A proteinase inhibitor from Caesalpinia echinata (pau-brasil) seeds for plasma kallikrein, plasmin and factor XIIa
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Ilana Cruz-Silva
Abstract
Caesalpinia echinata is a tree belonging to the Leguminosae family. The red color of the trunk, looking like burning wood (‘brasa’ in Portuguese), is the origin of the name Brazil. Seeds of leguminous plants contain high amounts of serine proteinase inhibitors that can affect different biological processes. Here we show that a protein isolated from seeds of C. echinata is able to inhibit enzymes that participate in blood coagulation and fibrinolysis. This inhibitor (CeKI) was purified to homogeneity by ion exchange and reversed-phase chromatography. SDS-PAGE indicated a single polypeptide chain with a molecular mass of 20 kDa. CeKI inhibits human plasma kallikrein (Ki=3.1 nM), plasmin (Ki=0.18 nM), factor XIIa (Ki=0.18 nM), trypsin (Ki=21.5 nM) and factor Xa (Ki=0.49 mM). CeKI inhibited kinin release from highmolecular- mass kininogen by kallikrein in vitro. The N-terminal sequence, determined by automatic Edman degradation, identified the inhibitor as a member of the Kunitz family. The secondary structure, determined by circular dichroism, is mainly a random coil followed by β-sheet structure. The action of CeKI on enzymes of the blood-clotting intrinsic pathway was confirmed by prolongation of the activated partial thromboplastin time.
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© Walter de Gruyter
Articles in the same Issue
- Hiroshi Maeda – 40 years of research
- Activation of the kallikrein-kinin system and release of new kinins through alternative cleavage of kininogens by microbial and human cell proteinases
- Molecular mechanism for activation and regulation of matrix metalloproteinases during bacterial infections and respiratory inflammation
- Role of bacterial proteases in pseudomonal and serratial keratitis
- Cysteine cathepsins in human cancer
- Secretory leukoprotease inhibitor and pulmonary surfactant serve as principal defenses against influenza A virus infection in the airway and chemical agents up-regulating their levels may have therapeutic potential
- Design of inhibitors against HIV, HTLV-I, and Plasmodium falciparum aspartic proteases
- Roles of Arg- and Lys-gingipains in coaggregation of Porphyromonas gingivalis: identification of its responsible molecules in translation products of rgpA, kgp, and hagA genes
- Coordinate expression of the Porphyromonas gingivalis lysine-specific gingipain proteinase, Kgp, arginine-specific gingipain proteinase, RgpA, and the heme/hemoglobin receptor, HmuR
- Genetic characterization of staphopain genes in Staphylococcus aureus
- Visualisation of tissue kallikrein, kininogen and kinin receptors in human skin following trauma and in dermal diseases
- Reduction of myocardial infarction by calpain inhibitors A-705239 and A-705253 in isolated perfused rabbit hearts
- A proteinase inhibitor from Caesalpinia echinata (pau-brasil) seeds for plasma kallikrein, plasmin and factor XIIa
- Plasma prekallikrein/kallikrein processing by lysosomal cysteine proteases
- Characteristics of the caspase-like catalytic domain of human paracaspase
- mRNA expression analysis of a variety of apoptosis-related genes, including the novel gene of the BCL2-family, BCL2L12, in HL-60 leukemia cells after treatment with carboplatin and doxorubicin
- Thermoplasma acidophilum TAA43 is an archaeal member of the eukaryotic meiotic branch of AAA ATPases
- Lipopolysaccharide binding of an exchangeable apolipoprotein, apolipophorin III, from Galleria mellonella
Articles in the same Issue
- Hiroshi Maeda – 40 years of research
- Activation of the kallikrein-kinin system and release of new kinins through alternative cleavage of kininogens by microbial and human cell proteinases
- Molecular mechanism for activation and regulation of matrix metalloproteinases during bacterial infections and respiratory inflammation
- Role of bacterial proteases in pseudomonal and serratial keratitis
- Cysteine cathepsins in human cancer
- Secretory leukoprotease inhibitor and pulmonary surfactant serve as principal defenses against influenza A virus infection in the airway and chemical agents up-regulating their levels may have therapeutic potential
- Design of inhibitors against HIV, HTLV-I, and Plasmodium falciparum aspartic proteases
- Roles of Arg- and Lys-gingipains in coaggregation of Porphyromonas gingivalis: identification of its responsible molecules in translation products of rgpA, kgp, and hagA genes
- Coordinate expression of the Porphyromonas gingivalis lysine-specific gingipain proteinase, Kgp, arginine-specific gingipain proteinase, RgpA, and the heme/hemoglobin receptor, HmuR
- Genetic characterization of staphopain genes in Staphylococcus aureus
- Visualisation of tissue kallikrein, kininogen and kinin receptors in human skin following trauma and in dermal diseases
- Reduction of myocardial infarction by calpain inhibitors A-705239 and A-705253 in isolated perfused rabbit hearts
- A proteinase inhibitor from Caesalpinia echinata (pau-brasil) seeds for plasma kallikrein, plasmin and factor XIIa
- Plasma prekallikrein/kallikrein processing by lysosomal cysteine proteases
- Characteristics of the caspase-like catalytic domain of human paracaspase
- mRNA expression analysis of a variety of apoptosis-related genes, including the novel gene of the BCL2-family, BCL2L12, in HL-60 leukemia cells after treatment with carboplatin and doxorubicin
- Thermoplasma acidophilum TAA43 is an archaeal member of the eukaryotic meiotic branch of AAA ATPases
- Lipopolysaccharide binding of an exchangeable apolipoprotein, apolipophorin III, from Galleria mellonella
