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Biomedical subjects

K Matsuda

Publications and source records attributed to K Matsuda.

At least 685 records · Page 38Linked to original sources
PubMed1985

Postoperative elevation of serum pancreatic secretory trypsin inhibitor.

Postoperative transient elevations of serum pancreatic secretory trypsin inhibitor are reported for the first time. The elevations were independent of the surgical procedures or sites, and the maximum serum pancreatic secretory trypsin inhibitor was seen on the 2nd to 4th postoperative day. The elevation of pancreatic secretory trypsin inhibitor was significantly correlated with the length of the operation time and the volume of blood loss during the operation. The change of serum pancreatic secretory trypsin inhibitor was also significantly correlated with those of white blood cell count, alpha 1-antitrypsin, and fibrinogen.

Adult↗
PubMed1985

Elevation of serum pancreatic secretory trypsin inhibitor (PSTI) in patients with serious injury.

Pancreatic secretory trypsin inhibitor (PSTI) in serum was measured periodically in 15 patients with serious abdominal and non-abdominal injuries. From the second or third posttraumatic day, serum PSTI began to rise. Elevation of serum PSTI to more than twice the initial value was seen in 93% of the patients following serious injury. In uneventful cases, it declined and returned to the level at the time of admission within 14 days, but in the patients with serious inflammations and in the patient who died, it remained elevated. The change in the concentration of serum PSTI was significantly correlated with those of the acute phase reactants (fibrinogen and alpha 1-antitrypsin). There was no correlation between the level of serum PSTI and serum amylase activity or creatinine.

Abdominal Injuries↗
PubMed1985

[Changes in serum pancreatic enzymes and pancreatic secretory trypsin inhibitor in patients with severe acute pancreatitis].

Serum pancreatic enzymes (amylase, trypsin, pancreatic elastase 1, pancreatic phospholipase A2) and serum pancreatic secretory trypsin inhibitor (PSTI) were measured in 22 patients with moderate or severe acute pancreatitis. Serum levels of all pancreatic enzymes were elevated at the initial determination, but they fell rapidly to normal in both moderate and severe pancreatitis. In contrast, PSTI in severe pancreatitis increased after admission and reached the maximum on the second to the forth day after onset. There was a significant positive correlation between the level of PSTI and that of acute phase reactant (fibrinogen, alpha 1-antitrypsin), and serum PSTI in severe acute pancreatitis changed as if it was one of acute phase reactants. There was also a significant negative correlation between the level of serum PSTI and that of alpha 2-macroglobulin.

Acute Disease↗
PubMed1985

Timing of the initiation of rRNA gene expression and nucleolar formation in cleavage embryos arrested by cytochalasin B and podophyllotoxin and in cytoplasm-extracted embryos of Xenopus laevis.

The timing mechanism of rRNA gene expression was studied in Xenopus laevis embryos whose cleavage was arrested by treatment with cytochalasin B or podophyllotoxin, and in fertilized eggs from which about 40% of the cytoplasm was extracted by micromanipulation. rRNA synthesis was activated in the cleavage-arrested embryos and also in cytoplasm-extracted embryos at the time when the control embryos commenced synthesizing rRNA at the late blastula stage. Formation of the nucleolar structure occurred at the normal time in the nuclei of cleavage embryos arrested by podophyllotoxin. Therefore, neither twelve continuous cell divisions nor the nuclear division which normally precedes the MBT (mid-blastula transition) was the factor determining the timing of rDNA expression. Moreover, lowering of the cytoplasmic:nuclear ratio to a certain threshold level was not a prerequisite for rDNA activation. Some regulatory mechanism dependent on the time elapsed from fertilization is likely to be the important factor permitting rDNA expression.

Animals↗
PubMed1985

[Pathology of the anomalous choledocho-pancreatic junction--action of pancreatic juice on the biliary tract].

