Characterization of a highly stable trypsin-like proteinase inhibitor from the seeds of Opuntia streptacantha (O. streptacantha Lemaire)

Phytochemistry

Volumn 70, Issue 11-12, 2009, Pages 1374-1381

  Torres Castillo, J A ^a   Jacobo, C Mondragón ^b   Blanco Labra, A ^a  

^a DEPARTAMENTO DE INGENIERÍA GENÉTICA   (Mexico)

^b Campo Experimental   (Mexico)

Author keywords

Cactaceae; Insect resistance; Opuntia streptacantha; Prickly pear; Proteinase inhibitor; Seed protein; Trypsin inhibitor

Indexed keywords

SERINE PROTEINASE INHIBITOR; TRYPSIN INHIBITOR;

AMINO ACID SEQUENCE; ARTICLE; CHEMISTRY; ENZYMOLOGY; ISOLATION AND PURIFICATION; MASS SPECTROMETRY; MOLECULAR WEIGHT; OPUNTIA; PLANT SEED; SEQUENCE HOMOLOGY; TEMPERATURE;

AMINO ACID SEQUENCE; MASS SPECTROMETRY; MOLECULAR WEIGHT; OPUNTIA; SEEDS; SEQUENCE HOMOLOGY; SERINE PROTEINASE INHIBITORS; TEMPERATURE; TRYPSIN INHIBITORS;

CACTACEAE; HEXAPODA; OPUNTIA; OPUNTIA STREPTACANTHA;

EID: 70349466430     PISSN: 00319422     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.phytochem.2009.08.009     Document Type: Article

References (43)

