메뉴 건너뛰기




Volumn 386, Issue 6, 2005, Pages 561-568

Kunitz-type Bauhinia bauhinioides inhibitors devoid of disulfide bridges: Isolation of the cDNAs, heterologous expression and structural studies

Author keywords

Cathepsins; Cruzipain; Elastase; Gene; Kallikreins; Proteinase inhibitors

Indexed keywords

APROTININ; CATHEPSIN G; CATHEPSIN L; COMPLEMENTARY DNA; CRUZIPAIN; CYSTEINE PROTEINASE INHIBITOR; DISULFIDE; KALLIKREIN; KALLIKREIN INHIBITOR; LEUKOCYTE ELASTASE; NICKEL; PANCREATIC ELASTASE; PLANT DNA; PLASMIN; SERINE PROTEINASE INHIBITOR; SIGNAL PEPTIDE;

EID: 26844473090     PISSN: 14316730     EISSN: 14316730     Source Type: Journal    
DOI: 10.1515/BC.2005.066     Document Type: Article
Times cited : (58)

References (41)
  • 2
    • 0020541585 scopus 로고
    • Cystatin, a protein inhibitor of cysteine proteinases. Improved purification from egg white, characterization, and detection in chicken serum
    • Anastasi, A., Brown, M.A., Kembhavi, A.A., Nicklin, M.J.H., Sayers, C.A., Sunter, D.C., and Barret, A.J. (1983). Cystatin, a protein inhibitor of cysteine proteinases. Improved purification from egg white, characterization, and detection in chicken serum. Biochem. J. 211, 219-238.
    • (1983) Biochem. J. , vol.211 , pp. 219-238
    • Anastasi, A.1    Brown, M.A.2    Kembhavi, A.A.3    Nicklin, M.J.H.4    Sayers, C.A.5    Sunter, D.C.6    Barret, A.J.7
  • 4
    • 0033919241 scopus 로고    scopus 로고
    • Unique features of the plant vacuolar sorting machinery
    • Bassham, D.C. and Raikhel, N.V. (2000). Unique features of the plant vacuolar sorting machinery. Curr. Opin. Cell Biol. 12, 491-495.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 491-495
    • Bassham, D.C.1    Raikhel, N.V.2
  • 5
    • 0024571818 scopus 로고
    • Human leukocyte and porcine pancreatic elastase: X-ray crystal structures, mechanism, substrate specificity, and mechanism-based inhibitors
    • Bode, W., Meyer, E. Jr., and Powers, J.C. (1989). Human leukocyte and porcine pancreatic elastase: X-ray crystal structures, mechanism, substrate specificity, and mechanism-based inhibitors. Biochemistry 28, 1951-1963.
    • (1989) Biochemistry , vol.28 , pp. 1951-1963
    • Bode, W.1    Meyer Jr., E.2    Powers, J.C.3
  • 6
    • 0031260101 scopus 로고    scopus 로고
    • The adaptation of insects to plant protease inhibitors
    • Bolter, C. and Jongsma, M.A. (1997). The adaptation of insects to plant protease inhibitors. J. Insect Physiol. 43, 885-895.
    • (1997) J. Insect Physiol. , vol.43 , pp. 885-895
    • Bolter, C.1    Jongsma, M.A.2
  • 7
    • 0030744398 scopus 로고    scopus 로고
    • A comparison of the enzymatic properties of the major cysteine proteinases from Trypanosoma congolense and Trypanosoma cruzi
    • Chagas, J.R., Authié, E., Serveau, C., Lalmanach, G., Juliano, L., and Gauthier, F. (1997). A comparison of the enzymatic properties of the major cysteine proteinases from Trypanosoma congolense and Trypanosoma cruzi. Mol. Biochem. Parasitol. 88, 85-94.
