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Biomedical subjects

Masayuki Takeuchi

Publications and source records attributed to Masayuki Takeuchi.

At least 19 recordsLinked to original sources
PubMed2006

Highly enantioselective recognition of dicarboxylic acid substrates by the control of nonlinear responses.

An allosteric host, in which the molecular information of the chiral guest was precisely introduced, exhibits unconventional enantioselectivity toward the target enantiomer even under the conditions of a -20% enantiomeric excess (ee) mixture within a certain concentration window. This is effected by incorporation of the structural information of the enantiomer into the host and the utilization of multiple equilibrium.

Journal Article↗
PubMed2006

Olefin metathesis of the aligned assemblies of conjugated polymers constructed through supramolecular bundling.

The ordered structures constructed from an aligner molecule 1o and conjugated polymers (CPs) were efficiently converted into the poly-pseudo-rotaxane structures by the template-assisted ring-closing olefin metathesis (RCM) of olefinic groups at the peripheral positions of 1o. Moreover, the poly-pseudo-rotaxane structures permitted the separation of the crystalline ordered assemblies of CP by size exclusion chromatography and the preservation of the sheet morphologies after the treatment with trifluoroacetic acid. The morphologies and the periodicities of assemblies were also maintained after the retrieving treatments.

Journal Article↗
PubMed2005

Post-translational excision of the carboxyl-terminal segment of CaM kinase phosphatase N and its cytosolic occurrence in the brain.

Ca2+/Calmodulin-dependent protein kinase (CaM kinase) phosphatase, occurring in the cytoplasm of all tissues, dephosphorylates and thereby deactivates multifunctional CaM kinases, such as CaM kinases I, II and IV. In contrast, CaM kinase phosphatase N has been reported to occur almost exclusively in the brain and to be localized in the nucleus in the transfected COS-7 cells, as examined immunocytochemically with antibodies against the carboxyl-terminal segment of the enzyme, indicating its involvement in the deactivation of CaM kinase IV. Here, we show that the majority of the naturally occurring CaM kinase phosphatase N in the brain exists not in the intact form of the enzyme (83.4 kDa) but in a form (61.1 kDa) in which the carboxyl-terminal segment containing nuclear localization signals is deleted, and that it is present mostly in the cytoplasm but a little in the nucleus throughout the central nervous system, although occurring mostly in the nucleus in some large neurons. Strong immunostaining of the enzyme was also observed at postsynaptic density. These findings suggest that CaM kinase phosphatase N is involved in the regulation of not only CaM kinase IV but also CaM kinases II and I.

Amino Acid Sequence↗
PubMed2005

Effects of long-term oral treatment with selective vasopressin V2 receptor antagonist (OPC-31260) on adriamycin-induced heart failure in rats.

BACKGROUND: In the treatment of heart failure, the effects of therapeutic agents on life prognosis remains unclear. We investigated the effects of long-term oral administration of a nonpeptide, selective, vasopressin V2 receptor antagonist, OPC-31260, on Sprague-Dawley rats that were treated with adriamycin to induce progressive water retention. METHODS: Intraperitoneal saline was administered to 14 rats as a control (Group 1). A total cumulative dose of 15 mg/kg of adriamycin was administered intraperitoneally in six equal doses over a period of 2 weeks to another 52 rats. Adriamycin-treated rats were further divided into Group 2, which received saline (p.o.), and Group 3, which received 50 mg/kg (p.o.) of V2 antagonist. Oral administration continued every day for 6 weeks. Group 1 rats also received saline (p.o.) for 6 weeks. RESULTS: The V2 antagonist decreased urine osmolality and increased diuresis of rats in Group 3. Urinary excretion of electrolytes was not increased by the V2 antagonist in Group 3. Serum osmolality was likewise unchanged by the V2 antagonist in Group 3. Plasma concentrations of vasopressin were significantly higher in Group 3 than in the other groups (Group 1, 4.0+/-1.1 pg/ml; Group 2, 4.2+/-1.5 pg/ml; Group 3, 8.5+/-1.0 pg/ml; p<0.05). During the experimental period, survival rate was higher in Group 3 than in Group 2 (Group 1, 100%; Group 2, 59%; Group 3, 83%). CONCLUSION: Our data show that administration of orally active V2 antagonist did not reduce the survival of adriamycin-treated rats through continuous aquaretic action, despite elevated plasma levels of vasopressin.

Administration, Oral↗
PubMed2005

Porphyrin-based organogels: control of the aggregation mode by a pyridine-carboxylic acid interaction.