1. Aguirre C., Valdés-Rodríguez S., Mendoza-Hernández G., Rojo-Domínguez A., and Blanco-Labra A. A novel 8.7 kDa protease inhibitor from chan seeds (Hyptis suaveolens L.) inhibits proteases from the larger grain borer Prostephanus truncatus (Coleoptera: Bostrichidae). Comp. Biochem. Physiol. Part B 138 (2004) 81-89
2. Barret A.J. A new assay for cathepsin B1 and other thiol proteinase. Anal. Biochem. 47 (1972) 280-293
3. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities utilizing the principle of protein dye binding. Anal. Biochem. 72 (1976) 248
4. Carreras M.E., Fuentes E., and Merino E.F. Seed protein patterns of nine species of Cactaceae. Biochem. Syst. Ecol. 5 (1997) 43-49
5. Conners R., Konarev A., Forsyth J., Lovegrove A., Marsh J., Joseph-Horne T., Shewry P., and Brady R.L. An unusual helix-turn-helix protease inhibitory motif in a novel trypsin inhibitor from seeds of Veronica (Veronica hederifolia L.). J. Biol. Chem. 282 (2007) 27760-27768
6. Elanger B., Kokowsky N., and Cohen W. The preparation and properties of two chromogenic substrates of trypsin. Arch. Biochem. Biophys. 95 (1961) 271-278
7. García-Carreño F.L., Dimes L.E., and Haard Norman F. Substrate-gel electrophoresis for composition and molecular weight of proteinases or proteinaceous proteinase inhibitors. Anal. Biochem. 214 (1993) 65-69
8. García-Gasca T., Salazar-Olivo L.A., Mendiola-Olaya E., and Blanco-Labra A. The effects of a proteinase inhibitor fraction from tepary (Phaseolus acutifolius) on in vitro cell proliferation and cell adhesion of transformed cells. Toxicol. In vitro 16 (2002) 229-233
9. Gómez-Hinostrosa C., and Hernández H.M. Diversity, geographical distribution, and conservation of Cactaceae in the Mier y Noriega region, Mexico. Biodivers. Conserv. 9 (2000) 403-418
10. Hivrale V.K., Chougule N.P., Chhabda P.J., Giri A.P., and Kachole M.S. Unraveling biochemical properties of cockroach (Periplaneta americana) proteinases with a gel X-ray film contact print method. Comp. Biochem. Physiol. Part B 141 (2005) 261-266
11. Jones B. The endogenous endoprotease inhibitors of barley and malt and their roles in malting and brewing. J. Cereal Sci. 42 (2005) 271-280
12. Kang S.-H., and Fuchs M.S. An improvement in the hummel chymotrypsin assay. Anal. Biochem. 54 (1973) 262-265
13. Kennedy R.C. The Bowman-Birk inhibitor from soybeans as an anticarcinogenic agent. Am. J. Clin. Nutr. 68 (1998) 1406S-1412S
14. Kim M., Park S., Kim J., Lee S.Y., Lim H.T., Cheong H., Kyung-Soo Hahm K., and Pak Y. Purification and characterization of a heat-stable serine protease inhibitor from the tubers of new potato variety "Golden Valley". Biochem. Biophys. Res. Commun. 346 3 (2006) 681-686
15. Koh C.Y., Kazimirova M., Trimnell A., Takac P., Labuda M., Nuttall P.A., and Kini R.M. Variegin, a novel fast and tight binding thrombin inhibitor from the tropical Bont tick. J. Biol. Chem. 282 40 (2007) 29101-29113
16. Konarev A., Anisimova I.N., Gavrilova V.A., Rozhkova V.T., Fido R., Tatham A.S., and Shewry P.R. Novel proteinase inhibitors in seeds of sunflower (Helianthus annuus L.): polymorphism, inheritance and properties. Theor. Appl. Genet. 100 (2000) 82-88
17. Konarev A., Anisimova I., Gavrilova V., Vachrusheva T.E., Yu Konechnaya G., Lewis M., and Shewry P. Serine proteinase inhibitors in the Compositae: distribution, polymorphism and properties. Phytochemistry 59 (2002) 279-291
18. Konarev A., Tomooka N., and Vaughan D.A. Proteinase inhibitor polymorphism in the genus Vigna subgenus Ceratotropis and its biosystematic implications. Euphytica 123 (2002) 165-177
19. Konarev A.V., Griffin J., Konechnaya G.Y., and Shewry P. The distribution of serine proteinase inhibitors in seeds of the Asteridae. Phytochemistry 65 (2004) 3003-3020
20. Konarev A., Lovegrove A., and Shewry P. Serine proteinase inhibitors in seeds of Cycas siamensis and other gymnosperms. Phytochemistry 69 (2008) 2482-2489
21. Lawrence P.K., and Koundal K.R. Plant protease inhibitors in control of phytophagous insects. Electron. J. Biotechnol. 5 (2002) 1-17