    • (1997) Mol. Biochem. Parasitol. , vol.88 , pp. 85-94
    • Chagas, J.R.1    Authié, E.2    Serveau, C.3    Lalmanach, G.4    Juliano, L.5    Gauthier, F.6
  • 9
    • 0024212067 scopus 로고
    • Rapid production of full-length cDNAs from rare transcripts: Amplification using a single gene-specific oligonucleotide primer
    • Frohman, M.A., Dush, M.K., and Martin, G.R. (1988). Rapid production of full-length cDNAs from rare transcripts: amplification using a single gene-specific oligonucleotide primer. Proc. Natl. Acad. Sci. USA 85, 8998-9002.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 8998-9002
    • Frohman, M.A.1    Dush, M.K.2    Martin, G.R.3
  • 11
    • 0032004129 scopus 로고    scopus 로고
    • In vivo responses of honey bee midgut proteases to two protease inhibitors from potato
    • Gatehouse, H.S., Christeller, J.T., Burgess, E.P., and Malone, L.A. (1998). In vivo responses of honey bee midgut proteases to two protease inhibitors from potato. J. Insect Physiol. 44, 141-147.
    • (1998) J. Insect Physiol. , vol.44 , pp. 141-147
    • Gatehouse, H.S.1    Christeller, J.T.2    Burgess, E.P.3    Malone, L.A.4
  • 12
    • 0032718660 scopus 로고    scopus 로고
    • Protein storage bodies and vacuoles
    • Herman, E.M. and Larkins, B.A. (1999). Protein storage bodies and vacuoles. Plant Cell 11, 601-613.
    • (1999) Plant Cell , vol.11 , pp. 601-613
    • Herman, E.M.1    Larkins, B.A.2
  • 13
    • 15244361469 scopus 로고    scopus 로고
    • Contribution of conserved Asn residues to the inhibitory activities of Kunitz-type protease inhibitors from plants
    • Iwanaga, S., Yamasaki, N., Kimura, M., and Kouzuma, Y. (2005). Contribution of conserved Asn residues to the inhibitory activities of Kunitz-type protease inhibitors from plants. Biosci. Biotechnol. Biochem. 69, 220-223.
    • (2005) Biosci. Biotechnol. Biochem. , vol.69 , pp. 220-223
    • Iwanaga, S.1    Yamasaki, N.2    Kimura, M.3    Kouzuma, Y.4
  • 14
    • 0029078878 scopus 로고
    • Isolation and characterization of guamerin, a new human leukocyte elastase inhibitor from Hirudo nipponia
    • Jung, H.I., Kim, S.I., Ha, K.S., Joe, C.O., and Kang, K.W. (1995). Isolation and characterization of guamerin, a new human leukocyte elastase inhibitor from Hirudo nipponia. J. Biol. Chem. 270, 13879-13884.
    • (1995) J. Biol. Chem. , vol.270 , pp. 13879-13884
    • Jung, H.I.1    Kim, S.I.2    Ha, K.S.3    Joe, C.O.4    Kang, K.W.5
  • 15
    • 0038089955 scopus 로고    scopus 로고
    • Substrate specificity of chymotrypsin. Study of induced strain by molecular mechanics
    • Kallies, B. and Mitzner, R. (1996). Substrate specificity of chymotrypsin. Study of induced strain by molecular mechanics. J. Mol. Model. 2, 149-159.
    • (1996) J. Mol. Model. , vol.2 , pp. 149-159
    • Kallies, B.1    Mitzner, R.2
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 17
    • 0038089976 scopus 로고    scopus 로고
    • Selection of chymotrypsin inhibitors from a conformationally constrained combinatorial peptide library
    • McBride, J.D., Freeman, N., Domingo, G.J., and Leatherbarrow, R.J. (1996). Selection of chymotrypsin inhibitors from a conformationally constrained combinatorial peptide library. J. Mol. Biol. 259, 819-827.
