Isolation and characterization of a trypsin inhibitor from the skin secretions of Kaloula pulchra hainana

Toxicon

Volumn 56, Issue 4, 2010, Pages 502-507

  Zhang, Yingxia ^a,b,c   Wang, Manchuriga ^b   Wei, Shuangshuang ^b  

^a Minister of Education   (China)

^b HAINAN UNIVERSITY   (China)

^c Hainan Provincial Key Laboratory for Tropical Hydrobiology and Biotechnology   (China)

Author keywords

Amphibian; Inhibitor; Kaloula pulchra hainana; Secretion; Skin; Trypsin

Indexed keywords

CHYMOTRYPSIN; DITHIOTHREITOL; ELASTASE; SUBTILISIN; THROMBIN; TRYPSIN INHIBITOR;

AMINO TERMINAL SEQUENCE; ARTICLE; CONTROLLED STUDY; FEMALE; FROG; GEL FILTRATION CHROMATOGRAPHY; ION EXCHANGE CHROMATOGRAPHY; KALOULA HAINANA; MALE; MOLECULAR WEIGHT; NONHUMAN; PH; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FUNCTION; PROTEIN ISOLATION; PROTEIN PURIFICATION; SKIN SECRETION; TEMPERATURE SENSITIVITY;

AMPHIBIA; ANURA; KALOULA PULCHRA;

EID: 77954953236     PISSN: 00410101     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.toxicon.2010.05.006     Document Type: Article

References (26)

1. Abboud R.T., Vimalanathan S. Pathogenesis of COPD. Part I. The role of protease-antiprotease imbalance in emphysema. Int. J. Tuberc. Lung Dis. 2008, 12:361-367.
2. Ali M.F., Lips K.R., Knoop F.C., Fritzsch B., Miller C., Conlon J.M. Antimicrobial peptides and protease inhibitors in the skin secretions of the crawfish frog, Rana areolata. Biochim. Biophys. Acta 2002, 1601:55-63.
3. Casteels P., Ampe C., Jacobs F., Tempst P. Functional and chemical characterization of Hymenoptaecin, an antibacterial polypeptide that is infection-induciblein the honeybee (Apis mellifera). J. Biol. Chem. 1993, 268:7044-7054.
4. Chen T., Shaw C. Identification and molecular cloning of novel trypsin inhibitor analogs from the dermal venom of the oriental fire-bellied toad (Bombina orientalis) and the European yellow-bellied toad (Bombina variegata). Peptides 2003, 24:873-880.
5. Christensen S., Valnickova Z., Thogersen I.B., Pizzo S.V., Nielsen H.R., Roepstorff P., Enghild J.J. Sodium dodecyl sulfate-stable complexes between serpins and active or inactive proteinases contain the region COOH-terminal to the reactive site loop. J. Biol. Chem. 1995, 270:14859-14862.
6. Clarke B.T. The natural history of amphibian skin secretions, their normal functioning and potential medical applications. Biol. Rev. Cambridge Philos. Soc. 1997, 72:365-379.
7. Conlon J.M., Kim J.B. A protease inhibitor of the Kunitz family from skin secretions of the tomato frog, Dyscophus guineti (Microhylidae). Biochem. Biophys. Res. Commun 2000, 279:961-964.
8. Conlon J.M., Iwamuro S., King J.D. Dermal cytolytic peptides and the system of innate immunity in anurans. Ann. N.Y. Acad. Sci. 2009, 1163:75-82.
9. Daly J.W., Noimai N., Kongkathip B., Kongkathip N., Wilham J.M., Garraffo H.M., Kaneko T., Spande T.F., Nimit Y., Nabhitabhata J., Chan-Ard T. Biologically active substances from amphibians: preliminary studies on anurans from twenty-one genera of Thailand. Toxicon 2004, 44:805-815.
10. Dixon M. The determination of enzyme inhibitor constants. Biochem. J. 1953, 55:170-171.
11. Duellman W.E., Trueb L. Relationship with the environment. Biology of Amphibians 1986, 197-228. McGraw-Hill, New York. W.E. Duellman, L. Trueb (Eds.).
12. Gebhard L.G., Carrizo F.U., Stern A.L., Burgardt N.I., Faivovich J., Lavilla E., Ermácora M.R. A Kazal prolyl endopeptidase inhibitor isolated from the skin of Phyllomedusa sauvagii. Eur. J. Biochem 2004, 271:2117-2126.
13. Han Y., Yu H., Yang X., Rees H.H., Liu J., Lai R. A serine proteinase inhibitor from frog eggs with bacteriostatic activity. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 2008, 149:58-62.
14. Lai R., Liu H., Lee W.H., 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. 2002, 131:47-53.
15. Laskowski M., Qasim M.A. What can the structures of enzyme-inhibitor complexes tell us about the structures of enzyme substrate complexes?. Biochim. Biophys. Acta 2000, 1477:324-337.
16. Li J., Wu J., Wang Y., Xu X., Liu T., Lai R., Zhu H. A small trypsin inhibitor from the frog of Odorrana grahami. Biochimie 2008, 90:1356-1361.
17. Lu C.X., Nan K.J., Lei Y. Agents from amphibians with anticancer properties. Anticancer Drugs 2008, 19:931-939.
18. Lu X., Ma Y., Wu J., Lai R. Two serine protease inhibitors from the skin secretions of the toad, Bombina microdeladigitora. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 2008, 149:608-612.
19. Mebs D., Wagner M.G., Pogoda W., Maneyro R., Kwet A., Kauert G. Lack of bufadienolides in the skin secretion of red bellied toads, Melanophryniscus spp. (Anura, Bufonidae), from Uruguay. Comp. Biochem. Physiol. C Toxicol. Pharmacol. 2007, 144:398-402.
20. Mignogna G., Pascarella S., Wechselberger C., Hinterleitner C., Mollay C., Amiconi G., Barra D., Kreil G. BSTI, a trypsin inhibitor from skin secretions of Bombina bombina related to protease inhibitors of nematodes. Protein Sci. 1996, 5:357-362.
21. Song G., Zhou M., Chen W., Chen T., Walker B., Shaw C. HV-BBI-a novel amphibian skin Bowman-Birk-like trypsin inhibitor. Biochem. Biophys. Res. Commun 2008, 372:191-196.
22. Yang H., Wang X., Liu X., Wu J., Liu C., Gong W., Zhao Z., Hong J., Lin D., Wang Y., Lai R. Antioxidant peptidomics reveals novel skin antioxidant system. Mol. Cell. Proteomics 2009, 8:571-583.
23. You D., Hong J., Rong M., Yu H., Liang S., Ma Y., Yang H., Wu J., Lin D., Lai R. The first gene-encoded amphibian neurotoxin. J. Biol. Chem. 2009, 284:22079-22086.
24. Zhang Y.X., Lai R., Lee W.H., Zhang Y. Frog albumin is expressed in skin and characterized as a novel potent trypsin inhibitor. Protein Sci. 2005, 14:2469-2477.
25. Zhao Y., Jin Y., Wei S.S., Lee W.H., Zhang Y. Purification and characterization of an irreversible serine protease inhibitor from skin secretions of Bufo andrewsi. Toxicon 2005, 46:635-640.
26. Zhao Y., Jin Y., Lee W.H., Zhang Y. Isolation and preliminary characterization of a 22-kDa protein with trypsin inhibitory activity from toad Bufo andrewsi skin. Toxicon 2005, 46:277-281.