The mechanism of action of pancreatic juice on the biliary tract was investigated in a 5-year-old girl with choledochal cyst and animal models of the anomalous choledocho-pancreatic junction produced by pancreatico-cholecystostomy in 26 dogs. The results are as follows: Pancreatic enzymes are activated when bile and pancreatic juice are mixed in the biliary tract. Successively, lysolecithin and free fatty acids are produced by hydrolysis of lecithin in bile with phospholipase A2. These substances including phospholipase A2 destroy the mucosal barrier. The initial site receiving mucosal damage appears to be the epithelial apical cell membrane. The transfer of phospholipase A2 but not amylase from the biliary tract to the blood stream was suggested by comparing enzyme activity of portal and hepatic venous blood. The presence of some mutagenic substances in the contents of the choledochal cyst was confirmed by Ames assay and Rec-assay. This suggests that activated pancreatic enzymes and successively produced harmful substances in the anomalous choledocho-pancreatic junction are responsible for not only inflammatory but positively carcinogenic action on the biliary tract. In conclusion, the anomalous choledocho-pancreatic junction requires operative separation of the bile duct from the pancreatic duct despite the presence or absence of a choledochal cyst.

Animals↗
PubMed1984

Enzyme immunoassay of human cytosolic aspartate aminotransferase.

A sensitive and specific sandwich enzyme immunoassay (EIA) for human cytosolic aspartate aminotransferase (c-AST) has been developed. Serum was incubated with anti-c-AST antibody-coated polystyrene beads, and further incubated with anti-c-AST antibody-peroxidase conjugate. The peroxidase activity bound to the polystyrene bead was proportional to the amount of c-AST. The method allows measurement of serum c-AST ranging from 50-2,000 micrograms/l. No cross-reactivity with m-AST or other serum components was observed. Recovery, within-day precision, and day-to-day precision were good. The levels of c-AST obtained by the proposed EIA were compared with those based on enzyme activity. The results suggest that there is a considerable excess of immunologically active but catalytically inactive c-AST in normal and patient's sera, and that variable specific activities of c-AST are may be found in sera from different individuals.

Antibody Specificity↗
PubMed1984

Inhibition of prostaglandin synthesis by sodium 2-[4-(2-oxocyclopentylmethyl)phenyl] propionate dihydrate (CS-600), a new anti-inflammatory drug, and its active metabolite in vitro and in vivo.

A new anti-inflammatory agent, sodium 2-[4-(2-oxocyclopentylmethyl)phenyl]propionate dihydrate (CS-600), was investigated for its inhibition of prostaglandin (PG) synthesis in vivo and in vitro. CS-600 caused a marked decrease in the level of urinary PGE2 and PGF2 alpha in rats. The dose of CS-600 which resulted in a 50% decrease of urinary PGE2 excretion was 1.9 mg/kg, p.o., and this value agreed well with the ID50 of the drug for carrageenin edema (1.2 mg/kg, p.o.). This suggests that CS-600 inhibits prostaglandin synthesis in vivo. However, CS-600 had only weak inhibitory activity against in vitro prostaglandin synthesis by bovine seminal vesicle microsomes (IC50:760 microM). A main plasma metabolite of CS-600, which was produced by stereospecific reduction of the cyclopentanone moiety to transhydroxy cyclopentane, exhibited potent inhibitory activity toward the prostaglandin synthetase of bovine seminal vesicle microsomes (IC50:11 microM). In cell cultures of 3T6 fibroblasts from mice, CS-600 inhibited production of PGE2 and PGF2 alpha by the cells at low concentrations (IC50 for PGE2:1.6 microM). The active metabolite exhibited more potent inhibition (IC50:0.29 microM), and conversion of CS-600 into the active metabolite occurred in the cell system. Inhibition of prostaglandin synthetase in the membrane fraction of the fibroblast cells was also investigated. Available evidence indicates that CS-600 is a pro-drug and exerts its pharmacological activities after conversion to the active metabolite.

Animals↗