cDNA cloning and pattern of expression of an adult, female-specific chymotrypsin from Aedes aegypti midgut

Insect Biochemistry and Molecular Biology

Volumn 27, Issue 4, 1997, Pages 283-289

  Jiang, Qijiao ^a   Hall, Martin ^b   Noriega, Fernando G ^a   Wells, Michael ^a  

^a UNIVERSITY OF ARIZONA   (United States)

^b UPPSALA UNIVERSITY   (Sweden)

Author keywords

Aedes aegypti; Chymotrypsin; Mosquito digestion; protease

Indexed keywords

CHYMOTRYPSIN; COMPLEMENTARY DNA; INSECT PROTEIN;

AEDES; AEDES AEGYPTI; AMINO ACID SEQUENCE; ANALYTIC METHOD; ANIMAL; ARTICLE; CATALYSIS; DIGESTION; DIGESTIVE SYSTEM; ENZYME ACTIVITY; ENZYME SPECIFICITY; ENZYMOLOGY; FEMALE; GENE; GENE EXPRESSION; GENE EXPRESSION REGULATION; GENETIC TRANSCRIPTION; GENETICS; MALE; MIDGUT; MOLECULAR CLONING; MOLECULAR DYNAMICS; MOLECULAR GENETICS; NONHUMAN; NUCLEOTIDE SEQUENCE; PROTEIN DEGRADATION; PROTEIN SYNTHESIS REGULATION; RNA TRANSLATION; SEQUENCE HOMOLOGY;

AEDES AEGYPTI; ANIMALIA; INSECTA;

EID: 0031127641     PISSN: 09651748     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0965-1748(97)00001-5     Document Type: Article

References (30)

