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Biomedical subjects

I Koyama

Publications and source records attributed to I Koyama.

At least 19 recordsLinked to original sources
PubMed1992

Selective inhibition of homosynaptic depression in a tetanized pathway by an adenosine A1 blocker in the CA1 region of rat hippocampal slice.

The involvement of adenosine A1 receptors in post-tetanic depression (PTD) of CA1, induced by 5 Hz, 20 s stimulation to the Schaffer collateral/commissural fibers was studied in the rat hippocampal slice. The tetanic stimulation induced post-tetanic depression (PTD) lasting for 5-10 min in the excitatory postsynaptic potentials (EPSP) and the population spike (PS) of the tetanized pathway (homosynaptic PTD), and of a non-tetanized pathway (heterosynaptic PTD). 8-Cyclopentyltheophylline (an adenosine A1 antagonist) blocked the induction of homosynaptic PTD, but not of heterosynaptic PTD. These results indicate that adenosine released during tetanic stimulation acts on the A1 receptor to induce the homosynaptic PTD.

Animals↗
PubMed1992

Intestinal type alkaline phosphatase hyperphosphatasemia associated with liver cirrhosis.

Hyperphosphatasemia due to increased intestinal type serum alkaline phosphatase was noted in a 48-year-old male who had asymptomatic liver cirrhosis. The alkaline phosphatase activity in the serum was 828 U/l (our reference range in adults: 57-194 U/l), 94% of which was of the intestinal type as measured by an immunoprecipitation method. The intestinal component of alkaline phosphatase was separated into two major and some minor components using electrophoresis and isoelectrofocusing. One of the major components had similar mobility to that of a standard intestinal enzyme purified from adult intestine. The components were heat-labile and neuraminidase-resistant. Serial lectin affinity chromatography, however, indicated that sugar chain compositions of the alkaline phosphatase were different from those of the standard tissue intestinal enzyme. These results and further enzymological studies suggest that the patient's serum alkaline phosphatase basically consisted of several intestine-like isoforms.

Alkaline Phosphatase↗
PubMed1992

Chemical nature of intestinal-type alkaline phosphatase in human kidney.

Approximately 10% of the alkaline phosphatase activity in human kidney is derived from the intestinal-type alkaline phosphatase isoform, which can be differentiated from adult intestinal alkaline phosphatase by selective reactivity with monoclonal antibodies. The NH2-terminal sequence of the renal intestinal-type alkaline phosphatase was shown to be identical to sequences of the adult and meconial alkaline phosphatases except for the NH2-terminal valine residue, which is missing in the renal intestinal-type enzyme. Incubation of purified meconial alkaline phosphatase with kidney homogenate resulted in removal of the NH2-terminal valine residue, indicating the presence of aminopeptidases in kidney that catalyze this hydrolysis. Furthermore, the oligosaccharide chains of the renal intestinal-type alkaline phosphatase were shown to differ from those of meconial and adult intestinal alkaline phosphatases, as revealed by lectin affinity chromatography. The heterogeneity of the intestinal-type alkaline phosphatase can therefore be generated both by partial peptide bond hydrolysis and differences in glycosylation.

Alkaline Phosphatase↗
PubMed1991

Liver-like alkaline phosphatase in the tissue-unspecific type enzyme found in rabbit organs.

Rabbit liver and kidney tissues are known to produce an intestinal-like alkaline phosphatase (IAP-like enzyme) as a dominant isozyme, with a minor isozyme of tissue-unspecific type (UAP), unlike humans and other mammalians. We investigated immunohistochemically and biochemically these unique isozymes in the rabbit liver and bone, and compared them with the human isozyme. In rabbit liver, UAP was found to be localized only in the apical part of the membrane of cells lining the bile duct, whereas IAP-like enzyme was found in the sinusoidal membrane of hepatocytes. Rabbit liver UAP was separated from IAP-like enzyme by DEAE-cellulose column chromatography. Rabbit bone tissue contained only one UAP isozyme. The two UAPs were biochemically and physicochemically compared with human liver AP. Both UAPs reacted with an anti-human liver AP monoclonal antibody, not with an anti-human bone AP monoclonal antibody, indicating that both enzymes have the same antigenicity as human liver AP. Rabbit liver and bone UAPs had similar N-linked sugar-chain heterogeneities to the respective human enzymes. In addition, rabbit bone AP also had an O-linked sugar chain, as did human bone AP, unlike rabbit and human liver APs.

Alkaline Phosphatase↗
PubMed1991

Purification and partial characterization of intestinal-like alkaline phosphatase in rabbit kidney.

