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Biomedical subjects

S Nishibe

Publications and source records attributed to S Nishibe.

At least 55 records · Page 3Linked to original sources
PubMed1986

Specific binding of human pancreatic secretory trypsin inhibitor to various cultured cells.

Pancreatic secretory trypsin inhibitor from human pancreatic juice bound specifically to cultured cells derived from a variety of human and nonhuman tissues. The binding pattern of pancreatic secretory trypsin inhibitor to various cells was quite different from that of epidermal growth factor, and these two polypeptides did not compete in binding to cultured cells with one another, indicating that the binding site for pancreatic secretory trypsin inhibitor was distinct from the receptor for epidermal growth factor.

Animals↗
PubMed1985

Studies on the specificity of the cholesterol-binding pancreatic proteinase and identification as human pancreatic elastase 1.

The proteolytic attack of the cholesterol-binding pancreatic proteinase (CBPP) on the oxidized insulin A and B chains as well as on glucagon was investigated by kinetic studies. The reaction products were isolated by high-pressure liquid chromatography and identified by amino acid analysis. The combined results reveal a pronounced selectivity of CBPP for the peptide bonds at the carboxy ends of Ala, Val, Leu, Ser, His and Thr residues with Ala, Val and Leu most favoured, indicating a close catalytic relationship to porcine pancreatic elastase [Narayanan, A. S. & Anwar, R. A. (1969) Biochem. J. 114, 11-17] and the anionic porcine pancreatic protease E [Kobayashi R., Kobayashi, Y. & Hirs, C. H. W. (1981) J. Biol. Chem. 256, 2460-2465] which resembles human pancreatic elastase 1. The immunological comparison indeed disclosed the identity of CBPP with human pancreatic elastase 1.

Animals↗
PubMed1985

Effects of protease inhibitors and calmodulin inhibitors on Ca2+ influx and catecholamine secretion in isolated bovine adrenal medullary cells.

Acetylcholine (ACh) (10(-4) M) induced Ca2+ influx (21.2 nmol/mg cell protein/3 min) and catecholamine (CA) secretion (11.5% of total CA content) in isolated bovine adrenal medullary cells. Both excess K+ (56 mM KCl) and a calcium ionophore (A-23187: 10(-5) M) also induced CA secretion (9.7 and 7.5%, respectively, of total CA content). Protease inhibitors [gabexate mesilate (FOY), TLCK], a synthetic substrate of protease (TAME) and calmodulin inhibitors (W-7, trifluoperazine, promethazine, chlorpromazine) inhibited Ca2+ influx and CA secretion induced by ACh. Protease inhibitors and a substrate of protease had no effect on CA secretion induced by excess K+, and a high concentration of calmodulin inhibitors was required to inhibit excess K+-induced CA secretion. CA secretion induced by A-23187 was not inhibited by these inhibitors and the substrate.

Adrenal Medulla↗
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↗
PubMed1983

Inhibition of catecholamine release from isolated bovine adrenal medullary cells by various inhibitors: possible involvement of protease, calmodulin and arachidonic acid.

Acetylcholine and arachidonic acid induced catecholamine secretion from isolated bovine adrenal medullary cells. Protease inhibitors and calmodulin inhibitors inhibited catecholamine secretion induced by acetylcholine but did not inhibit the secretion induced by arachidonic acid. BW 755-C, a lipoxygenase inhibitor, inhibited catecholamine release induced by acetylcholine. These results suggest that a protease and calmodulin are involved in the successive reaction after stimulus-receptor coupling and arachidonic acid or its metabolites might be important in catecholamine secretion from bovine adrenal medullary cells.

Acetylcholine↗
PubMed1983

Data processing for radioimmunoassay standard curve using microcomputer: a new BASIC program for weighted logit-log transformation.

A new BASIC program of the weighted linear, quadratic and cubic logit-log regression methods for data processing of radioimmunoassay standard curve was developed using a microcomputer. Using this program, three regression analyses are calculated and the table for root mean square of residuals in each regression are shown for the selection of the regression method. The data of three radioimmunoassays of human pancreatic enzymes and pancreatic secretory trypsin inhibitor were examined by this program and compared with those processed by the four parameter logistic method. The weighted cubic logit-log regression showed better fit in radioimmunoassays of human pancreatic enzymes with larger molecular weights. The present program is useful and practicable for its simplicity and accuracy.

Computers↗
PubMed1976

Biochemical studies of pigments from a pathogenic fungus Microsporum cookei. III. Comparison of the effects of xanthomegnin and O-methylxanthomegnin on the oxidative phosphorylation of rat liver mitochondria.

The effects of xanthomegnin and O-methylxanthomegnin on the oxidative phosphorylation of rat liver mitochondria were compared. The n-octanol/water partition coefficient of xanthomegnin was markedly enhanced by O-methylation, but O-methylation of xanthomegnin reduced the uncoupling effect on the respiratory system of mitochondria. Analogous results were obtained in the uncoupling action of 5-hydroxy-1, 4-naphthoquinone (juglone) and 5-methoxy-1, 4-naphthoquinone (O-methyljuglone) on the oxidative phosphorylation of rat liver mitochondria. These data indicate that the phenolic hydroxyl groups of xanthomegnin might contribute to its uncoupling action on the oxidative phosphorylation of mitochondria. Bovine serum albumin (BSA) improved the efficiency of oxidative phosphorylation of mitochondria which were uncoupled by xanthomegnin. Spectroscopic observations revealed that xanthomegnin interacted with BSA by means of hydrophobic and ionic forces but O-methylxanthomegnin showed only hydrophobic interaction. Analogous interactions between mitochondria and xanthomegnin or O-methylxanthomegnin were observed. These results indicate that the uncoupling action of xanthomegnin on the respiratory system in mitochondria might involve ionic interaction of xanthomegnin with cationic residues in the hydrophobic region of mitochondrial membrane proteins.

Animals↗