Biography:

In the past Michio Matsuda has collaborated on articles with Munekiyo Kaneko and Keiichiro Mori. One of their most recent publications is The plasminogen activator inhibitor-1 binding site in the kringle-2 domain of tissue-type plasminogen activator. Which was published in journal Biochemical and Biophysical Research Communications.

More information about Michio Matsuda research including statistics on their citations can be found on their Copernicus Academic profile page.

Michio Matsuda's Articles: (11)

The plasminogen activator inhibitor-1 binding site in the kringle-2 domain of tissue-type plasminogen activator

AbstractWe have shown that synthetic peptides containing the amino acid sequence Asn-Arg-Arg-Leu, derived from the amino acid sequence of the inner loop of the kringle-2 domain of tissue-type plasminogen activator (tPA), inhibited complex formation between two chain tPA and plasminogen activator inhibitor-1 (PAI-1) by binding to PAI-1. This binding was reversible and was inhibited by not only tPA but also by enzymatically inactive tPA. Quantitative analyses of the interaction of PAI-1 with the peptide containing the Asn-Arg-Arg-Leu sequence indicated that the PAI-1 binding site resides in the inner loop of the kringle-2 domain and is preferentially expressed in two chain tPA.

The plasminogen activator inhibitor-1 binding site in the kringle-2 domain of tissue-type plasminogen activator

AbstractWe have shown that synthetic peptides containing the amino acid sequence Asn-Arg-Arg-Leu, derived from the amino acid sequence of the inner loop of the kringle-2 domain of tissue-type plasminogen activator (tPA), inhibited complex formation between two chain tPA and plasminogen activator inhibitor-1 (PAI-1) by binding to PAI-1. This binding was reversible and was inhibited by not only tPA but also by enzymatically inactive tPA. Quantitative analyses of the interaction of PAI-1 with the peptide containing the Asn-Arg-Arg-Leu sequence indicated that the PAI-1 binding site resides in the inner loop of the kringle-2 domain and is preferentially expressed in two chain tPA.

A simple, large scale method for preparation of plasminogen-free fibrinogen

AbstractA simple method, involving lysine-Sepharose chromatography was developed for large scale preparation of fibrinogen free from detectable plasminogen. After incubation of the preparation with human urokinase under appropriate conditions for over 24 hours at 37°C, no evidence of degradation of the subunits of fibrinogen was detected by polyacrylamide gel electrophoresis in sodium dodecyl sulfate. Moreover, fibrin clots formed by addition of purified bovine thrombin were not lyzed during incubation for more than 72 hours. Large scale preparation of plasminogen-free fibrinogen requires only a smal column and the treatment takes only a short time, so this method seems much better than those used previously, such as Sephadex G-200 gel filtration or precipitation with ethanol-lysine or ethanol-epsilon aminocaproic acid.

Cryofibrinogen in the plasma of patients with skin ulcerative lesions on the legs: A complex of fibrinogen and cold insoluble globulin

AbstractCryofibrinogen was separated from the plasma of four patients with skin ulcers on the legs. It was identified as a complex of fibrinogen and the cold insoluble globulin based on its sedimentation coefficients, electrophoretic mobilities, thrombin-clottability and amino acid compositions. It formed a solid gel with fibrin strands in a short time at 4°C and readily redissolved at 37°C. The fibrinogen in the fraction was not significantly affected by proteolytic enzymes since its subunits were found to be well retained when examined by SDS polyacrylamide gel electrophoresis. The heat-defibrination at 56°C for 3 min resulted in a loss of gel forming capacity, however, the reconsitution with an equivalent amount of purified human fibrinogen apparently recovered it to a certain extent, but not to the initial level. The sedimentation coefficient of the non-fibrinogen fraction fell between 11 S and 13 S and its estimated molecular weight was 4.4 × 105. The amino acid compositions were found to be consistent with those recently reported on the cold insoluble globulin in the normal plasma.

PaperA preparation method of cold-insoluble globulin from rat plasma by means of fibrinmonomer-sepharose affinity chromatography

AbstractCold-insoluble globulin (CIg) was prepared from rat plasma by means of heat-defibrinogenation at 56°C for 4 min, salting-out at 25 % saturation of ammonium sulfate, ion-exchange chromatography on DEAE-cellulose and affinity chromatography using fibrinmonomer-Sepharose. Sodium dodecyl sulfate polyacrylamide gel electrophoresis run on the purified rat CIg showed a major 4.4 × 105 dalton polypeptide and a minor closely migrating doublet with a molecular weight half as large as the major one under unreducing conditions. When the sample was reduced, a doublet with an approximate molecular weight of 2.2 × 105 was noted. Other characteristics and properties described on human and bovine CIg's were found in the purified rat CIg as well, including electrophoretic mobility and immunological cross-reactivity with CIg of other species. The overall recovery and purification in a typical run were 33 % and 68-fold, respectively.

PaperFibrinogen Kawaguchi : An abnormal fibrinogen characterized by defective release of fibrinopeptide A

AbstractA congenital dysfibrinogenemia was found in a 32-year-old asymptomatic female and her immediate family. The propositus, apparently a heterozygote for the abnormality, characteristically showed defective release of fibrinopeptide A from half of her fibrinogen molecules. No fibrinopeptide A was cleaved off from the isolated abnormal molecule by thrombin or snake venoms (Reptilase and Ancrod) as evidenced by radio-immunoassay, high performance liquid chromatography and determination of the NH2-terminal amino acids. The abnormal fibrinogen formed a solid gel solely by the release of fibrinopeptide B upon incubation with thrombin. We provisionally designate this abnormal fibrinogen as “Fibrinogen Kawaguchi”, although possible identity with other abnormal fibrinogens is not excluded.