Two types of alkaline phosphatase (AP) isozymes in rabbit kidney, a major intestinal-like type and a minor tissue-unspecific type, have been identified. The former enzyme was purified from rabbit kidney by immunoaffinity chromatography using monoclonal anti-human intestinal AP antibody. The purified enzyme yielded a single protein band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and the apparent molecular size of its monomer subunit was found to be 72,000. Three amino acid residues within the first 16 N-terminal amino acid residues were different in purified AP and human intestinal AP. Although the rabbit enzyme possessed some peptide bands identical to those of human adult intestinal AP after Staphylococcus aureus V8 protease digestion, the enzyme did not react with monoclonal antibody against human adult intestinal AP alone, whereas it did react with monoclonal antibody against both human adult and fetal intestinal APs. The affinity of the enzyme for concanavalin A was identical to that of the fetal intestinal AP, but different from that of the adult enzyme. These results indicate that the antigenicity and certain properties of purified rabbit AP are more like those of human fetal intestinal AP or Kasahara isozyme, so-called intestinal-like AP, than like human adult intestinal AP.

Alkaline Phosphatase↗
PubMed1991

Regional differences in cholinergic innervation and drug sensitivity in the smooth muscles of pig stomach.

1 To evaluate the regional differences in cholinergic mechanisms in the stomach, innervation and receptor distribution were investigated by isometric tension recording, receptor binding assay and measurement of nerve-related enzyme activity in longitudinal and circular smooth muscle layers isolated from various regions of the pig stomach. 2 The response to transmural nerve stimulation (TMS) varied with the muscle layer and portion of stomach tested. Contraction was predominant in the smooth muscle from the pyloric antrum, relaxation in the corpus region. 3 The contraction to TMS was abolished by atropine (0.1-0.5 microM) and potentiated by physostigmine (1-2 microM). On the other hand, relaxation to TMS was unaffected by a combination of phentolamine and carteolol but was abolished by tetrodotoxin (TTX) (0.67-1.54 microM). In all preparations from various portions, physostigmine unmasked the contraction and atropine revealed the relaxation to TMS. 4 The activity of choline acetyltransferase (ChAT) and cholinesterase (ChE) was higher in longitudinal than in circular muscle layers and was also higher in the fundus than in any other portion. 5 The sensitivity (pD2 value) to acetylcholine (ACh) was higher in the longitudinal than in the circular muscle layers but did not differ largely among different regions of the stomach. The maximum response induced by ACh was also highest in longitudinal muscle of the fundus. In contrast, the population of muscarinic receptors, estimated from [3H]-QNB binding, increased from the fundic to pyloric portions. 6 These results suggest that there are regional differences in the responses to nerve stimulation in pig stomach, which are likely to depend partly on the quantitative differences in cholinergic nerve supply and in the responsiveness to ACh.

Acetylcholine↗
PubMed1990

Developmental changes in the antigenicity and sugar-chain heterogeneity of rabbit alkaline phosphatases.

1. Rabbit alkaline phosphatases (APs) clearly fused with the anti-human AP antibodies. In particular, fetal liver and kidney APs reacted slightly less with the anti-intestinal AP antibody as did adult enzymes, suggesting that intestinal AP-like isozyme is expressed at earlier stages of gestation in rabbit liver and kidney. 2. Immunohistochemical data indicated that intestinal AP-like isozyme in the kidney was mainly localized in the distal convoluted tubules and slightly in the proximal straight tubules, whereas liver/bone/kidney AP-like enzyme was found more in the glomeruli and interstitial capillary walls as a major component. 3. The sugar-chain heterogeneity of adult and fetal rabbit APs displayed organ-specificity as did of rat and human APs. Moreover, in fetal development, the expression of high-mannose type or hybrid type sugar chains precedes the expression of complex type sugar chains in fetal development.

Aging↗
PubMed1990

Effectiveness of taurine in protecting biomembrane against oxidant.

The effect of taurine in protecting biomembrane attacked by hypochlorous acid (HOCl) was examined using canine erythrocytes which had been pre-treated with HOCl. In the treatment, most of the HOCl was consumed as a result of its reaction with a number of electrophilic substances, such as free amino groups (-NH2) in the membrane, whereas hemoglobin inside the cells was not oxidized. The lysis of HOCl-treated erythrocytes was dependent on the concentration of HOCl and on the incubation time at 37 degrees C. Taurine inhibited the lysis at 37 degrees C in a dose dependent manner. During the incubation of HOCl-treated erythrocytes with taurine, an appreciable amount of monochlorotaurine (TauNHCl) was detected in the supernate. This suggests that taurine might remove the oxidized chlorine from HOCl-treated erythrocytes, resulting in the production of TauNHCl. The effect of taurine on the removal of Cl+ moiety was further examined using Sepharose gel with free amino groups. Taurine removed Cl+ moiety from HOCl-treated Sepharose gel, and the yield of TauNHCl depended on the concentration of taurine and the incubation time. These results indicate that taurine might inhibit the hemolysis by scavenging the oxidized chlorine moiety from the HOCl-treated erythrocytes. Inhibition of the HOCl-induced hemolysis was also observed with other amino acids.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