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45 results on '"Shibasaki, Yoshikazu"'

1. Immunogenic Cell Death Induced by Selective Intracellular Vaporization in vitro

Author

Ishijima, Ayumu, Yamaguchi, Satoshi, Azuma, Takashi, Kobayashi, Etsuko, Kakimi, Kazuhiro, Shibasaki, Yoshikazu, Nagamune, Teruyuki, Sakuma, Ichiro, Magjarevic, Ratko, Series Editor, Ładyżyński, Piotr, Associate Editor, Ibrahim, Fatimah, Associate Editor, Lackovic, Igor, Associate Editor, Rock, Emilio Sacristan, Associate Editor, Shiraishi, Yasuyuki, editor, Sakuma, Ichiro, editor, Naruse, Keiji, editor, and Ueno, Akinori, editor

Published
2021
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8. Roles of PI 3-kinase and Ras on insulin-stimulated glucose transport in 3T3-L1 adipocytes

Author

Katagiri, Hideki, Asano, Tomoichiro, Inukai, Kouichi, Ogihara, Takehide, Ishihara, Hisamitsu, Shibasaki, Yoshikazu, Murata, Tomiyasu, Terasaki, Jungo, Kikuchi, Yoshio, and Oka, Yoshitomo

Subjects
Phosphatidylinositol -- Physiological aspects, Protein kinases -- Physiological aspects, Fat cells -- Physiological aspects, Glucose metabolism -- Physiological aspects, Biological transport, Active -- Physiological aspects, Biological sciences
Abstract

Cell cultures of 3T3-L1 adipocyte exhibiting overexpression of dominant negative p85alpha and dominant negative Ras (N17Ras) were analyzed to determine the properties of glucose transport in the cell lines. Overexpression of dominant negative p85alpha phosphatidylinositol (PI) 3-kinase in 3T3-L1 increased glucose transport activity. The expression of the dominant negative mutant of p85alpha regulatory subunit of PI 3-kinase also inhibited the translocation of glucose transporters from the intracellular regions to the plasma membrane.

Published
1997

11. Cover Image, Volume 2, Issue 4

Author

Ishijima, Ayumu, primary, Yamaguchi, Satoshi, additional, Azuma, Takashi, additional, Kobayashi, Etsuko, additional, Shibasaki, Yoshikazu, additional, Nagamune, Teruyuki, additional, and Sakuma, Ichiro, additional

Published
2019
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13. Increased liver glucose-transporter protein and mRNA in streptozocin-induced diabetic rats

Author

Oka, Yoshitomo, Asano, Tomoichiro, Shibasaki, Yoshikazu, Lin, Jiann-Liang, Tsukuda, Katsunori, Akanuma, Yasuo, and Takaku, Fumimaro

Subjects
Streptozocin -- Physiological aspects, Type 1 diabetes -- Models, Type 1 diabetes -- Physiological aspects, Liver -- Physiological aspects, Glucose metabolism -- Abnormalities, Health
Abstract

In healthy people, normal blood glucose (sugar) concentrations are maintained by a balance between uptake of glucose by body tissues (using insulin) and release of glucose into the blood by the liver. Both uptake and release of glucose require that glucose be transported across the cell membrane, and a recently recognized class of proteins called glucose transporters (GTs) has been shown to mediate this transport. Different types of GTs have been described, some of which increase their activity in response to insulin, and some of which do not. In insulin-dependent diabetes mellitus (IDDM), the insulin-producing beta-cells of the pancreas are destroyed, with a subsequent failure to regulate blood glucose levels. Glucose metabolism in many tissues is markedly altered in IDDM. Output of glucose by the liver is increased in insulin-deficient conditions. Recent studies have shown that GTs in fat cells are decreased in the diabetic state, but the effect of diabetes on liver GTs has not been investigated. Rats were rendered diabetic with a single injection of streptozocin, which is toxic to the beta-cells. They were maintained for 10 days in the diabetic state, and then for an additional five days either with or without insulin replacement therapy. Levels of liver GTs and an index of the synthesis of liver GTs (GT mRNA levels) were measured. Diabetes caused an increase in liver GT and GT mRNA levels, which was attenuated by insulin replacement therapy. This is in contrast to the levels of GTs and GT mRNA in fat cells, which are decreased in diabetes. These alterations in liver GT levels may be responsible for the increased output of glucose by the liver that is seen in diabetes. (Consumer Summary produced by Reliance Medical Information, Inc.)

