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Biochemistry & Molecular Biology

Purification, cDNA cloning and characterization of Kunitz-type protease inhibitors from Apios americana tubers

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Pages 563-574 | Received 08 Oct 2019, Accepted 18 Nov 2019, Published online: 02 Dec 2019

References

  • Musgrave ME, Blackmon WJ. Respiration in a new tuber crop, Apios americana. J Am Soc Hortic Sci. 1995;120(4):656–660.
  • Asch DL, Hart JP. Crop domestication in prehistoric Eastern North America. In: Goodman RM, editor. Encyclopedia of plant and crop science. New York: Marcel Dekker; 2004. p. 314–319.
  • Kikuta C, Sugimoto Y, Konishi Y, et al. Physicochemical and structural properties of starch isolated from Apios americana Medikus. J Appl Glycosci. 2011;59(1):21–30.
  • Carlisi J, Wollard D. History, culture, and nutrition of Apios americana. J Nutraceuticals, Funct Med Foods. 2004;4(3-4):85–92. Haworth Press Inc..
  • Belamkar V, Farmer AD, Weeks NT, et al. Genomics-assisted characterization of a breeding collection of Apios americana, an edible tuberous legume. Sci Rep. 2016;6:34908.
  • Belamkar V, Wenger A, Kalberer SR, et al. Evaluation of phenotypic variation in a collection of: an edible tuberous legume. Crop Sci. 2015;55(2):712–726.
  • Iwai K, Matsue H. Ingestion of Apios americana Medikus tuber suppresses blood pressure and improves plasma lipids in spontaneously hypertensive rats. Nutr Res. 2007;27(4):218–224.
  • Kuramoto S, Kaneyoshi G, Morinaga Y, et al. Angiotensin-converting enzyme-inhibitory peptides isolated from pepsin hydrolyzate of Apios americana tuber and their hypotensive effects in spontaneously hypertensive rats. Food Sci Technol Res. 2013;19(3):399–407.
  • Chu Q, Chen M, Song D, et al. Apios americana Medik flowers polysaccharide (AFP-2) attenuates H2O2 induced neurotoxicity in PC12 cells. Int J Biol Macromol. 2019;123:1115–1124.
  • Yan F, Yang Y, Yu L, et al. Effects of C-glycosides from Apios americana leaves against oxidative stress during hyperglycemia through regulating mitogen-activated protein kinases and nuclear factor erythroid 2-related factor 2. J Agric Food Chem. 2017;65(34):7457–7466.
  • Zhang Y, Kouzuma Y, Miyaji T, et al. Purification, characterization, and cDNA cloning of a Bowman-Birk type trypsin inhibitor from Apios americana Medikus tubers. Biosci Biotechnol Biochem. 2008;72(1):171–178.
  • Zhang Y, Zhou C, Tang S, et al. Effect of AATI, a Bowman-Birk type inhibitor from Apios americana, on proliferation of cancer cell lines. Food Chem. 2011;128(4):909–915.
  • Srikanth S, Chen Z. Plant protease inhibitors in therapeutics-focus on cancer therapy. Front Pharmacol. 2016;7:470.
  • Cristina Oliveira de Lima V, Piuvezam G, Leal Lima Maciel B, et al. Trypsin inhibitors: promising candidate satietogenic proteins as complementary treatment for obesity and metabolic disorders? J Enzyme Inhib Med Chem. 2019;34(1):405–419.
  • Haq SK, Atif SM, Khan RH. Protein proteinase inhibitor genes in combat against insects, pests, and pathogens: natural and engineered phytoprotection. Arch Biochem Biophys. 2004;431(1):145–159.
  • Kouzuma Y, Irie S, Yamazaki R, et al. Purification and cDNA cloning of a lectin and a lectin-like protein from Apios americana Medikus tubers. Biosci Biotechnol Biochem. 2014;78(4):574–581.
  • Filippova IY, Lysogorskaya EN, Oksenoit ES, et al. L-Pyroglutamyl-L-phenylalanyl-L-leucine-p-nitroanilide—a chromogenic substrate for thiol proteinase assay. Anal Biochem. 1984;143(2):293–297.
  • Bunyatang O, Chirapongsatonkul N, Bangrak P, et al. Molecular cloning and characterization of a novel bi-functional alpha-amylase/subtilisin inhibitor from Hevea brasiliensis. Plant Physiol Biochem. 2016;101:76–87.
  • Stein RL. Catalysis by human leukocyte elastase: substrate structural dependence of rate-limiting protolytic catalysis and operation of the charge relay system. J Am Chem Soc. 1983;105(15):5111–5116.
  • Bieth J. Some kinetic consequences of the tight binding of protein-proteinase-inhibitors to proteolytic enzymes and their application to the determination of dissociation constants. Berlin, Heidelberg: Springer; 1974. ( (Proteinase Inhibitors)).