To find a new strategy for designing porphyrin-based organogelators, hydrogen-bond-donating (carboxylic acid)/accepting (pyridine) substituents or electron-donating (dialkylamino)/withdrawing (pyridine) substituents were introduced into peripheral positions of a porphyrin (1cp or 1ep, respectively), and the gelation properties were compared with those of symmetrical reference compounds bearing two pyridyl substituents or two ester groups (1pp or 1ee, respectively). It was found that the symmetrical molecules show a solubility that is quite inferior to that of 1cp and 1ep having a dipole moment and precipitate from most organic solvents. 1cp, 1ep, and 1ee formed gels with cyclohexane, methylcyclohexane, and several alcoholic solvents, but scanning electron microscopy (SEM) and transmission electron microscopy (TEM) observations revealed that their superstructures constructed in the organogels are very different. In cyclohexane, 1cp resulted in a sheetlike structure, whereas 1ep and 1ee resulted in a fiberlike structure. The difference is attributed to the two-dimensional interactive forces in 1cp consisting of the porphyrin-porphyrin pi-pi stacking and the carboxylic acid-pyridine hydrogen bonding. In fact, when the hydrogen-bonding interaction was weakened by alcoholic solvents or by adding pyridine or N,N-(dimethylamino)pyridine, the sheetlike structure was transfigured to the fiberlike structure. Further detailed analyses of their aggregation modes were conducted by spectroscopic methods such as ultraviolet-visible (UV-vis) absorption, Fourier transform infrared (FT-IR), and X-ray diffraction (XRD). On the basis of these findings, the influence of these peripheral substituents on the gel formation and the aggregation mode was discussed.

Journal Article↗
PubMed2005

Identification of major Ca(2+)/calmodulin-dependent protein kinase phosphatase-binding proteins in brain: biochemical analysis of the interaction.

Ca(2+)/calmodulin-dependent protein kinase phosphatase (CaMKP) is a unique protein phosphatase that specifically dephosphorylates and regulates multifunctional Ca(2+)/calmodulin-dependent protein kinases (CaMKs). To clarify the physiological significance of CaMKP, we identified glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and fructose bisphosphate aldolase as major binding partners of CaMKP in a soluble fraction of rat brain using the two-dimensional far-Western blotting technique, in conjunction with peptide mass fingerprinting analysis. We analyzed the affinities of these interactions. Wild type CaMKP-glutathione S-transferase (GST) associated with GAPDH in a GST pull-down assay. Deletion analysis suggested that the N-terminal side of the catalytic domain of CaMKP was responsible for the binding to GAPDH. Further, anti-CaMKP antibody coimmunoprecipitated GAPDH in a rat brain extract. GAPDH was phosphorylated by CaMKI or CaMKIV in vitro; however, when CaMKP coexisted, the phosphorylation was markedly attenuated. Under these conditions, CaMKP significantly dephosphorylated CaMKI and CaMKIV, which had been phosphorylated by CaMK kinase, whereas it did not dephosphorylate the previously phosphorylated GAPDH. The results suggest that CaMKP regulates the phosphorylation level of GAPDH in the CaMKP-GAPDH complex by dephosphorylating and deactivating CaMKs that are responsible for the phosphorylation of GAPDH.

Animals↗
PubMed2004

Molecular design of synthetic receptors with dynamic, imprinting, and allosteric functions.

Sugar recognition in an aqueous system has been achieved using a boronic acid-diol interaction. Combination with an intramolecular amino group has enabled us to read out the binding process as a change in the fluorescence intensity. The novel interaction has been extended to dynamic sugar sensing utilizing an allosteric effect, molecular imprinting, and control of molecular assemblies.

Biomimetics↗
PubMed2004

Helical structures of conjugate polymers created by oxidative polymerization using synthetic lipid assemblies as templates.

The morphology of conjugate polymers (such as poly(ethylenedioxythiophene), poly(pyrrole), and poly(aniline)) can be controlled in their polymerization processes, by applying the concept of the templating method to oxidative polymerization. As oxidative polymerization of these monomers produces cationic intermediates, the anionic assemblies can act as potential templates due to the mutual electrostatic attractive force. Oxidative polymerization of ethylenedioxythiophene (EDOT), pyrrole, and aniline was carried out using helical superstructures of synthetic lipid assemblies as templates. Interestingly, we have found that oxidative polymerization of these monomers results in novel polymeric aggregates, such as a helical-tape structure and an intertwined helical structure, and that both the right-handed and left-handed helical structures can be created by a change in the hydrophilic head groups. This is the first example of helical superstructures composed of conjugate polymers that have been designed utilizing a convenient templating method.

Journal Article↗
PubMed2004

Identification and characterization of nuclear localization signals of CaMKP-N.

Calmodulin-dependent protein kinase phosphatase (CaMKP) and CaMKP-N dephosphorylate and regulate multifunctional Ca(2+)/calmodulin-dependent protein kinases. The enzymatic properties of CaMKP-N and CaMKP resemble each other, whereas their localizations are different. CaMKP-N is localized in the nucleus, whereas CaMKP is localized in the cytosol. In the present study, the nuclear localization signals (NLSs) of CaMKP-N were identified and characterized. CaMKP-N contains two NLSs, NLS1 and NLS2, at the C-terminus. A cluster of basic residues in the NLSs is important for their function. NLS1 and NLS2 function independently, but mutagenesis analysis suggests that these NLSs interact with each other.

Amino Acid Sequence↗