Published
1990

16. Epiregulin Recognition Mechanisms by Anti-epiregulin Antibody 9E5

Author

Kado, Yuji, primary, Mizohata, Eiichi, additional, Nagatoishi, Satoru, additional, Iijima, Mariko, additional, Shinoda, Keiko, additional, Miyafusa, Takamitsu, additional, Nakayama, Taisuke, additional, Yoshizumi, Takuma, additional, Sugiyama, Akira, additional, Kawamura, Takeshi, additional, Lee, Young-Hun, additional, Matsumura, Hiroyoshi, additional, Doi, Hirofumi, additional, Fujitani, Hideaki, additional, Kodama, Tatsuhiko, additional, Shibasaki, Yoshikazu, additional, Tsumoto, Kouhei, additional, and Inoue, Tsuyoshi, additional

Published
2016
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20. Association of active γ-secretase complex with lipid rafts

Author

Urano, Yasuomi, primary, Hayashi, Ikuo, additional, Isoo, Noriko, additional, Reid, Patrick C., additional, Shibasaki, Yoshikazu, additional, Noguchi, Noriko, additional, Tomita, Taisuke, additional, Iwatsubo, Takeshi, additional, Hamakubo, Takao, additional, and Kodama, Tatsuhiko, additional

Published
2005
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27. Co-localization of glucokinase with actin filaments

Author

Murata, Tomiyasu, primary, Katagiri, Hideki, additional, Ishihara, Hisamitsu, additional, Shibasaki, Yoshikazu, additional, Asano, Tomoichiro, additional, Toyoda, Yukiyasu, additional, Pekiner, Bilgehan, additional, Pekiner, Can, additional, Miwa, Ichitomo, additional, and Oka, Yoshitomo, additional

Published
1997
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36. Defect in Tyrosine Kinase Activity of the Insulin Receptor from a Patient with Insulin Resistance and Acanthosis Nigricans*

Author

YAMAMOTO, RITSUKO, primary, SHIBA, TERUO, additional, TOBE, KAZUYUKI, additional, SHIBASAKI, YOSHIKAZU, additional, KOSHIO, OSAMU, additional, IZUMI, TETSURO, additional, ODAWARA, MASATO, additional, MIKAMI, YUHEI, additional, MATSUURA, NOBUO, additional, AKANUMA, YASUO, additional, TAKAKU, FUMIMARO, additional, and KASUGA, MASATO, additional

Published
1990
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37. Phosphatidylinositol-4-phosphate 5-kinase γ is associated with cell–cell junction in A431 epithelial cells

Author

Akiyama, Chiyuki, Shinozaki-Narikawa, Naeko, Kitazawa, Takatoshi, Hamakubo, Takao, Kodama, Tatsuhiko, and Shibasaki, Yoshikazu

Subjects
EPITHELIAL cells, CHEMICAL reactions, CELL communication, EPITHELIUM
Abstract

