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Biomedical subjects

M Shiota

Publications and source records attributed to M Shiota.

At least 145 records · Page 8Linked to original sources
PubMed1985

[Fundamental and clinical studies on aztreonam in the field of obstetrics and gynecology].

Fundamental and clinical studies were performed on aztreonam (AZT), a new antibiotic with single beta-lactam ring, with the following results. Following intravenous drip infusion of 1 g, transfer of AZT to the internal genital organs was found to be good. Transfer of AZT to exudate of pelvic dead space was also good. AZT was given to 6 cases, who had gynecological or obstetrical infectious disease. AZT was effective in the 5 cases out of 6, although it showed high MIC against bacteria isolated from the effective cases. The above results demonstrated that AZT was a safe and effective drug.

Adult↗
PubMed1985

[Basic and clinical studies on cefminox in the field of obstetrics and gynecology].

Basic and clinical studies were carried out on cefminox (CMNX, MT-141), a new cephem antibiotic. Results obtained were as follows. Following each 1 g of intravenous drip infusion and intravenous injection, transfer of CMNX to the internal genital organs was good. Transfer of CMNX into exudate of the pelvic dead space was also good and showed high concentration. CMNX was given to 2 cases. Clinical efficacy was good in 1 case, and could not be evaluated in 1 case. No side effects were observed in both cases. The above results show that CMNX is an effective agent.

Adult↗
PubMed1985

[Fundamental and clinical studies on cefpimizole in the field of obstetrics and gynecology].

The findings from fundamental and clinical studies on cefpimizole (AC-1370) in the treatment of infections in obstetrics and gynecology are reported. We investigated the transfer of AC-1370 into female genital tissues of 6 patients and the transfer of the drug into the pelvic dead space exudate in 9 patients by means of determining its concentrations in the tissues 90 to 210 minutes after the end of intravenous drip infusion of the drug over 1 hour. The mean concentration was 13.06 micrograms/g for the oviduct, 16.50 micrograms/g for the ovary, 16.50 micrograms/g for the endometrium, 14.92 micrograms/g for the myometrium, 16.58 micrograms/g for the uterine cervix, 17.75 micrograms/g for the portio vaginalis, 10.46 micrograms/ml for the uterine arterial serum and 9.91 micrograms/ml for the antecubital venous serum. The drug proved to be well transferred into the pelvic dead space exudate; it reached a peak of mean 2 hours after the end of the intravenous drip infusion of the drug over 1 hour, then decreased steadily, and was found to be a mean of 16.7 micrograms/ml even 8 hours after the end of the intravenous drip infusion. Four patients with infections in obstetrics and gynecology were then treated with AC-1370. Three out of the 4 patients responded to the treatment, while the response of another patient was unknown. None of the 4 patients showed any side effects of the drug or any abnormalities in laboratory findings.

Adult↗
PubMed1984

Lactate metabolism in the perfused rat hindlimb.

