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Biomedical subjects

M Matsuda

Publications and source records attributed to M Matsuda.

At least 919 records · Page 51Linked to original sources
PubMed1989

[Metastasis of cancer of the renal pelvis and ureter to the adrenal gland].

A 67-year-old man was found to have a metastatic tumor of left adrenal gland originating from the left renal pelvic and ureteral cancer. Histopathological findings of the renal pelvic and ureteral cancer indicated transitional cell carcinoma, which was the diagnosis for the adrenal tumor. Diagnosis of cancer of the renal pelvis and ureter with metastasis to the adrenal gland before operation is very rare. A review of the literature on the metastasis from cancer of renal pelvis and ureter was made.

Adrenal Gland Neoplasms↗
PubMed1989

[Cell kinetic effects of cis-platinum on cancer cells in a culture system and in cases of cervical cancer using monoclonal antibody of BrdU].

Flow cytometric analyses were done in cervical squamous cell carcinoma cell line (SKG-IIIa) and in cancer cells of cervical cancer cases treated with CDDP using monoclonal antibody of BrdU. 1) In fundamental studies using culture system, accumulation of late S phase cells and of mid S phase cells was observed after 48 hours at the dose of 0.2 micrograms/ml and 0.5 micrograms/ml of CDDP, respectively. 2) Accumulation of early S phase cells was observed at the condition of 1 microgram/ml and 3 micrograms/ml of CDDP. All S phase cells decreased gradually thereafter 3) In clinical studies, accumulation of early S phase cells was observed in cancer cells of cervical cancer cases after intra-arterial infusion of CDDP. However, cell cycle recycling was observed in tumor cells which retained their low sensitivity to CDDP after 21-day treatment with intra-arterial infusion of CDDP.

Antibodies, Monoclonal↗
PubMed1989

[Malignant lymphoma of testis: a clinicopathologic study of twenty-six cases].

A clinicopathologic study was made on 26 patients with testicular lymphoma. Because they all presented scrotal swelling as an initial manifestation, they were thought to be affected with primary testicular lymphoma. The age at admission ranged from 39 to 87 years, with a median of 63 years. Stage of disease was I E in 8 patients, II E in 7, and III E in 8. Two- and five-year survival rates were 38% and 26%, respectively. The most common histological type was the diffuse large cell type, especially immunoblastic type. Immunohistochemistry revealed that almost all cases were B cell derived tumors. In our study, an obvious correlation between the histological type and the prognosis for patients could not be observed. However, the initial stage of the disease appeared to affect the outcome in patients with testicular lymphoma.

Adult↗
PubMed1989

[The influence of ferric metabolism on Ga-67 distribution in the human body].

This investigation was undertaken to make clear the influence of ferric metabolism on Ga-67 distribution in human body. Count ratios for each organ to femoral soft tissue (i.e. relative Ga-67 uptake) were calculated in 125 scintigrams obtained 48 hours following injection, and the relation between the relative Ga-67 uptake in each organ and serum Fe, or UIBC were investigated. The relative Ga-67 uptake in the liver and the lumbar vertebra had negative correlation to serum Fe, and had positive correlation to UIBC. However, there was no significant difference in the relative Ga-67 uptake in the lumbar vertebra between normal and high serum Fe group. Only in group with exceedingly low serum Fe, each vertebral body was visualized separately in posterior view of the abdomen. These findings indicated that in group with exceedingly low serum Fe, Ga-67 accumulated mainly in the bone marrow, and in group with high serum Fe, Ga-67 accumulated mainly in the bone. The urinary bladder was visualized only in group with high serum Fe, which suggested that the excretion of Ga-67 to the urine was continued yet at 48 hours after injection. Ferric metabolism affected remarkably on the relative Ga-67 uptake in the liver, the bone marrow and the bone, and also the excretion of Ga-67 to the urine.

Adolescent↗
PubMed1989

Fibrinogen Kyoto III: a congenital dysfibrinogen with a gamma aspartic acid-330 to tyrosine substitution manifesting impaired fibrin monomer polymerization.