PaperExpression of prothrombinase activity and CD9 antigen on the surface of small vesicles from stimulated human endothelial cells

AbstractWe employed flow cytometry and monoclonal antibodies (MoAb) to study the surface membrane protein of shed particles (small vesicles, SV) that were released from vascular endothelial cells (EC) by agonists such as a Ca ionophore (A23187) and thrombin. After stimulation of EC by A23187, CD9 antigens disappeared entirely from the EC surface in a time- and concentration-dependent manner; they subsequently moved onto the SV surface. Von Willebrand factor (vWF) and P-selectin from Weibel-Palade (W-P) bodies were expressed rapidly on the EC surface after thrombin stimulation, but not on the SV surface. P-selectin may have some effect on maintenance of hemostasis on the EC surface. We demonstrated that the surfaces of SV and EC significantly supported prothrombinase activity and confirmed that A23187-induced SV from EC express binding sites for factors IXa and Xa. These results suggest that the SV are an important factor in a novel controlling mechanism of the coagulation system on the EC surface.

Regular paperEffect of staphylokinase concentration on plasminogen activation

AbstractActivation of Glu- and Lys-plasminogen by various concentrations of recombinant staphylokinase (SAK) were studied by the generation of amidolytic activity from the chromogenic substrate S-2251 (H-D-Val-Leu-Lys-pNA) and by SDS-PAGE analysis.Surprisingly, excess SAK decreased and fixed the rate of S-2251 hydrolysis in a mixture of Lys-plasminogen and SAK. Since the effect of SAK on S-2251 hydrolysis by plasmin was similar, the hydrolysis kinetics by free plasmin and plasmin-SAK complex were studied. Hydrolysis by either enzyme form followed Michaelis-Menten kinetics with a Km of 0.38 mM for plasmin and 3.74 mM for SAK-plasmin complex. The catalytic rate constant was 22.7 s−1 for plasmin and 21.0 s−1 for the SAK-plasmin complex.With excess SAK and vigorous removal of plasmin activity from plasminogen, the pre-activation lag period differed greatly between Glu- and Lys-plasminogen. Based on the different substrate specificity of plasmin and plasmin-SAK complex, we analyzed the Glu-plasminogen activation with either catalytic or excess SAK. With excess SAK, almost no Lys-plasminogen was detectable and whole Glu-plasminogen was converted directly to Glu-plasmin, then gradually to Lys-plasmin. In contrast, Lys-plasminogen appeared rapidly with catalytic amount of SAK. These results suggest that inhibition of Glu-plasminogen to Lys-plasminogen conversion in the plasminogen-SAK complex in the presence of excess SAK prolonged the initial lag phase of activation.

Regular ArticleSoluble fibrin augments spreading of fibroblasts by providing RGD sequences of fibrinogen in soluble fibrin

AbstractWe previously reported that fibroblasts were found to spread far more avidly on NaBr-solubilized fibrin monomer (FM) monolayers than on immobilized fibrinogen (Fbg), indicating that removal of fibrinopeptides by thrombin is a prerequisite for the fibrin-mediated augmentation of cell spreading [J. Biol. Chem. 272 (1997) 8824–8829]. Soluble fibrin (SF), a 1:2 complex of fibrin-monomer and fibrinogen, is known to be present in the circulating blood under the pathological condition in which blood coagulation is activated. However, its physiological roles are still incompletely known. Fibroblasts spread on immobilized purified soluble fibrin. Cells spreading on immobilized soluble fibrin were blocked by the exogenous addition of soluble fibrin and glycine–arginine–glycine–aspartic acid–serine–phenylalanine (GRGDSP)-synthetic peptide but not by the addition of fibrinogen or fibrin monomer. However, cell spreading activity was decreased in the surfaces coated with fragment X, whose Aα-chains lack carboxyl-terminal segments including arginine–glycine–aspartic acid (RGD)-2 domain, fibrin monomer complexes. It suggests that the RGD-2 domain of fibrinogen after being complexed with fibrin monomer plays a pivotal role for soluble fibrin-dependent cell spreading.Soluble fibrin in plasma derived from the patients of disseminated intravascular coagulation (DIC) was immuno-purified using the monoclonal antibody (mAb) which specifically recognizes the Ca++-dependent conformer of fibrinogen. The purified soluble fibrin consisted of desAA-fibrin monomer and two fibrinogen molecules and did show the cell spreading activity. Thus, soluble fibrin in plasma plays a role as the modulator of thrombogenic process in vivo.

Short communicationDevelopment of a passive direct methanol fuel cell stack for high methanol concentration

AbstractIn order to develop a vertically arranged passive DMFC with a porous carbon plate, PCP, the effect of the head height of the methanol solution in contact with the porous carbon plate on the power generation was investigated for a 55 mm height using a single cell. The single cell was operated at several methanol concentrations greater than 70 wt%. By filling the reservoir with 90 and 100 wt% methanol solutions, power densities greater than 30 mW cm−2 for over 10 h were demonstrated. Based on the result of the single cell study, a passive DMFC stack consisting of 8 unit cells with the PCP was designed and fabricated. The power generation characteristics were then experimentally measured. The maximum power output of 1.8 W, which was almost 10% lower than that expected from the single cell performance, was obtained with 100% methanol. At the same time, a nonuniform cell voltage among the 8 unit cells was found as a reason for the decreasing power output with the increasing current.

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