A preparation of isolated rat hindleg was perfused with a medium consisting of bicarbonate buffer containing Ficoll and fluorocarbon, containing glucose and/or lactate. The leg was electrically prestimulated to deplete partially muscle glycogen. The glucose was labelled uniformly with 14C and with 3H in positions 2, 5 or 6, and lactate uniformly with 14C and with 3H in positions 2 or 3. Glucose carbon was predominantly recovered in glycogen, and to a lesser extent in lactate. The 3H/14C ration in glycogen from [5-3H,U-14C]- and [6-3H,U-14C]-glucose was the same as in glucose. Nearly all the utilized 3H from [2-3H]glucose was recovered as water. Insulin increased glucose uptake and glycogen synthesis 3-fold. When the muscle was perfused with a medium containing 10 mM-glucose and 2 mM-lactate, there was little change in lactate concentration. 14C from lactate was incorporated into glycogen. There was a marked exponential decrease in lactate specific radioactivity, much greater with [3H]- than with [14C]-lactate. The 'apparent turnover' of [U-14C]lactate was 0.28 mumol/min per g of muscle, and those of [2-3H]- and [3-3H]-lactate were both about 0.7 mumol/min per g. With 10 mM-lactate as sole substrate, there was a net uptake of lactate, at a rate of about 0.15 mumol/min per g, and the apparent turnover of [U-14C]lactate was 0.3 mumol/min per g. The apparent turnover of [3H]lactate was 3-5 times greater. When glycogen synthesis was low (no prestimulation, no insulin), the incorporation of lactate carbon into glycogen exceeded that from glucose, but at high rates of glycogen deposition the incorporation of lactate carbon was much less than that of glucose. Lactate incorporation into glycogen was similar in fast-twitch white and fast-twitch red muscle, but was very low in slow-twitch red fibres. We find that (a) pyruvate in muscle is incorporated into glycogen without randomization of carbon, and synthesis is not inhibited by mercaptopicolinate or cycloserine; (b) there is extensive lactate turnover in the absence of net lactate uptake, and there is a large dilution of 14C-labelled lactate from endogenous supply; (c) there is extensive detritiation of [2-3H]- and [3-3H]-lactate in excess of 14C utilization.

Animals↗
PubMed1983

Proteolytic activation of calcium-activated, phospholipid-dependent protein kinase by calcium-dependent neutral protease.

A Ca2+-dependent protease I), which hydrolyzes casein at Ca2+ concentrations lower than the 10(-5) M range, is purified roughly 4000-fold from the soluble fraction of rat brain. This protease is able to activate Ca2+-activated, phospholipid-dependent protein kinase (protein kinase C) by limited proteolysis analogously to the previously known Ca2+-dependent analogously to the previously known Ca2+-dependent protease (Ca2+ protease II) which is active at the millimolar range of Ca2+ (Inoue, M., Kishimoto, A., Takai, Y., and Nishizuka, Y. (1977) J. Biol. Chem. 252, 7610-7616). The protein kinase fragment thus produced shows a molecular weight of about 5.1 X 10(4), and is significantly smaller than native protein kinase C (Mr = 7.7 X 10(4). Although protein kinase C may be normally activated in a reversible manner by the simultaneous presence of phospholipid and diacylglycerol at Ca2+ concentrations less than 10(-6) M, this enzyme fragment is fully active without any lipid fractions and independent of Ca2+. The limited proteolysis of protein kinase C is markedly enhanced in the velocity by the addition of phospholipid and diacylglycerol, which are both required for the reversible activation of the enzyme. However, casein hydrolysis by this protease is not affected by phospholipid and diacylglycerol. Available evidence suggests that, at lower concentrations of this divalent cation, Ca2+ protease I reacts preferentially with the active form of protein kinase C which is associated with membrane, and converts it to the permanently active form. In contrast, the inactive form of protein kinase C, which is free of membrane phospholipid, does not appear to be very susceptible to the proteolytic attack. It remains unknown, however, whether this mechanism of irreversible activation of protein kinase C does operate in physiological processes. It is noted that Ca2+ protease II, which is active at higher concentrations of Ca2+, proteolytically activates protein kinase C irrespective of the presence and absence of phospholipid and diacylglycerol.

Animals↗
PubMed1982

Cancer of the pancreas with hyperamylasemia.

A 66-yr-old woman had several attacks resembling relapsing acute pancreatitis with elevation of serum amylase for about three months. Obstruction of the main pancreatic duct was detected with endoscopic retrograde pancreatoductography, though no abnormality was revealed on celiac and mesenteric arteriograms. At that time she had no jaundice. Laparotomy revealed a walnut-sized tumor in the head of the pancreas compressing the main pancreatic duct. Pancreaticoduodenectomy was performed. The pathological diagnosis of the tumor was well-differentiated papillary cysto-adenocarcinoma of the pancreas. She had no attack of hyperamylasemia since the operation, and is well 2 years after the surgery. Close attention to persistent elevation of pancreatic amylase levels in serum and urine would enhance the chance of detection of small pancreatic cancers before the development of jaundice.