A congenital dysfibrinogen characterized by impaired fibrin monomer polymerization was found in an asymptomatic 50-year-old woman and her two sons. On sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) run according to the method of Laemmli, we noticed two gamma chain species in fibrinogen and its plasmic fragments D1 and D2, consisting of a normal species and an apparently lower molecular weight (mol wt) variant in respective fractions. However, in fragment D3 only a single gamma chain remnant was observed. By chromatofocusing of the plasmic-CaCl2 digests of the abnormal fibrinogen, we separately isolated the normal and abnormal D1 species, the latter having been eluted in a slightly higher pH range. As expected, the abnormal D1 species failed to interfere with thrombin clotting of normal fibrinogen and normal fibrin monomer polymerization, whereas the normal D1 species inhibited them markedly. By analyzing the lysyl endopeptidase digests of the isolated gamma chain, we identified a replacement of aspartic acid by tyrosine at position 330 of the mutant gamma chain. The point mutation from an aspartic acid (pK for the beta-carboxyl = 3.86) to a tyrosine (pK for the aromatic hydroxyl = 10.07) may have perturbed the folding gamma chain structure in the D domain of fibrinogen specifically required for polymerization.

Amino Acid Sequence↗
PubMed1988

Normal plasmic cleavage of the gamma-chain variant of "fibrinogen Saga" with an Arg-275 to His substitution.

We have identified a gamma-Arg-275 to His substitution in an abnormal fibrinogen designated as "fibrinogen Saga" characterized by impaired fibrin monomer polymerization. By chromatofocusing chromatography, we isolated normal and abnormal fragment D1 populations separately from the plasmic-calcium digests of fibrinogen derived from the propositus, a heterozygote for the abnormality. We found that both normal and abnormal fragment D1's were similarly protected from digestion by plasmin in the presence of calcium ions and further degraded to fragments D2 and D3 due to cleavage of the gamma-chain remnant when calcium ions were replaced by chelating agents. Abnormal fragment D1 failed to inhibit both thrombin-clotting of normal fibrinogen and polymerization of normal fibrin monomer, while normal D1 exhibited marked inhibitory activities. In an aberrant peptide comprising residues gamma-274-302 isolated by HPLC from the lysyl endopeptidase-digests of abnormal fragment D1, we identified a His substituting for an Arg at position 2, which corresponds to position 275 of the mutant gamma-chain.

Adolescent↗
PubMed1988

Enterotoxin of Clostridium perfringens type A forms ion-permeable channels in a lipid bilayer membrane.

The enterotoxin of Clostridium perfringens type A was found to form ion-permeable channels in a lipid bilayer. A patch clamp technique was used to detect channel activities in an asolectin bilayer with incorporated enterotoxin. About 20% of the lipid bilayer patches examined showed rectangular or stepwise shift of membrane current. The shifts indicated the gating of ion-permeable channels in the patches. The channels showed high conductance (40-450 pS), no rectification in current-voltage curves and occasional long-lasting events. The significance of these findings is discussed in relation to the mechanism of action of the toxin.

Clostridium perfringens↗
PubMed1988

Substitution of gamma Arg-275 by Cys in an abnormal fibrinogen, "fibrinogen Osaka II". Evidence for a unique solitary cystine structure at the mutation site.

In an abnormal fibrinogen with impaired fibrin monomer polymerization designed as fibrinogen Osaka II, we have identified substitution of Arg by Cys at position 275 of the gamma chain. This Cys is linked to a free cysteine molecule by a disulfide link as evidenced by fast atom bombardment mass spectrometry. This finding was supported by identification of a single cysteine released from isolated abnormal fragment D1 upon reduction. This unique cystine structure at the mutation site has not been reported heretofore in any abnormal protein including fibrinogen. The substitution may well perturb the structure required for fibrin monomer polymerization, specifically that assigned to the carboxyl-terminal D domain of fibrinogen. Indeed, isolated fragment D1 with the Cys substitution failed to inhibit thrombin-mediated clotting of normal fibrinogen and normal fibrin monomer polymerization, while normal fragment D1 inhibited them markedly. Our data seem to provide supporting evidence that the putative polymerization site(s) assigned to the D domain of fibrinogen may be structure-dependent, including the carboxyl-terminal segment of the gamma chain as well as a contiguous region that contains the gamma 275 residue.

Adolescent↗
PubMed1988

Characterization of an apparently lower molecular weight gamma-chain variant in fibrinogen Kyoto I. The replacement of gamma-asparagine 308 by lysine which causes accelerated cleavage of fragment D1 by plasmin and the generation of a new plasmin cleavage site.

