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Biomedical subjects

K Ishihara

Publications and source records attributed to K Ishihara.

At least 775 records · Page 43Linked to original sources
PubMed1981

[The phenol turbidity test for measurement of pulmonary surfactants in amniotic fluid--rapid test for fetal lung maturity (author's transl)].

A simple and sensitive procedure for the quantitative estimation of pulmonary surfactants in the amniotic fluid is described. The method is based on the formation of turbidity from the amniotic fluid surfactants with phenol. Amniotic fluid drawn through an intrauterine catheter was centrifuged at 2000 rpm for 5 min. One ml of 5% aqueous phenol solution was added to 1.0 ml of the diluted supernatant. Control solution was prepared by addition of 1.0 ml of distilled water to the supernatant, instead of phenol solution. The turbidity was measured spectrophotometrically against control at 340 nm 5 to 10 min after agitation on a Vortex mixer for 5 sec. The turbidity obtained from amniotic fluid with phenol was proportional to the increase in total phospholipids in the fluid measured enzymatically. Moreover, only lecithin in the phospholipids was related to the turbidity formation. Sphyngomyelin, lysolecithin, phosphatidylethanolamin did not produce any turbidity with phenol. The spectrophotometric reading of 87 cases (31-41 weeks) was ranged at 0.18-3.52. Four cases with lower value (0.40) showed neonatal respiratory problem. The phenol turbidity test is more useful for the detection of fetal lung maturity comparing with the generally used shake test.

Amniotic Fluid↗
PubMed1980

The common identity of UDP-N-acetylgalactosamine 4-sulfatase, nitrocatechol sulfatase (arylsulfatase), and chondroitin 4-sulfatase.

Evidence is presented indicating that three sulfatase activities towards UDP-N-acetylgalactosamine 4-sulfate, nitrocatechol sulfate, and chondroitin 4-sulfate are functions of the same hen oviduct enzyme. Using chondroitin [35S]sulfate from chick embryo cartilage, it is shown that hydrolysis of ester sulfate by this enzyme is limited to 4-sulfate groups occurring in the non-reducing terminal N-acetylgalactosamine 4-sulfate and N-acetylgalactosamine 4,6-bissulfate residues.

Animals↗
PubMed1980

Correlation of quantitative changes of gastric mucosal glycoproteins with aspirin-induced gastric damage in rats.

Quantitative changes of gastric mucosal glycoproteins with the gastric damage induced by acetylsalicylic acid (aspirin) in rat have been studied. Gastric injury was easily observed macroscopically within one hour after the oral administration of aspirin. The most striking changes occurred at five hours, and the injury was overcome within nine hours after dosing. The glycoproteins extracted from rat stomack with Tris buffer containing Triton X-100 were fractionated on Bio-Gel A-1.5 m column chromatography and divided into three fractions. The first peak, corresponding to gastric mucus macromolecular neutral and acidic glycoproteins with or without sulphate (Fr.I), was diminished after aspirin administration. A considerable alteration of Fr.I (49% of control) appeared at three hours, and a gradual return to the control value was observed subsequently. The changes in the amount of the glycoproteins were detected before the macroscopical changes of the mucosa. These results suggest that gastric ulceration induced by aspirin may be caused by a deficiency of gastric mucus macromolecular glycoproteins of gastric mucus.

Animals↗
PubMed1980

Increase of pancreatic somatostatin concentration in early phases of streptozotocin diabetes in rats.

A small yet significant increase of immunoassayable pancreatic somatostatin concentration (0.107 +/- 0.005 vs. 0.156 +/- 0.017 microgram/g at 24 hr, p less than 0.05) was found in rats, 24 hr as well as 7 days after treatment with a diabetogenic dose of streptozotocin (65 mg/kg BW). These animals were characterized by marked decreases of insulin in the pancreas without any significant changes in pancreatic glucagon concentration. These results suggest that an abrupt deprivation of insulin from islets results in an elevation of pancreatic somatostatin concentration, and that glucagon in the pancreas plays a minor role in determining pancreatic somatostatin concentration in rats with insulin-deprived diabetes of short duration.

Animals↗
PubMed1980

Pancreatic insulin, glucagon and somatostatin concentrations in rats with islet cell tumors induced by streptozotocin.

Hyperinsulinemic and hypoglycemic rats with islet tumors induced by streptozotocin were shown to have significantly decreased immunoreactive insulin and somatostatin concentration (expressed as per g wet weight (w. wt) and content (expressed as per whole pancreas) in the pancreas surrounding the tumor as compared to those of age and weight adjusted controls. The pancreatic glucagon concentration of the former was significantly lower than that of the latter but no significant difference between glucagon content in the two groups was observed. Thus, inverse relationships were demonstrated between circulating insulin and somatostatin as well as insulin in the pancreas. It is suggested that a large amount of insulin in plasma results in a decrease in pancreatic insulin and somatostatin.

Adenoma, Islet Cell↗
PubMed1980

Portal somatostatin responds to intragastric glucose: effects of streptozotocin diabetes.

Changes in somatostatin levels in portal response to intragastric glucose loading were examined in normal controls and streptozotocin diabetic rats for one week duration. The mean (+/- SEM) basal level of somatostatin was more significantly elevated in diabetic rats (401 +/- 62 pg/ml) than in controls (171 +/- 13 pg/ml). However, no significant difference in somatostatin concentrations 30 min after glucose loading was found between diabetic and control animals (587 +/- 113 vs. 443 +/- 47 pg/ml). Glucose loading caused a significant elevation of somatostatin in controls, but not in diabetic rats. These results suggest a physiologic role of somatostatin in nutrient homeostasis, and that abnormalities in D cell function are present in streptozotocin diabetes of short duration.

Animals↗
PubMed1980

Somatostatin concentration responds to arginine in portal plasma: effects of fasting, streptozotocin diabetes, and insulin administration in diabetic rats.

Changes of somatostatin concentration in response to a single i.v. injection of arginine (400 mg/kg body weight) were examined in extracted portal plasma of normal and diabetic rats in the fully fed state and after 24 h or fasting, as well as in diabetic rats treated with insulin for one week. In both normal and diabetic animals fasted for 24 h, the basal level of somatostatin declined but the magnitude of the arginine-induced elevation of somatostatin was not affected, suggesting a physiologic role of the tetradecapeptide in nutrient homeostasis. When compared with intact rats, diabetic animals were shown to have increased levels of somatostatin before and after arginine administration, both of which were attenuated by insulin replacement therapy. These findings suggest that alterations of D cell function in streptozotocin diabetes may be related to either insulin deficiency or its metabolic consequences.

Animals↗