The Experts below are selected from a list of 42 Experts worldwide ranked by ideXlab platform
Hidechika Okada - One of the best experts on this subject based on the ideXlab platform.
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CPR-Total (TAFI and Activated TAFI) Levels in Plasma/Serum of Hemophiliacs
Microbiology and Immunology, 2020Co-Authors: Noriko Okada, Hidechika OkadaAbstract:Arginine Carboxypeptidase (CPR) is a single-chain plasma protein generated during coagulation from a precursor (proCPR). proCPR is the same molecule as thrombin activable fibrinolysis inhibitor (TAFI), which retards fibrin clot lysis in vitro and most likely modulates fibrinolysis in vivo. In this study, the amount of CPR-total, which includes proCPR (TAFI) and CPR (activated TAFI), in hemophiliac patients was evaluated using a newly developed enzyme linked immunosorbent assay (ELISA). The amount of CPR-total in plasma or serum of most of the hemophiliac patients was in the range of healthy individuals. There was no significant difference in hemophiliac patients with or without HIV-1 infection. However, two out of the 74 hemophiliac patients showed a significantly high level. The upregulation of CPR-total might contribute to compensate for inefficient coagulation in some hemophiliac individuals.
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Arginine Carboxypeptidase cpr in human plasma determined with sandwich elisa
Microbiology and Immunology, 1999Co-Authors: Akihiro Morioka, William Campbell, Yoko Kaneko, Noriko Okada, Kyoko Obata, Tomoyuki Nomura, Hidechika OkadaAbstract:There are two types of Carboxypeptidases present in human blood, Carboxypeptidase N (CPN) and Arginine Carboxypeptidase (CPR). CPR is generated during coagulation from a precursor (proCPR) which can be converted to the active form by trypsin in vitro. Since it is difficult to distinguish the two types of Carboxypeptidases in human blood by the measurement of enzyme activity, we established a quantitative sandwich ELISA by which CPR can be quantitated. The amount of CPR in plasma, fresh serum and heated serum were essentially the same. Therefore the ELISA assay does not distinguish proCPR, activated CPR and inactivated CPR. With the ELISA method, CPR was quantitated in plasma from fifty patients with rheumatoid arthritis and eleven patients with severe hepatitis as well as healthy individuals. The amount of CPR in plasma obtained from patients with rheumatoid arthritis was not found to be lower than that of normal subjects. Furthermore, the patients who suffered severe hepatitis and had very low levels of CPR-total were fatal. This suggests that a decrease of CPR level might be a good indication of a patient's prognosis to death by hepatitis.
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measurement of Arginine Carboxypeptidase generating activity of adult plasma
Microbiology and Immunology, 1998Co-Authors: Motoi Watanabe, William Campbell, Yasushige Ishikawa, Hidechika OkadaAbstract:Arginine Carboxypeptidase (CPR) is a novel Carboxypeptidase which was first described by Campbell and Okada. CPR is generated from a stable precursor of CPR (proCPR) during coagulation or under other circumstances and is promptly inactivated at 37 C. Therefore, it is not easy to determine CPR in blood samples. Since proCPR can be separated from the other basic Carboxypeptidase (Carboxypeptidase N; CPN) by passing plasma through DEAE gel, we have established a method to determine the amount of proCPR after converting it to active CPR by trypsin treatment. We first separated the proCPR from CPN using a filter cup tube (FC tube) packed with DEAE Sephadex, and measured activity after conversion of the enzyme to its active form using trypsin. With this method, no significant decrease in proCPR was noted in the plasma of patients including those with rheumatoid arthritis (RA), although CPR activity in fresh sera has been reported to be decreased. This discrepancy suggests that proCPR is not depleted in most patient sera, but that the level of activity of the enzyme which converts proCPR into active CPR may be compromised in RA patients.
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Pro-Carboxypeptidase R cleaves bradykinin following activation.
International Archives of Allergy and Immunology, 1994Co-Authors: Tsurayuki Shinohara, William Campbell, Noriko Okada, Chikai Sakurada, Takashi Suzuki, Oki Takeuchi, Seiyo Ikeda, Hidechika OkadaAbstract:Arginine Carboxypeptidase (CPR) is a labile enzyme present in human serum which is unrelated to Carboxypeptidase N. In this study we demonstrate that CPR exists in a precursor form in plasma and can b
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changes in Arginine Carboxypeptidase cpr activity in stressed rats
Pathophysiology, 1994Co-Authors: Katsumi Kato, Nagao Shinagawa, Tetsusi Hayakawa, Hiromitsu Takeyama, William Campbell, Hidechika OkadaAbstract:Abstract An Arginine Carboxypeptidase (CPR) is generated from its precursor (ProCPR) by proteolytic enzyme and may function in vivo in the removal of C-terminal Arginine from inflammatory peptides such as C3a and C5a. We studied changes in this enzyme activity in rats submitted to liver cirrhois, hepatectomy, splenectomy, burning or endotoxin challenge. It is suggested that this enzyme could be activated with simultaneous generation of active peptides such as C3a and C5a at inflammatory sites to prevent their excess activity and inactivated due to its instability.