Aged↗
PubMed1982

Intracellular redox state and control of gluconeogenesis in perfused chicken liver.

The role of the cellular redox state in the control of gluconeogenesis was studied in hemoglobin-free perfused chicken liver, by fluorimetric measurement of the redox states of intracellular pyridine nucleotides. The aminotransferase inhibitor, aminooxyacetate, completely inhibited gluconeogenesis from lactate in the perfused rat liver and to a small extent in the perfused chicken liver. In chicken liver, the highest rate of glucose production was seen with lactate, followed by fructose, pyruvate, and glycerol. When compared at 5 mM, the rate of glucose production from pyruvate was only 10% of that from lactate. Glucose production from a pyruvate/lactate mixture decreased with increasing proportions of pyruvate, together with redox changes of pyridine nucleotides to a more oxidized state. Increased reduction of pyridine nucleotides upon infusion of ethanol was associated with an increased glucose production from pyruvate, and the increase was abolished during octanoate infusion. This abolishment was accompanied by an increase in the acetoacetate to beta-hydroxybutyrate ratio with an oxidation of pyridine nucleotides. The octanoate-inhibited gluconeogenesis occurred at the higher lactate concentration (10 mM) with a transient oxidation of pyridine nucleotides. No significant inhibition was observed at 1 mM lactate, although an instant reduction of pyridine nucleotides was taking place. The rate of beta-hydroxybutyrate generation during octanoate infusion was 2.2 times higher at 1 mM than at 10 mM lactate. The inhibitory effect of octanoate on glyconeogenesis was completely relieved by the addition of NH4Cl. The results demonstrate that the regeneration of NADH in the cytosol is limited in chicken liver, and that gluconeogenesis is regulated, in part, by alteration in the redox states of mitochondria and cytosol.

Ammonium Chloride↗
PubMed1982

Stimulation of gluconeogenesis by glucagon and norepinephrine in the perfused chicken liver.

The effects of glucagon and norepinephrine on gluconeogenesis by perfused chicken liver were studied with fluorimetric monitoring of the redox states of the intracellular pyridine nucleotides. Glucagon stimulated glucose production from precursors entering the pathway both above and below the level of triose phosphates without causing a detectable effect on the redox states of pyridine nucleotides. Glucagon stimulation was not abolished by subsequent infusion of octanoate or ethanol. The presence of a pyruvate/lactate mixture plus NH4Cl resulted in a maximum efficacy of glucagon. Glucose production from lactate and fructose was stimulated by norepinephrine. Norepinephrine always caused a change towards increased reduction of pyridine nucleotides with an increase in the beta-hydroxybutyrate/acetoacetate ratio, but displayed no stimulation of glucose and lactate production from pyruvate. As a result of octanoate infusion with lactate, the changes induced by norepinephrine were reversed. The responses to norepinephrine and phenylephrine were decreased markedly in liver perfused with a calcium-free medium and/or with phentolamine. Infusion of calcium into the calcium-deficient liver caused an abrupt elevation of glucose production together with a reduction of pyridine nucleotides, and the original response to norepinephrine was recovered. The results demonstrate that the effects of glucagon and norepinephrine on gluconeogenesis are not identical, and that norepinephrine stimulation is mediated through an alpha-adrenergic and calcium-dependent mechanism in which redox changes of mitochondrial pyridine nucleotides are involved.

Animals↗
PubMed1981

Calcium-dependent neural proteases, widespread occurrence of a species of protease active at lower concentrations of calcium.