  • Schägger H. Tricine–SDS-PAGE. Nat Protoc. 2006;1:16–22.
  • Towbin H, Staehelin T, Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A. 1979;76(9):4350–4354.
  • Shimizu Y, Yamazaki H, Yoshida S, et al. Molecular cloning, functional expression, and characterization of isolectin genes of hemolytic lectin CEL-III from the marine invertebrate Cucumaria echinata. Biosci Biotechnol Biochem. 2012;76(2):276–282.
  • Jiménez T, Martín I, Hernández-Nistal J, et al. The accumulation of a Kunitz trypsin inhibitor from chickpea (TPI-2) located in cell walls is increased in wounded leaves and elongating epicotyls. Physiol Plant. 2008;132(3):306–317.
  • Schoofs L, Clynen E, Trypsin SM. Chymotrypsin inhibitors in insects and gut leeches. Curr Pharm Des. 2002;8(7):483–491.
  • Zhou D, Lobo YA, Batista IF, et al. Crystal structures of a plant trypsin inhibitor from Enterolobium contortisiliquum (EcTI) and of its complex with bovine trypsin. PLoS One. 2013;8(4):e62252.
  • Ozawa K, Michael L. The reactive site of trypsin inhibitors. J Biol Chem. 1966;241(17):3955–3961.
  • Kouzuma Y, Yamasaki N, Kimura M. Th e tissue-type plasminogen activator inhibitor ETIa from Erythrina variegata: structural basis for the inhibitory activity by cloning, expression, and mutagenesis of the cDNA encoding ETIa. J Biochem. 1997;121(3):456–463.
  • Kouzuma Y, Yamasaki N, Kimura M. Cloning, expression, and mutagenesis of trypsin inhibitor ETIb from Erythrina variegata seeds. Biosci Biotechnol Biochem. 1997;61(6):1041–1043.
  • Srinivasan A, Giri AP, Harsulkar AM, et al. A Kunitz trypsin inhibitor from chickpea (Cicer arietinum L.) that exerts anti-metabolic effect on podborer (Helicoverpa armigera) larvae. Plant Mol Biol. 2005;57(3):359–374.
  • Rashed NA, Macdonald MH, Matthews BF. Protease inhibitor expression in soybean roots exhibiting susceptible and resistant interactions with soybean cyst nematode. J Nematol. 2008;40(2):138.
  • Christopher A, Virginia S, Alan D, et al. Molecular cloning and pattern of expression of an α-L-fucosidase gene from pea seedlings. J Biol Chem. 1995;270(42):24839–24843.
  • Tarragó T, Martínez I, Torrent M, et al. The fuc1 gene product (20 kDa FUC1) of Pisum sativum has no α-L-fucosidase activity. Plant Mol Biol. 2003;51(6):877–884.
  • Terada S, Fujimura S, Katayama H, et al. Purification and characterization of two kunitz family subtilisin inhibitors from seeds of Canavalia lineata. J Biochem. 1994;115(3):392–396.
  • Terada S, Katayama H, Noda K, et al. Amino acid sequences of kunitz family subtilisin inhibitors from seeds of Canavalia lineata. J Biochem. 1994;115(3):397–404.
  • Brandao-Costa RMP, Araujo VF, Porto ALF. CgTI, a novel thermostable Kunitz trypsin-inhibitor purified from Cassia grandis seeds: purification, characterization and termiticidal activity. Int J Biol Macromol. 2018;118(Pt B):2296–2306.
  • de Oliveira CFR, Oliveira CT, Taveira GB, et al. Characterization of a Kunitz trypsin inhibitor from Enterolobium timbouva with activity against Candida species. Int J Biol Macromol. 2018;119:645–653.
  • Valueva Tatyana A, Revina Tatyana A, Kladnitskaya Galina V, et al. Kunitz-type proteinase inhibitors from intact and Phytophthora- infected potato tubers. FEBS Lett. 1998;426(1):131–134.
  • Valueva TA, Revina TA, Mosolov VV, et al. Primary structure of potato Kunitz-type serine proteinase inhibitor. Biol Chem. 2000;381(12):1215–1221.
  • Pouvreau L, Gruppen H, Van Koningsveld GA, et al. The most abundant protease inhibitor in potato tuber (cv. Elkana) is a serine protease inhibitor from the Kunitz family. J Agric Food Chem. 2003;51(17):5001–5005.
  • Batista IFC, Oliva MLV, Araujo MS, et al. Primary structure of a kunitz-type trypsin inhibitor from Enterolobium contortisiliquum seeds. Phytochemistry. 1996;41(4):1017–1022.
  • Wu HC, Lin JY. The complete amino acid sequence of a kunitz family trypsin inhibitor from seeds of acacia confusa. J Biochem. 1993;113(2):258–263.
  • Lin JY, Chu SC, Wu HC, et al. Trypsin inhibitor from the seeds of Acacia confusa. J Biochem. 1991;110(6):879–883.
  • Habib H, Fazili KM. Plant protease inhibitors: a defense strategy in plants. Biotechnol Mol Biol Rev. 2007;2(3):68–85.

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