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T Fushiki

Publications and source records attributed to T Fushiki.

99 records · Page 6Linked to original sources
PubMed1984

Stimulatory effect of an endogenous peptide in rat pancreatic juice on pancreatic enzyme secretion in the presence of atropine: evidence for different mode of action of stimulation from exogenous trypsin inhibitors.

A new factor which activated the secretion of pancreatic enzymes was discovered and purified from rat bile-pancreatic juice. A fraction below M.W.10,000 of rat bile-pancreatic juice enhanced trypsinogen secretion by injection into anesthetized rat duodenum. The factor was purified from this fraction using its biological activity as an index by Sephadex G-50, SP Sephadex C-50 and HPLC. This factor was a peptide of which molecular weight was about 6,000 and had trypsin inhibitory activity. From these and some other findings, it was suggested that the peptide was identical with the "Kazal type" inhibitor. In the anesthetized and atropine-treated rat, of which intestinal trypsin was removed by thoroughly washing with saline containing 5 microM soybean trypsin inhibitor (SBTI), pancreatic secretion became basal state, and was not stimulated by injection of SBTI into its duodenum any longer. Under this condition, however, injection of this purified peptide brought about markedly stimulation of pancreatic enzyme secretion. These results suggest that this peptide has a certain function which enhances pancreatic enzyme secretion by the different manner from exogenous trypsin inhibitors such as SBTI.

Animals↗
PubMed1983

Influence of folate-binding protein from bovine milk on the absorption of folate in gastrointestinal tract of rat.

The absorption of [14C]pteroylglutamic acid (PteGlu) bound to the folate-binding protein of bovine milk was investigated in rat gastrointestinal tract in vivo and in situ. When bound [14C]PteGlu was given to rat intragastrically via oral intubation, a considerable amount of PteGlu was released from folate-binding protein under the acidic conditions in stomach, and it recombined with folate-binding protein in jejunum in vivo. Compared with free PteGlu, bound PteGlu was more gradually absorbed in small intestine, but finally the total amount of bound PteGlu absorbed was almost the same as that of free PteGlu. In all experiments in situ, bound PteGlu was only slightly absorbed in jejunum, where free PteGlu was rapidly absorbed under the same conditions. On the other hand, the absorption rates of the two forms of PteGlu were almost similar to each other in ileum. These results suggest that PteGlu bound to folate-binding protein is absorbed by a manner different from that of free PteGlu in rat gastrointestinal tract.

Animals↗
PubMed1983

Evidence for an essential arginyl residue in bovine milk gamma-glutamyltransferase.

Treatment of bovine milk gamma-glutamyltransferase with 2,3-butanedione in borate buffer markedly inactivates its gamma-glutamyltransferase activity. Inactivation is prevented by a combination of the gamma-glutamyl donor and acceptor substrates, glutathione, and glycylglycine, but less effectively by only one of them. Serine plus borate of maleate provides no protection against the inactivation. Amino acid analysis of the enzyme treated with butanedione in the presence and absence of the protecting substrate combination indicates that complete inactivation correlates with the modification of a single arginyl residue per molecule. The residue modified is associated with the smaller subunit of the two equal subunits which comprise the enzyme. The butanedione-treated enzyme retains a hydrolytic activity, another but less significant catalytic function of the enzyme. The results indicate that the arginyl residue is involved in recognizing the anionic moiety of the acceptor and in binding it to the acceptor site located on the smaller subunit of the enzyme.

Amino Acids↗
PubMedDate not supplied

Grooming behavior in mice induced by stimuli of corn oil in oral cavity.

Mice show a strong preference for corn oil, which was thought to be elicited by stimulation in the oral cavity. Grooming behavior is known to be induced by dopamine D(1) stimulation in rodents. Therefore, we evaluated stimulation by corn oil in the oral cavity and the contribution of D(1) receptors to corn-oil-induced grooming in mice. Intraoral injection (0.1 ml) of corn oil induced grooming behavior similarly to SKF 38393 (10 mg/kg i.p.), a D(1) agonist, and both were antagonized by pretreatment with SCH 23390, a D(1) antagonist. However, a higher dose was needed for antagonism of the corn-oil-induced grooming compared with that induced by SKF 38393. Long-chain fatty acids, their methyl esters and alcohol, their triglycerides, mineral oil and silicone oil but not glycerin, a short-chain triglyceride, xanthan gum solution, or sucrose solution also induced grooming in mice. Xanthan gum solution, which was suggested to mask oil-like texture, attenuated the silicone-oil- but not corn-oil-induced grooming when injected intraorally as a mixture with an equal volume of the oil (50% suspension). The silicone-oil-induced grooming was reduced by SCH 23390 similarly to that induced by corn oil. These results suggested that stimulation by the oil-like texture in the oral cavity in mice induced grooming behavior and that it might be mediated at least partially via D(1) receptors. Moreover, stimuli other than texture might also contribute to the corn-oil-induced grooming.

2,3,4,5-Tetrahydro-7,8-dihydroxy-1-phenyl-1H-3-ben↗
PubMedDate not supplied

Monitor peptide (rat pancreatic secretory trypsin inhibitor) directly stimulates the proliferation of the nontransformed intestinal epithelial cell line, IEC-6.

BACKGROUND/AIMS: The growth-stimulating activity of monitor peptide [rat pancreatic secretory trypsin inhibitor (PSTI)-61] was evaluated in the rat intestinal epithelial cell line IEC-6. In response to food intake, monitor peptide induces cholecystokinin release and the subsequent secretion of pancreatic enzyme into the rat small intestine. METHODS: Monitor peptide was purified from rat bile-pancreatic juice. The proliferation of IEC-6 cells was determined by both counting cell number and [3H]-thymidine incorporation. Ornithine decarboxylase (ODC) activity was assessed by radiometric technique using L-[1-14C]-ornithine. RESULTS: Monitor peptide (10(2)-10(5) ng/ml) induced a significant increase in the incorporation of [3H]-thymidine into IEC-6 cells, and this effect was observed in a dose-dependent manner. A significant increase in the cell number was also observed. An antibody specific for the synthetic NH2-terminal fragment of monitor peptide completely abrogated the growth-stimulating effects of this peptide. In addition, monitor peptide effectively increased the ODC activity of IEC-6 cells. CONCLUSIONS: These results indicate that monitor peptide stimulates the growth of intestinal epithelial cells, and suggest that polyamine metabolism may be involved in this mechanism of growth induction.

Animals↗