Congenitally abnormal fibrinogen Kyoto I with impaired fibrin monomer polymerization contains a normal gamma-chain and a gamma-chain variant (gamma Kyoto I) that has an apparently lower Mr on sodium dodecyl sulfate-polyacrylamide gel electrophoresis in the Laemmli system (Laemmli, U. K. (1970) Nature 227, 680-685) but migrates with apparently normal Mr in the Weber and Osborn system (Weber, K., and Osborn, M. (1969) J. Biol. Chem. 244, 4406-4412). Reverse-phase high performance liquid chromatographic analyses of the cyanogen bromide or lysyl endopeptidase cleavage fragments of the purified gamma-chains of fibrinogen Kyoto I showed the presence of peptides not seen from normal fibrinogen. Amino acid sequence analysis of these peptides indicated that gamma Asn308 of the gamma-chain variant is replaced by lysine. Purified fragment D1 of fibrinogen Kyoto I also contains two types of D1 gamma-remnants: normal and apparently lower Mr types. Abnormal fragment D1 is cleaved faster to fragments D2 and D3 by plasmin in the presence of [ethylenebis(oxyethylenenitrilo)]tetraacetic acid (EGTA) than normal fragment D1, as analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, followed by immunoblotting using anti-gamma-chain monoclonal antibody. Analysis of peptides released from fragment D1 by plasmin in the presence of EGTA demonstrated the cleavage of the gamma Lys308-Gly309 bond. Fragment D1 of fibrinogen Kyoto I has normal calcium binding properties. The data suggest that a region or conformation containing gamma Asn308 affects the polymerization of fibrin monomers and that the gamma Asn308----Lys replacement causes a conformational change in the gamma-chain which results in the accelerated cleavage of gamma Lys356-Ala357 and gamma Lys302-Phe303 bonds by plasmin and also results in the generation of a new plasmin cleavage site between Lys308 and Gly309 in the presence of EGTA. During these studies, we found that part of the gamma Lys212-Glu213 bond in fragment D1 is cleaved by plasmin in the presence of EGTA.

Amino Acid Sequence↗
PubMed1988

Occurrence of three distinct molecular species of chondroitin sulfate proteoglycan in the developing rat brain.

More than 60% of brain chondroitin sulfate proteoglycans were extracted from 10-day-old rat brains by homogenization in ice-cold phosphate-buffered saline containing protease inhibitors. Although the soluble proteoglycan preparation was a mixture of chondroitin sulfate proteoglycans with a different hydrodynamic size as well as a different molecular density, each subfraction of the proteoglycans contained chondroitin sulfate side chains with virtually identical molecular weight (approximately 15,000) and chondroitin sulfate disaccharide composition (high content of 4-sulfate unit). Digestion of the purified proteoglycan preparation with protease-free chondroitinase ABC produced five core proteins with Mr = 250,000 (designated as 250K protein), 220,000 (220K), 150,000 (150K), 130,000 (130K), and 93,000 (93K). All these core proteins were obtained from chondroitin sulfate proteoglycan preparations extracted from various regions of the brain, but their composition varied among different brain regions. Analysis for amino acid composition of these core proteins and two-dimensional mapping of their proteolytic peptides revealed that three major core proteins (250K, 220K, and 150K proteins) were structurally different. These observations indicate that at least three distinct types of chondroitin sulfate proteoglycan occur in the developing rat brain.

Amino Acids↗
PubMed1988

Combined factor VII and protein C deficiency found in a patient with peripheral pulmonary artery stenosis accompanied by progressive pulmonary hypertension and hemoptysis.

A congenital deficiency of factor VII and protein C was found in a 21-year-old female suffering from recurrent and progressive attacks of dyspnea and hemoptysis over the last four years. She has been followed in our Department since the age of 17 under a diagnosis of peripheral pulmonary artery stenosis and pulmonary hypertension as confirmed by cardiac catheterization and angiography. Prolonged prothrombin time repeatedly examined during this time period prompted us to perform detailed coagulation studies. We found that factor VII and protein C were both half normal in activity as well as in antigen. Three other members of her immediate family were also found to be affected with this combined deficiency. Since the genes encoding factor VII and protein C are located in different chromosomes, the 13th and the second chromosomes, respectively, expression of the combined hereditary deficiency is a random and very rare association on the basis of frequencies of 1:50,000 for factor VII and 1:16,000 for protein C deficiencies.

Adult↗