A species of neutral protease having high affinity for Ca2+ in the 10(-5) M range, originally found in canine cardiac muscle (Mellgren, R.L. (1980) FEBS Lett. 109, 129-133), is detected in a wide variety of rat tissues when a sensitive assay with 125I-iodinated casein as substrate is employed. This species of protease absolutely requires Ca2+, and other divalent cations are practically inactive. Although the activity of this enzyme apparently shows striking diversity among tissues tested, the enzymes obtained from various sources reveal similar physical and kinetic properties, and are capable of activating as Ca2+-activated, phospholipid-dependent protein kinase by limited proteolysis. The enzyme has a pH optimum at 7.5 to 8.0 and a molecular weight of about 8.8 X 10(4). The enzyme in its purified form is very sensitive to leupeptin and other thiol-protease inhibitors, but that in crude preparations is far less susceptible to the same inhibitors.

Animals↗
PubMed1980

Intracellular redox state and stimulation of gluconeogenesis by glucagon and norepinephrine in the perfused rat liver.

The role of the cellular redox state in the hormonal stimulation of gluconeogenesis was studied in hemoglobin-free perfused rat liver, by fluorimetric measurement of the redox states of intracellular pyridine nucleotides. The maximum rate of glucose production from lactate/pyruvate mixture was observed with a lactate/pyruvate ratio of 10/1, which corresponds to the ratio observed in vivo. Increased reduction of pyridine nucleotides on infusion of ethanol or octanoate was associated with an increased production of glucose from pyruvate, whereas glucose production from lactate decreased. Stimulation of gluconeogenesis from lactate by glucagon was affected by the lactate/pyruvate ratio; a decrease of the lactate/pyruvate ratio resulted in a decrease of the efficacy of glucagon. Stimulation by glucagon of glucose production from pyruvate was abolished during octanoate infusion, although it was still observable during ethanol infusion. In contrast to glucagon, the stimulatory effect of norepinephrine on gluconeogenesis was unaffected by the ratio of lactate to pyruvate. Norepinephrine in the presence of octanoate and ethanol still induced stimulation of glucose production from lactate and pyruvate, which was always accompanied by a transient reduction of pyridine nucleotides. The results demonstrate that the regeneration of NADH in the cytosol is one of the regulatory factors in gluconeogenesis, and that the effects of glucagon and norepinephrine on gluconeogenesis and on the redox state of pyridine nucleotides are not identical.

Animals↗
PubMed1980

Effects of calcium ions on the activation of gluconeogenesis by norepinephrine in perfused rat liver.

The effects of calcium ions on the activation of gluconeogenesis by norepinephrine were studied in the perfused rat liver. The norepinephrine-mediated enhancement of gluconeogenesis was accompanied by a transient increase in the reduction level of pyridine nucleotides. There was a positive correlation between the increases in the rate of glucose production and the reduction level of pyridine nucleotides induced by norepinephrine. These changes were "dose-dependent" with respect to the norepinephrine concentration from 5 nM to 1 muM and were mimicked by phenylephrine. The omission of calcium from the perfusate did not modify the basal rate of gluconeogenesis from lactate and pyruvate or the increased rate of glucose production induced by glucagon and isoproterenol. The extents of the responses to norepinephrine and phenylephrine, however, were decreased markedly in liver perfused with a calcium-free medium and/or with phentolamine. Infusion of calcium into the calcium-deficient liver caused an abrupt elevation of glucose production together with a transient reduction of pyridine nucleotides, and the original extent of the response to norepinephrine was recovered. The data presented provide evidence indicating that stimulation of gluconeogenesis by norepinephrine is mediated through an alpha-adrenergic and calcium-dependent mechanism in which redox changes of mitochondrial pyridine nucleotides are involved.

Animals↗
PubMed1979

Studies on the Sm-Co magnet as a dental material.

The Sm-Co magnet has superior and convenient magnetic properties as compared with conventional ones used hitherto in prosthesis, and even very small pieces can provide the force necessary in dentistry. Also, the magnet has high corrosion resistance and is innocuous to tissues. Therefore, it can be used as a dental material, overcoming the limitations in past applications.

Animals↗