    • (1996) J. Mol. Biol. , vol.259 , pp. 819-827
    • McBride, J.D.1    Freeman, N.2    Domingo, G.J.3    Leatherbarrow, R.J.4
  • 18
    • 0026556882 scopus 로고
    • β-Trefoil fold. Patterns of structure and sequence in the Kunitz inhibitors, interleukins 1β and 1α and fibroblast growth factors
    • Murzin, A.G., Lesk, A.M., and Chothia, C. (1992). β-Trefoil fold. Patterns of structure and sequence in the Kunitz inhibitors, interleukins 1β and 1α and fibroblast growth factors. J. Mol. Biol. 223, 531-543.
    • (1992) J. Mol. Biol. , vol.223 , pp. 531-543
    • Murzin, A.G.1    Lesk, A.M.2    Chothia, C.3
  • 19
    • 0038148068 scopus 로고    scopus 로고
    • Effect of plant Kunitz inhibitors from Bauhinia bauhinioides and Bauhinia rufa on pulmonary edema caused by activated neutrophils
    • Neuhof, C., Oliva, M.L., Maybauer, D., Maybauer, M., de Oliveira, C., Sampaio, M.U., Sampaio, C.A., and Neuhof, H. (2003). Effect of plant Kunitz inhibitors from Bauhinia bauhinioides and Bauhinia rufa on pulmonary edema caused by activated neutrophils. Biol. Chem. 384, 939-944.
    • (2003) Biol. Chem. , vol.384 , pp. 939-944
    • Neuhof, C.1    Oliva, M.L.2    Maybauer, D.3    Maybauer, M.4    de Oliveira, C.5    Sampaio, M.U.6    Sampaio, C.A.7    Neuhof, H.8
  • 20
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen, H., Engelbrecht, J., Brunak, S., and von Heijne, G. (1997). Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 10, 1-6.
    • (1997) Protein Eng. , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    von Heijne, G.4
  • 22
    • 0032706011 scopus 로고    scopus 로고
    • Characterization of a tissue kallikrein inhibitor isolated from Bauhinia bauhinioides seeds: Inhibition of the hydrolysis of kininogen related substrates
    • Oliva, M.L., Mendes, C.R., Juliano, M.A., Chagas, J.R., Rosa, J.C., Greene, L.J., Sampaio, M.U., and Sampaio, C.A.M. (1999). Characterization of a tissue kallikrein inhibitor isolated from Bauhinia bauhinioides seeds: inhibition of the hydrolysis of kininogen related substrates. Immunopharmacology 45, 163-169.
    • (1999) Immunopharmacology , vol.45 , pp. 163-169
    • Oliva, M.L.1    Mendes, C.R.2    Juliano, M.A.3    Chagas, J.R.4    Rosa, J.C.5    Greene, L.J.6    Sampaio, M.U.7    Sampaio, C.A.M.8
  • 23
    • 0034935397 scopus 로고    scopus 로고
    • Bauhinia bauhinioides plasma kallikrein inhibitor: Interaction with synthetic peptides and fluorogenic peptide substrates related to the reactive site sequence
    • Oliva, M.L., Mendes, C.R., Santomauro-Vaz, E.M., Juliano, M.A., Mentele, R., Auerswald, E.A., Sampaio, M.U., and Sampaio, C.A.M. (2001a). Bauhinia bauhinioides plasma kallikrein inhibitor: interaction with synthetic peptides and fluorogenic peptide substrates related to the reactive site sequence. Curr. Med. Chem. 8, 977-984.
    • (2001) Curr. Med. Chem. , vol.8 , pp. 977-984
    • Oliva, M.L.1    Mendes, C.R.2    Santomauro-Vaz, E.M.3    Juliano, M.A.4    Mentele, R.5    Auerswald, E.A.6    Sampaio, M.U.7    Sampaio, C.A.M.8
  • 24
    • 0035116666 scopus 로고    scopus 로고
    • Synthetic peptides and fluorogenic substrates related to the reactive site sequence of Kunitz-type inhibitors isolated from Bauhinia: Interaction with human plasma kallikrein
    • Oliva, M.L., Santomauro-Vaz, E.M., Andrade, S.A., Juliano, M.A., Pott, V.J., Sampaio, M.U., and Sampaio, C.A.M. (2001b). Synthetic peptides and fluorogenic substrates related to the reactive site sequence of Kunitz-type inhibitors isolated from Bauhinia: interaction with human plasma kallikrein. Biol. Chem. 382, 109-113.
