrine hormones; Neurosecretory cells; Penaeus monodon; Prohormone convertase 2 (PC2)

Indexed keywords

COMPLEMENTARY DNA; GLUCAGON; PROPROTEIN CONVERTASE 2;

ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME LOCALIZATION; ENZYME STRUCTURE; GLUCOSE METABOLISM; HORMONE BINDING; IMMUNOHISTOCHEMISTRY; MALE; MOLECULAR DYNAMICS; NONHUMAN; NUCLEOTIDE SEQUENCE; PENAEUS MONODON; PRIORITY JOURNAL; PROTEIN EXPRESSION; QUANTITATIVE ANALYSIS; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; RNA SEQUENCE; SEQUENCE ANALYSIS;

EID: 84862732915     PISSN: 00166480     EISSN: 10956840     Source Type: Journal    
DOI: 10.1016/j.ygcen.2012.05.005     Document Type: Article

References (24)

1. T.A. Bell, D.V. Lightner, Handbook of Normal Penaeid Shrimp Histology, World Aquaculture Society, Baton Rouge, La., 1988.
2. Benjannet S., Rondeau N., Paquet L., Boudreault A., Lazure C., Chretien M., et al. Comparative biosynthesis, covalent post-translational modifications and efficiency of prosegment cleavage of the prohormone convertases PC1 and PC2: glycosylation, sulphation and identification of the intracellular site of prosegment cleavage of PC1 and PC2. Biochem. J. 1993, 294(Pt 3):735-743.
3. Bryan P., Pantoliano M.W., Quill S.G., Hsiao H.Y., Poulos T. Site-directed mutagenesis and the role of the oxyanion hole in subtilisin. Proc. Nat. Acad. Sci. U.S.A. 1986, 83:3743-3745.
4. Chung J.S., Zmora N., Katayama H., Tsutsui N. Crustacean hyperglycemic hormone (CHH) neuropeptides family: functions, titer, and binding to target tissues. Gen. Comp. Endocrinol. 2010, 166:447-454.
5. Cummins S.F., York P.S., Hanna P.H., Degnan B.M., Croll R.P. Expression of prohormone convertase 2 and the generation of neuropeptides in the developing nervous system of the gastropod Haliotis. Int. J. Dev. Biol. 2009, 53:1081-1088.
6. De Kleijn D.P., Van Herp F. Molecular biology of neurohormone precursors in the eyestalk of Crustacea. Comp. Biochem. Physiol. B: Biochem. Mol. Biol. 1995, 112:573-579.
7. Gomez-Saladin E., Wilson D.L., Dickerson I.M. Isolation and in situ localization of a cDNA encoding a Kex2-like prohormone convertase in the nematode Caenorhabditis elegans. Cell. Mol. Neurobiol. 1994, 14:9-25.
8. Hwang J.R., Siekhaus D.E., Fuller R.S., Taghert P.H., Lindberg I. Interaction of Drosophila melanogaster prohormone convertase 2 and 7B2. Insect cell-specific processing and secretion. J. Biol. Chem. 2000, 275:17886-17893.
9. Li Q.-L., Naqvi S., Shen X., Liu Y.-J., Lindberg I., Friedman T.C. Prohormone convertase 2 enzymatic activity and its regulation in neuro-endocrine cells and tissues. Regul. Pept. 2003, 110:197-205.
10. Livak K.J., Schmittgen T.D. Analysis of relative gene expression data using real-time quantitative PCR and the 2-ΔΔCT method. Methods 2001, 25:402-408.
11. Mbikay M., Seidah N.G., Chretien M. Neuroendocrine secretory protein 7B2: structure, expression and functions. Biochem. J. 2001, 357:329-342.
12. Mentrup B., Weidemann W. The exon-intron organization of the prohormone convertase PC2 gene from the insect Lucilia cuprina. Gene 1999, 237:29-33.
13. Ouimet T., Mammarbachi A., Cloutier T., Seidah N.G., Castellucci V.F. CDNA structure and in situ localization of the Aplysia californica pro-hormone convertase PC2. FEBS Lett. 1993, 330:343-346.
14. Rouille Y., Westermark G., Martin S.K., Steiner D.F. Proglucagon is processed to glucagon by prohormone convertase PC2 in alpha TC1-6 cells. Proc. Nat. Acad. Sci. U.S.A. 1994, 91:3242-3246.
15. Schagger H., von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100kDa. Anal. Biochem. 1987, 166:368-379.
16. Seidah N.G., Chretien M. Eukaryotic protein processing: endoproteolysis of precursor proteins. Curr. Opin. Biotechnol. 1997, 8:602-607.
17. Seidah N.G., Day R., Marcinkiewicz M., Chretien M. Mammalian paired basic amino acid convertases of prohormones and proproteins. Ann. N. Y. Acad. Sci. 1993, 680:135-146.
18. Smit A.B., Spijker S., Geraerts W.P. Molluscan putative prohormone convertases: structural diversity in the central nervous system of Lymnaea stagnalis. FEBS Lett. 1992, 312:213-218.
19. Tangprasittipap A., Tiensuwan M., Withyachumnarnkul B. Characterization of candidate genes involved in growth of black tiger shrimp Penaeus monodon. Aquaculture 2010, 307:150-156.
20. Toullec J.Y., Kamech N., Gallois D., Maibeche M., Papon V., Boscameric M., et al. Molecular cloning and cellular expression of crustacean PC2-like prohormone convertase. Biochim. Biophys. Acta 2002, 1574:145-151.
21. Udomkit A., Treerattrakool S., Panyim S. Crustacean hyperglycemic hormones of Penaeus monodon: cloning, production of active recombinant hormones and their expression in various shrimp tissues. J. Exp. Mar. Biol. Ecol. 2004, 298:79-91.
22. von Heijne G. A new method for predicting signal sequence cleavage sites. Nucleic Acids Res. 1986, 14:4683-4690.
23. Wilson H.E., White A. Prohormones: their clinical relevance. Trends Endocrinol. Metab. 1998, 9:396-402.
24. Zhang X., Pan H., Peng B., Steiner D.F., Pintar J.E., Fricker L.D. Neuropeptidomic analysis establishes a major role for prohormone convertase-2 in neuropeptide biosynthesis. J. Neurochem. 2010, 112:1168-1179.