A small trypsin inhibitor from the frog of Odorrana grahami

Biochimie

Volumn 90, Issue 9, 2008, Pages 1356-1361

  Li, Jianxu ^a,d   Wu, Jing ^a,d   Wang, Yipeng ^b,d   Xu, Xueqing ^b,d   Liu, Tongguang ^a   Lai, Ren ^a,b   Zhu, Huajie ^c  

^a KUNMING INSTITUTE OF ZOOLOGY   (China)

^b AGRO ENVIRONMENTAL PROTECTION INSTITUTE   (China)

^c KUNMING INSTITUTE OF BOTANY   (China)

^d UNIVERSITY OF CHINESE ACADEMY OF SCIENCES   (China)

Author keywords

Amphibian; Odorrana grahami; Serine protease inhibitor

Indexed keywords

SERINE PROTEINASE; SERINE PROTEINASE INHIBITOR; TRYPSIN INHIBITOR;

AMINO ACID SEQUENCE; ARTICLE; CIRCULAR DICHROISM; DNA SYNTHESIS; ENZYME INHIBITION; FROG; MASS SPECTROMETRY; MOLECULAR CLONING; NONHUMAN; PROTEIN ANALYSIS; PROTEIN PURIFICATION; PROTEIN SECONDARY STRUCTURE; SKIN SECRETION;

AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; CLONING, MOLECULAR; CONSERVED SEQUENCE; FEMALE; MALE; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, SECONDARY; RANIDAE; SEQUENCE ALIGNMENT; TRYPSIN; TRYPSIN INHIBITORS;

AMPHIBIA; ANURA; RANA GRAHAMI;

EID: 47749117189     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2008.04.005     Document Type: Article

References (25)

1. Laskowski Jr. M., and Qasim M.A. What can the structures of enzyme-inhibitor complexes tell us about the structures of enzyme substrate complexes?. Biochim. Biophys. Acta. 1477 (2000) 324-337
2. Bode W., and Huber R. Natural protein proteinase inhibitors and their interaction with proteinases. Eur. J. Biochem. 204 (1992) 433-451
3. Christeller J.T. Evolutionary mechanisms acting on proteinase inhibitor variability. FEBS J. 272 (2005) 5710-5722
4. Korsinczky M.L., Schirra H.J., Rosengren K.J., West J., Condie B.A., Otvos L., Anderson M.A., and Craik D.J. Solution structures by 1H NMR of the novel cyclic trypsin inhibitor SFTI-1 from sunflower seeds and an acyclic permutant. J. Mol. Biol. 311 (2001) 579-591
5. Mulvenna J.P., Foley F.M., and Craik D.J. Discovery, structural determination, and putative processing of the precursor protein that produces the cyclic trypsin inhibitor sunflower trypsin inhibitor 1. J. Biol. Chem. 280 (2005) 32245-32253
6. Hernandez J.F., Gagnon J., Chiche L., Nguyen T.M., Andrieu J.P., Heitz A., Trinh Hong T., Pham T.T., and Le Nguyen D. Squash trypsin inhibitors from Momordica cochinchinensis exhibit an atypical macrocyclic structure. Biochemistry 39 (2000) 5722-5730
7. Miyamoto K., Tsujibo H., Hikita Y., Tanaka K., Miyamoto S., Hishimoto M., Ima C., Kamei K., Hara S., and Inamori Y. Cloning and nucleotide sequence of the gene encoding a serine proteinase inhibitor named marinostatin from a marine bacterium, Alteromonas sp. strain B-10-31. Biosci. Biotechnol. Biochem. 62 (1998) 2446-2449
8. Richardson J.S. The anatomy and taxonomy of protein structure. Adv. Protein Chem. 34 (1981) 167-339
9. Qi R.F., Song Z.W., and Chi C.W. Structural features and molecular evolution of Bowman-Birk protease inhibitors and their potential application. Acta Biochim. Biophys. Sin. (Shanghai) 37 (2005) 283-292
10. Li J., Zhang C., Xu X., Wang J., Yu H., Lai R., and Gong W. Trypsin inhibitory loop is an excellent lead structure to design serine protease inhibitors and antimicrobial peptides. FASEB J. 21 (2007) 2466-2473
11. Han J., Zhang L., Shao X., Shi J., and Chi C. The potent inhibitory activity of histone H1.2 C-terminal fragments on furin. FEBS J. 273 (2006) 4459-4469
12. Dixon B.M. The determination of enzyme inhibitor constants. Biochem. J. 55 (1953) 170-171
13. van Gent D., Sharp P., Morgan K., and Kalsheker N. Serpins: structure, function and molecular evolution. Int. J. Biochem. Cell Biol. 35 (2003) 1536-1547
14. Mizuguchi J., Utsunomiya N., Nakanishi M., Arata Y., and Fukazawa H. Differential sensitivity of anti-IgM-induced and NaF-induced inositol phospholipid metabolism to serine protease inhibitors in BAL17 B lymphoma cells. Biochem. J. 263 (1989) 641-646
15. Guerrini M., Guglieri S., Beccati D., Torri G., Viskov C., and Mourier P. Conformational transitions induced in heparin octasaccharides by binding with antithrombin III. Biochem, J. 399 (2006) 191-198
16. Higgins P.J., Staiano-Coico L., and Ryan M.P. Cell-shape-dependent modulation of p52 (PAI-1) gene expression involves a secondary response pathway. Biochem. J. 306 Pt 2 (1995) 497-504
17. Bevins C.L., and Zasloff M. Peptides from frog skin. Annu. Rev. Biochem. 59 (1990) 395-414
18. Erspamer V., Melchiorri P., Broccardo M., Erspamer G.F., Falaschi P., Improota G., Negr L., and Ren T. The brain-gut-skin triangle: new peptides. Peptides Suppl. 2 (1981) 7-16
19. Anastasi A., Erspamer V., and Bucci M. Isolation and structure of bombesin and alytesin, 2 analogous active peptides from the skin of the European amphibians Bombina and Alytes. Experientia 27 (1971) 166-167
20. Lai R., Liu H., Lee W.H., and Zhang Y. A novel bradykinin-related peptide from skin secretions of toad Bombina maxima and its precursor containing six identical copies of the final product. Biochem. Biophys. Res. Commun. 286 (2001) 259-263
21. Severini C., Improta G., Falconieri-Erspamer G., Salvadori S., and Erspamer V. The tachykinin peptide family. Pharmacol. Rev. 54 (2002) 285-322
22. Chen T., Reid C.N., Walker B., Zhou M., Shaw C., and Kasinakinin S. a novel histamine-releasing heptadecapeptide from frog (Kassina senegalensis) skin secretion. Biochem. Biophys. Res. Commun. 337 (2005) 474-480
23. Mignogna G., Pascarella S., Wechselberger C., Hinterleitner C., Mollay C., Amiconi G., Barra D., and Kreil G. Bsti, a trypsin inhibitor from skin secretions of Bombina bombina related to protease inhibitors of nematodes. Protein Sci. 5 (1996) 357-362
24. Conlon J.M., and Kim J.B. A protease inhibitor of the Kunitz family from skin secretions of the tomato frog, Dyscophus guineti (Microhylidae). Biochem. Biophys. Res. Commun. 279 (2000) 961-964
25. Lai R., Liu H., Lee W.H., and Zhang Y. Identification and cloning of a trypsin inhibitor from skin secretions of Chinese red-belly toad Bombina maxima. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 131 (2002) 47-53