M. Van Sande - One of the best experts on this subject based on the ideXlab platform.
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purification and characterization of a new Arginine Carboxypeptidase in human serum
Biochimica et Biophysica Acta, 1990Co-Authors: Dirk Hendriks, S. Scharpe, Marie-paule Lommaert, W Wang, M. Van SandeAbstract:Abstract A Carboxypeptidase capable of cleaving basic amino acids from synthetic peptide substrates in present in fresh human serum, and not in human heparinized plasma. Its activity is generated during the process of coagulation. Because of its unstability at room temperature and at 37°C, we named it unstable Carboxypeptidase (Carboxypeptidase U). Carboxypeptidase U was partially purified from fresh human serum by chromatography on DEAE-cellulose and Mono-Q sepharose and was found to be a 435 kDa protein. We compared this enzyme with Carboxypeptidase N, purified from human serum by a two-step affinity chromatography on Arginine-Sepharose 4B, followed by ion-exchange chromatography on Mono-Q sepharose. Carboxypeptidase U cleaves hippuryl- l -Arginine and hippuryl- l -lysine, but at a different relative rate than Carboxypeptidase N, and has no esterase activity on hippuryl- l -argininic acid. Its activity was inhibited by o-phenanthroline, dl -2-mercaptomethyl-3-guanidinoethylthiopropanoic acid, CoCl2, 2-mercaptoethanol, dithiothreitol and 4-chloromercuribenzoic acid. These characteristics differentiate Carboxypeptidase U from Carboxypeptidase N and other known Carboxypeptidase.
Dirk Hendriks - One of the best experts on this subject based on the ideXlab platform.
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purification and characterization of a new Arginine Carboxypeptidase in human serum
Biochimica et Biophysica Acta, 1990Co-Authors: Dirk Hendriks, S. Scharpe, Marie-paule Lommaert, W Wang, M. Van SandeAbstract:Abstract A Carboxypeptidase capable of cleaving basic amino acids from synthetic peptide substrates in present in fresh human serum, and not in human heparinized plasma. Its activity is generated during the process of coagulation. Because of its unstability at room temperature and at 37°C, we named it unstable Carboxypeptidase (Carboxypeptidase U). Carboxypeptidase U was partially purified from fresh human serum by chromatography on DEAE-cellulose and Mono-Q sepharose and was found to be a 435 kDa protein. We compared this enzyme with Carboxypeptidase N, purified from human serum by a two-step affinity chromatography on Arginine-Sepharose 4B, followed by ion-exchange chromatography on Mono-Q sepharose. Carboxypeptidase U cleaves hippuryl- l -Arginine and hippuryl- l -lysine, but at a different relative rate than Carboxypeptidase N, and has no esterase activity on hippuryl- l -argininic acid. Its activity was inhibited by o-phenanthroline, dl -2-mercaptomethyl-3-guanidinoethylthiopropanoic acid, CoCl2, 2-mercaptoethanol, dithiothreitol and 4-chloromercuribenzoic acid. These characteristics differentiate Carboxypeptidase U from Carboxypeptidase N and other known Carboxypeptidase.
W Wang - One of the best experts on this subject based on the ideXlab platform.
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purification and characterization of a new Arginine Carboxypeptidase in human serum
Biochimica et Biophysica Acta, 1990Co-Authors: Dirk Hendriks, S. Scharpe, Marie-paule Lommaert, W Wang, M. Van SandeAbstract:Abstract A Carboxypeptidase capable of cleaving basic amino acids from synthetic peptide substrates in present in fresh human serum, and not in human heparinized plasma. Its activity is generated during the process of coagulation. Because of its unstability at room temperature and at 37°C, we named it unstable Carboxypeptidase (Carboxypeptidase U). Carboxypeptidase U was partially purified from fresh human serum by chromatography on DEAE-cellulose and Mono-Q sepharose and was found to be a 435 kDa protein. We compared this enzyme with Carboxypeptidase N, purified from human serum by a two-step affinity chromatography on Arginine-Sepharose 4B, followed by ion-exchange chromatography on Mono-Q sepharose. Carboxypeptidase U cleaves hippuryl- l -Arginine and hippuryl- l -lysine, but at a different relative rate than Carboxypeptidase N, and has no esterase activity on hippuryl- l -argininic acid. Its activity was inhibited by o-phenanthroline, dl -2-mercaptomethyl-3-guanidinoethylthiopropanoic acid, CoCl2, 2-mercaptoethanol, dithiothreitol and 4-chloromercuribenzoic acid. These characteristics differentiate Carboxypeptidase U from Carboxypeptidase N and other known Carboxypeptidase.
Marie-paule Lommaert - One of the best experts on this subject based on the ideXlab platform.
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purification and characterization of a new Arginine Carboxypeptidase in human serum
Biochimica et Biophysica Acta, 1990Co-Authors: Dirk Hendriks, S. Scharpe, Marie-paule Lommaert, W Wang, M. Van SandeAbstract:Abstract A Carboxypeptidase capable of cleaving basic amino acids from synthetic peptide substrates in present in fresh human serum, and not in human heparinized plasma. Its activity is generated during the process of coagulation. Because of its unstability at room temperature and at 37°C, we named it unstable Carboxypeptidase (Carboxypeptidase U). Carboxypeptidase U was partially purified from fresh human serum by chromatography on DEAE-cellulose and Mono-Q sepharose and was found to be a 435 kDa protein. We compared this enzyme with Carboxypeptidase N, purified from human serum by a two-step affinity chromatography on Arginine-Sepharose 4B, followed by ion-exchange chromatography on Mono-Q sepharose. Carboxypeptidase U cleaves hippuryl- l -Arginine and hippuryl- l -lysine, but at a different relative rate than Carboxypeptidase N, and has no esterase activity on hippuryl- l -argininic acid. Its activity was inhibited by o-phenanthroline, dl -2-mercaptomethyl-3-guanidinoethylthiopropanoic acid, CoCl2, 2-mercaptoethanol, dithiothreitol and 4-chloromercuribenzoic acid. These characteristics differentiate Carboxypeptidase U from Carboxypeptidase N and other known Carboxypeptidase.