    • (2001) Biol. Chem. , vol.382 , pp. 109-113
    • Oliva, M.L.1    Santomauro-Vaz, E.M.2    Andrade, S.A.3    Juliano, M.A.4    Pott, V.J.5    Sampaio, M.U.6    Sampaio, C.A.M.7
  • 25
    • 0037699905 scopus 로고    scopus 로고
    • Kinetic characterization of factor Xa binding using a quenched fluorescent substrate based on the reactive site of factor Xa inhibitor from Bauhinia ungulata seeds
    • Oliva, M.L., Andrade, S.A., Juliano, M.A., Sallai, R.C., Torquato, R.J., Sampaio, M.U., Pott, V.J., and Sampaio, C.A. (2003). Kinetic characterization of factor Xa binding using a quenched fluorescent substrate based on the reactive site of factor Xa inhibitor from Bauhinia ungulata seeds. Curr. Med. Chem. 10, 1085-1093.
    • (2003) Curr. Med. Chem. , vol.10 , pp. 1085-1093
    • Oliva, M.L.1    Andrade, S.A.2    Juliano, M.A.3    Sallai, R.C.4    Torquato, R.J.5    Sampaio, M.U.6    Pott, V.J.7    Sampaio, C.A.8
  • 27
    • 0034710260 scopus 로고    scopus 로고
    • A novel proteinase inhibitor gene transiently induced by tobacco mosaic virus infection
    • Park, K., Cheong, J., Lee, S., Suh, M., and Choi, D. (2000). A novel proteinase inhibitor gene transiently induced by tobacco mosaic virus infection. Biochim. Biophys. Acta 1492, 509-512.
    • (2000) Biochim. Biophys. Acta , vol.1492 , pp. 509-512
    • Park, K.1    Cheong, J.2    Lee, S.3    Suh, M.4    Choi, D.5
  • 28
    • 0017732763 scopus 로고
    • Specificity of porcine pancreatic elastase, human leukocyte elastase and cathepsin G. Inhibition with peptide chloromethyl ketones
    • Powers, J.C., Gupton, B.F., Harley, A.D., Nishino, N., and Whitley, R.J. (1977). Specificity of porcine pancreatic elastase, human leukocyte elastase and cathepsin G. Inhibition with peptide chloromethyl ketones. Biochim. Biophys. Acta 485,156-166.
    • (1977) Biochim. Biophys. Acta , vol.485 , pp. 156-166
    • Powers, J.C.1    Gupton, B.F.2    Harley, A.D.3    Nishino, N.4    Whitley, R.J.5
  • 29
    • 0025776716 scopus 로고
    • Characterization of proteinase-3 (PR-3), a neutrophil serine proteinase. Structural and functional properties
    • Rao, N.V., Wehner, N.G., Marshall, B.C., Gray, W.R., Gray, B.H., and Hoidal, J.R. (1991). Characterization of proteinase-3 (PR-3), a neutrophil serine proteinase. Structural and functional properties. J. Biol. Chem. 25, 9540-9548.
    • (1991) J. Biol. Chem. , vol.25 , pp. 9540-9548
    • Rao, N.V.1    Wehner, N.G.2    Marshall, B.C.3    Gray, W.R.4    Gray, B.H.5    Hoidal, J.R.6
  • 30
    • 0001144526 scopus 로고
    • Seed storage proteins: The enzyme inhibitors
    • Richardson, M. (1991). Seed storage proteins: the enzyme inhibitors. Methods Plant Biochem. 5, 259-305.
