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3 results on '"Serine proteinase inhibitor"'

1. Characterization of a novel Kazal-type serine proteinase inhibitor of Arabidopsis thaliana.

Author

Pariani, Sebastián, Contreras, Marisol, Rossi, Franco R., Sander, Valeria, Corigliano, Mariana G., Simón, Francisco, Busi, María V., Gomez-Casati, Diego F., Pieckenstain, Fernando L., Duschak, Vilma G., and Clemente, Marina

Subjects
*SERINE proteinase inhibitors, *ARABIDOPSIS thaliana, *PLANT physiology, *PLANT defenses, *PHYTOPATHOGENIC microorganisms, *TRYPSIN
Abstract

Many different types of serine proteinase inhibitors have been involved in several kinds of plant physiological processes, including defense mechanisms against phytopathogens. Kazal-type serine proteinase inhibitors, which are included in the serine proteinase inhibitor family, are present in several organisms. These proteins play a regulatory role in processes that involve serine proteinases like trypsin, chymotrypsin, thrombin, elastase and/or subtilisin. In the present work, we characterized two putative Kazal-type serine proteinase inhibitors from Arabidopsis thaliana , which have a single putative Kazal-type domain. The expression of these inhibitors is transiently induced in response to leaf infection by Botrytis cinerea , suggesting that they play some role in defense against pathogens. We also evaluated the inhibitory specificity of one of the Kazal-type serine proteinase inhibitors, which resulted to be induced during the local response to B. cinerea infection. The recombinant Kazal-type serine proteinase inhibitor displayed high specificity for elastase and subtilisin, but low specificity for trypsin, suggesting differences in its selectivity. In addition, this inhibitor exhibited a strong antifungal activity inhibiting the germination rate of B. cinerea conidia in vitro . Due to the important role of proteinase inhibitors in plant protection against pathogens and pests, the information about Kazal-type proteinase inhibitors described in the present work could contribute to improving current methods for plant protection against pathogens. [ABSTRACT FROM AUTHOR]

Published
2016
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2. The full-length cDNA of anticoagulant protein infestin revealed a novel releasable Kazal domain, a neutrophil elastase inhibitor lacking anticoagulant activity

Author

Lovato, Diogo Ventura, Nicolau de Campos, Ivan Torres, Amino, Rogerio, and Tanaka, Aparecida Sadae

Subjects
*RECOMBINANT protease inhibitors, *RECOMBINANT proteins, *PANSTRONGYLUS geniculatus, *BLOOD coagulation factors
Abstract

Abstract: Infestins are Kazal-type serine proteinase inhibitors found in the midgut of the Chagas'' disease vector, Triatoma infestans. In previous studies, we characterized two double-headed infestins with potent anticoagulant activity; infestin 1–2, which inhibits thrombin and infestin 3–4, a factor XIIa inhibitor. In the present work, we have cloned the full-length cDNA of infestins'' precursor. The translated cDNA predicted a polypeptide containing a signal peptide and seven Kazal-type domains, four domains from infestin 1–2 and infestin 3–4, and three new domains. Northern blot analysis confirmed that infestins are synthesized in a single transcript (~1800 bp) in the insect midgut, but not in salivary glands. Based on the cDNA sequence, the three new Kazal domains were named infestin 1R, 2R and 3R. Infestin 2R-3R has 77% amino acid sequence identity to infestin 1–2 and the same basic amino acid residue at P1 position in the inhibitory reactive site suggesting that these two proteins have a similar inhibitory specificity. In contrast, infestin 1R has two different characteristics when compared to the other infestins: i) a hydrophobic amino acid residue at P1 position in the inhibitory reactive site and ii) a prediction to be processed as a single Kazal domain. These two characteristics were experimentally demonstrated by the purification of native infestin 1R from T. infestans midgut. Native infestin 1R was shown to be processed as a single Kazal domain by mass spectrometry and it was able to inhibit neutrophil elastase, subtilisin A and chymotrypsin. To further characterize infestin 1R inhibitory activity, it was expressed as a recombinant protein in bacteria. Recombinant infestin 1R inhibited neutrophil elastase with the same K i of the native inhibitor. Moreover, it inhibited subtilisin A, chymotrypsin and proteinase K but did inhibit neither thrombin nor coagulation assays. In conclusion, unlike the other described infestins, infestin 1R did not present anticoagulant activity and is processed as a single Kazal domain with inhibitory specificity towards proteases that hydrolyze peptide bonds after hydrophobic amino acid residues. [Copyright &y& Elsevier]