Abstract: Cell to cell contact in epithelial cells is crucial for tissue integrity and is maintained by junctional complexes, such as the adherens junction (AJ). Actin polymerization has been shown to be important for AJ formation; however, the molecular mechanisms have yet to be clarified. It has been shown that increased phosphatidylinositol-4,5-bisphosphate (PIP2) induces actin polymerization. It is thus of interest to know more about the production of PIP2 during cell–cell adhesion formation in epithelial cells. The distribution of phosphatidylinositol-4-phosphate 5-kinase γ635 (PIP5Kγ635), an isoform of the PIP2 synthesizing enzymes, was examined in epithelial cell line A431. It was found that, in non-contact cells, PIP5Kγ635 was not concentrated at the plasma membrane. However, in cells that were in contact, PIP5Kγ635 localized to the intercellular contact sites and colocalized with E-cadherin and β-catenin, two components of AJ, and with polymerized actin, but did not colocalize with focal adhesion, integrin-mediated cell–substratum complex. Decreasing calcium ion concentration induced both disruption of intercellular adhesion and the dissociation of both PIP5Kγ635 and actin from the contact site. These results suggest that PIP5K has an important role in actin polymerization in epithelial cell–cell adhesion. [Copyright &y& Elsevier]

Published
2005
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42. Phosphatidylinositol-4-phosphate 5-kinase gamma is associated with cell-cell junction in A431 epithelial cells.

Author

Akiyama C, Shinozaki-Narikawa N, Kitazawa T, Hamakubo T, Kodama T, and Shibasaki Y

Subjects
Actins metabolism, Adherens Junctions chemistry, Adherens Junctions metabolism, Cadherins metabolism, Calcium pharmacology, Cell Adhesion, Cell Communication drug effects, Cell Line, Tumor, Cytoskeleton metabolism, Epithelial Cells ultrastructure, Focal Adhesions chemistry, Humans, Intercellular Junctions chemistry, Isoenzymes metabolism, Microscopy, Confocal, Epithelial Cells metabolism, Intercellular Junctions metabolism, Phosphotransferases (Alcohol Group Acceptor) metabolism
Abstract

Cell to cell contact in epithelial cells is crucial for tissue integrity and is maintained by junctional complexes, such as the adherens junction (AJ). Actin polymerization has been shown to be important for AJ formation; however, the molecular mechanisms have yet to be clarified. It has been shown that increased phosphatidylinositol-4,5-bisphosphate (PIP2) induces actin polymerization. It is thus of interest to know more about the production of PIP2 during cell-cell adhesion formation in epithelial cells. The distribution of phosphatidylinositol-4-phosphate 5-kinase gamma635 (PIP5Kgamma635), an isoform of the PIP2 synthesizing enzymes, was examined in epithelial cell line A431. It was found that, in non-contact cells, PIP5Kgamma635 was not concentrated at the plasma membrane. However, in cells that were in contact, PIP5Kgamma635 localized to the intercellular contact sites and colocalized with E-cadherin and beta-catenin, two components of AJ, and with polymerized actin, but did not colocalize with focal adhesion, integrin-mediated cell-substratum complex. Decreasing calcium ion concentration induced both disruption of intercellular adhesion and the dissociation of both PIP5Kgamma635 and actin from the contact site. These results suggest that PIP5K has an important role in actin polymerization in epithelial cell-cell adhesion.

Published
2005
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43. Association of active gamma-secretase complex with lipid rafts.

Author

Urano Y, Hayashi I, Isoo N, Reid PC, Shibasaki Y, Noguchi N, Tomita T, Iwatsubo T, Hamakubo T, and Kodama T

Subjects
Amyloid Precursor Protein Secretases, Blotting, Western, Cell Line, Tumor, Detergents pharmacology, Endopeptidases, Humans, Hydroxymethylglutaryl-CoA Reductase Inhibitors pharmacology, Immunoprecipitation, Protein Binding, Aspartic Acid Endopeptidases metabolism, Lipid Metabolism
Abstract