    • (1991) Methods Plant Biochem. , vol.5 , pp. 259-305
    • Richardson, M.1
  • 33
    • 0027988296 scopus 로고
    • Protein secondary structure from circular dichroism spectroscopy. Combining variable selection principle and cluster analysis with neural network, ridge regression and self-consistent methods
    • Sreerama, N. and Woody, R.W. (1993). Protein secondary structure from circular dichroism spectroscopy. Combining variable selection principle and cluster analysis with neural network, ridge regression and self-consistent methods. J. Mol. Biol. 242, 497-507.
    • (1993) J. Mol. Biol. , vol.242 , pp. 497-507
    • Sreerama, N.1    Woody, R.W.2
  • 34
    • 0002770411 scopus 로고
    • Complete amino acid sequence of the α-amylase/subtilisin inhibitor from barley
    • Svendsen, I.B, Hejgaard, J., and Mundy, J. (1986). Complete amino acid sequence of the α-amylase/subtilisin inhibitor from barley. Carlsberg Res. Commun. 51, 43-50.
    • (1986) Carlsberg Res. Commun. , vol.51 , pp. 43-50
    • Svendsen, I.B.1    Hejgaard, J.2    Mundy, J.3
  • 35
    • 0020643467 scopus 로고
    • Human plasma proteinase inhibitors
    • Travis, J. and Salvesen, G.S. (1983). Human plasma proteinase inhibitors. Annu. Rev. Biochem. 52, 655-709.
    • (1983) Annu. Rev. Biochem. , vol.52 , pp. 655-709
    • Travis, J.1    Salvesen, G.S.2
  • 36
    • 0032502952 scopus 로고    scopus 로고
    • Kunitz-type proteinase inhibitors from intact and Phytophthora-infected potato tubers
    • Valueva, T.A., Revina, T.A., Kladnitskaya, G.V., and Mosolov, V.V. (1998). Kunitz-type proteinase inhibitors from intact and Phytophthora-infected potato tubers. FEBS Lett. 426, 131-134.
    • (1998) FEBS Lett. , vol.426 , pp. 131-134
    • Valueva, T.A.1    Revina, T.A.2    Kladnitskaya, G.V.3    Mosolov, V.V.4
  • 37
    • 0032894143 scopus 로고    scopus 로고
    • What do proteins need to reach different vacuoles?
    • Vitale, A. and Raikhel, N.V. (1999). What do proteins need to reach different vacuoles? Trends Plant Sci. 4, 149-155.
    • (1999) Trends Plant Sci. , vol.4 , pp. 149-155
    • Vitale, A.1    Raikhel, N.V.2
  • 38
  • 39
    • 0010673007 scopus 로고
    • Endogenous α-amylase inhibitor in various cereals
    • Weselake, R.J., MacGregor, A.W., and Hill, R.D. (1985). Endogenous α-amylase inhibitor in various cereals. Cereal Chem. 62, 120-123.
    • (1985) Cereal Chem. , vol.62 , pp. 120-123
    • Weselake, R.J.1    MacGregor, A.W.2    Hill, R.D.3
  • 40
    • 0242696058 scopus 로고    scopus 로고
    • Individual tyrosine side-chain contributions to circular dichroism of ribonuclease
    • Woody, A.Y. and Woody, R.W. (2003). Individual tyrosine side-chain contributions to circular dichroism of ribonuclease. Biopolymers 72, 500-513.
    • (2003) Biopolymers , vol.72 , pp. 500-513
    • Woody, A.Y.1    Woody, R.W.2
  • 41
    • 0022002541 scopus 로고
    • The proteolytic activities of chymopapain, papain, and papaya proteinase III
    • Zucker, S., Buttle, D.J., Nicklin, M.J., and Barrett, A.J. (1985). The proteolytic activities of chymopapain, papain, and papaya proteinase III. Biochim. Biophys. Acta 828, 196-204.
    • (1985) Biochim. Biophys. Acta , vol.828 , pp. 196-204
    • Zucker, S.1    Buttle, D.J.2    Nicklin, M.J.3    Barrett, A.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.