1. Barillas-Mury C., Graf R., Hagedorn H. H. and Wells M. A. (1991) cDNA and deduced amino acid sequence of a blood meal-induced trypsin from the mosquito, Aedes aegypti. Insect Biochem. 21, 825-831.
2. Barillas-Mury C., Noriega F. G. and Wells M. A. (1995) Early trypsin activity is part of the signal transduction system that activates transcription of the late trypsin gene in the midgut of the mosquito, Aedes aegypti. Insect Biochem. Molec. Biol. 25, 241-246.
3. Barrett A. J. and Rawlings N. D. (1995) Perspectives in biochemistry and biophysics: families and clans of serine peptidases. Arch. Biochem. Biophys. 318, 247-250.
4. Borovsky D. and Schlein Y. (1988) Quantitative determination of trypsin-like and chymotrypsin-like enzymes in insects. Arch. Insect Biochem. Physiol. 8, 249-260.
5. Briegel H. and Lea A. O. (1975) Relationship between protein and proteolytic activity in the midgut of mosquitoes. J. Insect Physiol. 21, 1597-1604.
6. Clements, A. N. (1992) The Biology of Mosquitoes. Vol. 1. Chapman and Hall, London.
7. Craik C. S., Choo Q. L., Swift G. H., Quinto C., Macdonna R. J. and Rutter W. J. (1984) Structure of two related rat pancreatic trypsin genes. J. Biol. Chem. 259, 14255-14264.
8. Del Mar E. G., Largman G., Brodric J. W., Fasset M. and Geokas M. C. (1980) Substrate specificity of human pancreatic elastase 2. Biochemistry 19, 468-472.
9. Felix C. R., Betschart B., Billingsley P. F. and Freyvogel T. A. (1991) Post-feeding induction of trypsin in the midgut of Aedes aegypti L. (Diptera: Culicidae) is separable into two cellular phases. Insect Biochem. 21, 197-203.
10. Feng D. F. and Doolittle R. F. (1987) Progressive sequence alignment as a prerequisite to correct phylogenetic trees. J. Molec. Evol. 25, 351-360.
11. George D. G., Barker W. C. and Hunt L. T. (1990) Mutation data matrix and its uses. Methods Enzymol. 183, 333-351.
12. Gooding R. H. (1969) Studies on proteinases from some blood-sucking insects. Proc. Entomol. Soc. Ontario 100, 139-145.
13. Graf R. and Briegel H. (1982) Comparison between aminopeptidase and trypsin activity in blood-fed females of Aedes aegypti. Rev. Suisse Zool. 89, 845-850.
14. Graf R., Binz H. and Briegel H. (1988) Monoclonal antibodies as probes for Aedes aegypti trypsin. Insect Biochem. 18, 463-470.
15. Hall M., Scott T., Sugumaran M., Söderhäll K. and Law J. H. (1995) Proenzyme of Manduca sexta phenol oxidase: purification, activation, substrate specificity of the active enzyme, and molecular cloning. Proc. Natl. Acad. Sci. U.S.A. 92, 7764-7768.
16. Henikoff S. (1984) Unidirectional digestion with exonuclease III creates targeted breakpoints for DNA sequencing. Gene 28, 351-359.
17. Horler E. and Briegel H. (1995) Proteolytic enzymes of female Anopheles: biphasic synthesis, regulation and multiple feeding. Arch. Insect Biochem. Physiol. 28, 189-205.
18. Jiang, Q. (1996) Cloning and characterization of midgut-specific gene/gene products in the mosquito Aedes aegypti. PhD dissertation. University of Arizona.
19. Kalhok S. E., Tabak L. M., Prosser D. E., Brook W., Downe A. E. and White B. (1993) Isolation, sequencing and characterization of two cDNA clones coding for trypsin-like enzymes from the midgut of Aedes aegypti. Insect Molec. Biol. 2, 71-79.
20. Kunz P. A. (1978a) Resolution and properties of the proteinases in the larva of the mosquito Aedes aegypti. Insect Biochem. 8, 43-51.
21. Kunz P. A. (1978b) Resolution and properties of the proteinases in adult Aedes aegypti. Insect Biochem. 8, 169-175.
22. Muller H.-M., Catteruccia F., Vizioli J., Della Torre A. and Crisanti A. (1995) Constitutive and blood-meal induced trypsin genes in Anophetes gambiae. Exp. Parasitol. 81, 371-385.
23. Noriega F. G. and Wells M. A. (1993) A comparison of three methods for isolating RNA from mosquitoes. Insect Molec. Biol. 2, 21-24.
24. Noriega F. G., Barillas-Mury C. and Wells M. A. (1994) Dietary control of late trypsin gene transcription in Aedes aegypti. Insect Biochem. Molec. Biol 24, 627-631.
25. Noriega F. G., Wang X., Pennington J. E., Barillas-Mury C. and Wells M. A. (1996a) Early trypsin, a female-specific midgut protease in Aedes aegypti: isolation, amino-terminal sequence determination, and cloning and sequencing of the gene. Insect Biochem. Molec. Biol. 26, 119-126.
26. Noriega F. G., Pennington J. E., Barillas-Mury C., Wang X.-Y. and Wells M. A. (1996b) Aedes aegypti midgut early trypsin is post-transcriptionally regulated by blood feeding. Insect Molec. Biol. 5, 25-29.
27. Pennington J. E., Noriega F. G. and Wells M. A. (1995) The expression of early trypsin in Aedes aegypti. J. Cell Biochem. 21A (Suppl.), 211.
28. Sanger F., Nicklen S. and Coulson A. R. (1977) DNA sequencing with chain terminating inhibitors. Proc. Natl. Acad. Sci. U.S.A. 74, 5463-5467.
29. Wilcox P. E. (1970) The serine proteases. Methods Enzymol. 19, 64-108.
30. Yang Y. J. and Davies D. M. (1971) Trypsin and chymotrypsin during metamorphosis in Aedes aegypti and properties of the chymotrypsin. J. Insect. Physiol. 17, 117-131.