Cholesterol has been implicated in the pathogenesis of Alzheimer's disease (AD). Although the underlying mechanisms are not yet clear, several studies have provided evidence for the involvement of cholesterol-rich lipid rafts in the production of amyloid beta peptide (Abeta), the major component of amyloid deposits in AD. In this regard, the gamma-secretase complex is responsible for the final cleavage event in the processing of beta-amyloid precursor protein (betaAPP), resulting in Abeta generation. The gamma-secretase complex is a multiprotein complex composed of presenilin, nicastrin (NCT), APH-1, and PEN-2. Recent reports have suggested that gamma-secretase activity is predominantly localized in lipid rafts, and presenilin and NCT have been reported to be localized in lipid rafts. In this study, various biochemical methods, including coimmunoprecipitation, in vitro gamma-secretase assay, and methyl-beta-cyclodextrin (MbetaCD) treatment, are employed to demonstrate that all four components of the active endogenous gamma-secretase complex, including APH-1 and PEN-2, are associated with lipid rafts in human neuroblastoma cells (SH-SY5Y). Treatment with statins, 3-hydroxy-3-methylglutaryl-CoA-reductase inhibitors, significantly decreased the association of the gamma-secretase complex with lipid rafts without affecting the distribution of flotillin-1. This effect was partially abrogated by the addition of geranylgeraniol. These results suggest that both cholesterol and protein isoprenylation influence the active gamma-secretase complex association with lipid rafts.

Published
2005
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44. [Visualization of phosphoinositide: signaling lipids in living cells].

Author

Shinozaki-Narikawa N and Shibasaki Y

Subjects
Actins metabolism, Animals, Cell Movement, Endocytosis, Green Fluorescent Proteins, Histocytochemistry, Luminescent Proteins, Phagocytosis, Phosphatidylinositols physiology, Phosphorylation, Phosphatidylinositols metabolism, Signal Transduction
Published
2004

45. Dibasic amino acid residues at the carboxy-terminal end of kinase homology domain participate in the plasma membrane localization and function of phosphatidylinositol 5-kinase gamma.

Author

Arioka M, Nakashima S, Shibasaki Y, and Kitamoto K

Subjects
Amino Acid Sequence, Amino Acids chemistry, Animals, Base Sequence, Cell Line, Cell Membrane enzymology, DNA Primers, Immunohistochemistry, Molecular Sequence Data, Mutagenesis, Site-Directed, Phosphotransferases (Alcohol Group Acceptor) chemistry, Phosphotransferases (Alcohol Group Acceptor) genetics, Sequence Homology, Amino Acid, Amino Acids metabolism, Phosphotransferases (Alcohol Group Acceptor) metabolism
Abstract

Type I phosphatidylinositol 4-phosphate (PI(4)P) 5-kinases (PIP5Ks) catalyze the synthesis of phosphatidylinositol 4,5-bisphosphate (PI(4,5)P(2)), an essential lipid molecule involved in various cellular processes such as regulation of actin cytoskeleton and membrane traffic. The protein localizes to the plasma membrane where its activity has been shown to be regulated by small GTPase ARFs and/or phosphatidic acid. Deletion analysis of amino- or carboxy-terminal sequences of PIP5Kgamma fused with EGFP demonstrated that the presence of central kinase homology domain (KHD), a 380 amino acid-long region highly conserved among PIP5K family, was necessary and sufficient for the plasma membrane localization of PIP5Kgamma. Particularly, the dibasic Arg-Lys sequence located at the carboxy-terminal end of KHD was shown to be crucial for the plasma membrane targeting of PIP5Kgamma, since the deletion or charge-reversal mutation of this dibasic sequence resulted in the mislocalization of the protein to the cytoplasm. Mislocalized mutants also failed to complement the temperature-sensitive growth of Saccharomyces cerevisiae mss4-1 mutant defective in PIP5K function. The presence of dibasic residues at the C-terminal end of KHD was conserved among mammalian as well as invertebrate PIP5K family members, but not in the type II PIPKs that are not targeted to the plasma membrane, suggesting that the conserved dibasic motif provides a mechanism essential for the proper localization and cellular function of PIP5Ks.

Published
2004
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