Published
2006
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3. Characterization of a novel Kazal-type serine proteinase inhibitor of Arabidopsis thaliana

Author

Marisol Contreras, Mariana G. Corigliano, Marina Clemente, Franco Rubén Rossi, Valeria A. Sander, Vilma G. Duschak, Fernando Luis Pieckenstain, Francisco Simon, Maria V. Busi, Diego F. Gomez-Casati, and Sebastián Pariani

Subjects
0106 biological sciences, 0301 basic medicine, Serine Proteinase Inhibitors, Otras Ciencias Biológicas, INHIBITORY ACTIVITY, Arabidopsis, Biology, Genes, Plant, 01 natural sciences, Biochemistry, Ciencias Biológicas, Serine, 03 medical and health sciences, BOTRYTIS CINEREA, Thrombin, Gene Expression Regulation, Plant, Proteinase 3, medicine, Amino Acid Sequence, chemistry.chemical_classification, SERINE PROTEINASE INHIBITOR, Sequence Homology, Amino Acid, KAZAL-TYPE DOMAIN, fungi, Elastase, Subtilisin, ARABIDOPSIS THALIANA, food and beverages, General Medicine, Trypsin, Recombinant Proteins, 030104 developmental biology, Enzyme, chemistry, Botrytis, CIENCIAS NATURALES Y EXACTAS, 010606 plant biology & botany, medicine.drug
Abstract

Many different types of serine proteinase inhibitors have been involved in several kinds of plant physiological processes, including defense mechanisms against phytopathogens. Kazal-type serine proteinase inhibitors, which are included in the serine proteinase inhibitor family, are present in several organisms. These proteins play a regulatory role in processes that involve serine proteinases like trypsin, chymotrypsin, thrombin, elastase and/or subtilisin. In the present work, we characterized two putative Kazal-type serine proteinase inhibitors from Arabidopsis thaliana, which have a single putative Kazal-type domain. The expression of these inhibitors is transiently induced in response to leaf infection by Botrytis cinerea, suggesting that they play some role in defense against pathogens. We also evaluated the inhibitory specificity of one of the Kazal-type serine proteinase inhibitors, which resulted to be induced during the local response to B. cinerea infection. The recombinant Kazal-type serine proteinase inhibitor displayed high specificity for elastase and subtilisin, but low specificity for trypsin, suggesting differences in its selectivity. In addition, this inhibitor exhibited a strong antifungal activity inhibiting the germination rate of B. cinerea conidia in vitro. Due to the important role of proteinase inhibitors in plant protection against pathogens and pests, the information about Kazal-type proteinase inhibitors described in the present work could contribute to improving current methods for plant protection against pathogens. Fil: Pariani Alvarez, Sebastian Adolfo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús). Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús); Argentina Fil: Contreras, Susana Marisol. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús). Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús); Argentina Fil: Rossi, Franco Rubén. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús). Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús); Argentina Fil: Sander, Valeria Analía. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús). Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús); Argentina Fil: Corigliano, Mariana Georgina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús). Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús); Argentina Fil: Simon, Francisco. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús). Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús); Argentina Fil: Busi, María Victoria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosinteticos y Bioquimicos. Universidad Nacional de Rosario. Facultad de Cs.bioquímicas y Farmaceuticas. Centro de Estudios Fotosinteticos y Bioquimicos; Argentina Fil: Gomez Casati, Diego Fabian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosinteticos y Bioquimicos. Universidad Nacional de Rosario. Facultad de Cs.bioquímicas y Farmaceuticas. Centro de Estudios Fotosinteticos y Bioquimicos; Argentina Fil: Pieckenstain, Fernando Luis. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús). Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús); Argentina Fil: Duschak, Vilma Gladys. Dirección Nacional de Instituto de Investigación. Administración Nacional de Laboratorio e Instituto de Salud “Dr. C. G. Malbrán”. Instituto Nacional de Parasitología "Dr. Mario Fatala Chaben”; Argentina Fil: Clemente, Marina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús). Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús); Argentina

Published
2016
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