22. López-García, J.J., Fuentes-Rodríguez, J.M., Rodríguez, R.A., 2001. Production and use of Opuntia as forage in northern Mexico. In: Candelario Mondragón Jacobo, Salvador Pérez-González (Eds.), Cactus (Opuntia spp.) as Forage. FAO 169, Rome, Italy.
23. Mello M., Tanaka A., and Silva-Filho M. Molecular evolution of Bowman-Birk type proteinase inhibitors in flowering plants. Mol. Phylogenet. Evol. 27 (2003) 103-112
24. Mohamed-Yasseen Y., Barringer S., and Splittstoesser W.E. A note on the uses of Opuntia spp. in Central/North America. J. Arid Environ. 32 (1996) 347-353
25. Mondragon J.C. Verification of the apomictic origin of cactus pear (Opuntia spp. Cactaceae) seedlings of open pollinated and crosses from Central Mexico. J. PACD (2001) 49-56
26. Nerd A., and Nobel P.S. Water relations during ripening for fruit of well-watered versus water-stressed Opuntia ficus-indica. J. Am. Soc. Hort. Sci. 125 (2000) 653-657
27. Nobel P.S., and Zutta B.R. Temperature tolerances for stems and roots of two cultivated cacti, Nopalea cochenillifera and Opuntia robusta: acclimation, light, and drought. J. Arid Environ. 72 5 (2007) 633-642
28. Ortega-Baes P., and Godínez-Alvarez H. Global diversity and conservation priorities in the Cactaceae. Biodivers. Conserv. 15 (2006) 817-827
29. Otlewski J., and Krowarsch D. Squash inhibitor family of serine proteinases. Acta Biochim. Pol. 43 (1996) 431-444
30. Pernas M., Sánchez-Monge R., and Salcedo G. Biotic and abiotic stress can induce cystatin expression in chestnut. FEBS Lett. 467 (2000) 206-210
31. Qi R., Song Z., and Chi C. Structural features and molecular evolution of Bowman-Birk protease inhibitors and their potential application. Acta Biochim. Biophys. Sinica 37 (2005) 283-292
32. Rawlings, N.D., Morton, F.R., Kok, C.Y., Kong, J., Barrett, A.J., 2008. MEROPS: the peptidase database. Nucl. Acid Res. 36(database issue), 320-325.
33. Rodríguez Macedo M.L., Mara de Saa C., Machado Freire C.M., and Postali Parra J.R. A Kunitz-type inhibitor of Coleopteran proteases, isolated from Adenanthera pavonina L. seeds and its effect on Callosobruchus maculatus. J. Agric. Food Chem. 5 (2004) 2533-2540
34. Ruseler-van E.J.G.H., Lieshout L.M.C., Smits S.A., Kessel I., and Laman J.D. Potato tuber proteins efficiently inhibited human faecal proteolytic activity: implications for treatment of peri-anal dermatitis. Eur. J. Clin. Invest. 34 (2004) 303-311
35. Sakamoto Y., Suzuki M., Kanayama N., and Terao T. Suppression of urokinase expression and invasion by a soybean Kunitz trypsin inhibitor are mediated through inhibition of src-dependent signaling pathways. J. Biol. Chem. 280 (2005) 31428-31437
36. Salzet M., Chopin V., Baerti J., Matias I., and Malecha J. Theromin, a novel leech thrombin inhibitor. J. Biol. Chem. 275 40 (2000) 30774-30780
37. Sawano Y., Hatano K., Miyakawa T., Komagata H., Miyauchi Y., Yamazaki H., and Tanokura M. Proteinase inhibitor from Ginkgo seeds is a member of the plant nonspecific lipid transfer protein gene family. Plant Physiol. 146 (2008) 1909-1919
38. Schägger H., and Von Jagow G. Tricine-sodium dodecyl sulfate-poliacryamide gel eletrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 66 (1987) 368-379
39. Shewry P.R. Enzyme inhibitors of seeds: types and properties. In: Shewry P.R., and Casey R. (Eds). Seed Proteins (1999), Kluwer Academic Publishers, The Netherlands 587-615
40. Tiffin P., and Gaut B. Molecular evolution of the wound-induced serine protease inhibitor wip1in Zea and related genera. Mol. Biol. Evol. 18 (2001) 2092-2101
41. Uchoa A.F., Souza P.A.S., Zarate R.M.L., Gomes-Filho E., and Campos F.A.P. Isolation and characterization of a reserve protein from the seeds of Opuntia ficus-indica (Cactaceae). Braz. J. Med. Biol. Res. 31 (1998) 757-761
42. Valueva T.A., and Mosolov V.V. Role of inhibitors of proteolytic enzymes in plant defense against phytopathogenic microorganisms. Biochemistry (Moscow) 69 (2004) 1305-1309
43. Vega-Villasante F., Chiapa-Cortés C.I., Rocha S., Romero-Schmidt H.L., and Nolasco H. Nutritional quality and ecological impact of the use of Ferocactus peninsulae, Opuntia cholla and other desert plants as cattle forage in the Baja California peninsula. J. Arid Environ. 35 (1997) 499-509