6 results on '"FUkumoto, H."'
Search Results
2. Evidence for a family of human glucose transporter-like proteins. Sequence and gene localization of a protein expressed in fetal skeletal muscle and other tissues.
- Author
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Kayano, T, Fukumoto, H, Eddy, R L, Fan, Y S, Byers, M G, Shows, T B, and Bell, G I
- Abstract
Complementary DNA clones encoding a glucose transporter-like protein have been isolated from a human fetal skeletal muscle cDNA library. The 496-amino acid fetal muscle glucose transporter-like protein has 64.4 and 51.6% identity with the previously described human erythrocyte/HepG2 and liver glucose transporter sequences, respectively. RNA blotting studies indicate that transcripts encoding this glucose transporter-like protein are present in most tissues, although their relative abundance varies. The gene encoding this protein has been localized to human chromosome 12p13.3. The identification and characterization of a third human glucose transporter-related protein suggests that there is a family of proteins having similar sequences and structures which are involved in nutrient transport by mammalian cells.
- Published
- 1988
- Full Text
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3. Cloning and characterization of the major insulin-responsive glucose transporter expressed in human skeletal muscle and other insulin-responsive tissues
- Author
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Fukumoto, H, Kayano, T, Buse, J B, Edwards, Y, Pilch, P F, Bell, G I, and Seino, S
- Abstract
Complementary DNA clones encoding a facilitative glucose transporter-like protein have been isolated from human small intestine and muscle cDNA libraries. This 509-amino acid protein has 65.3, 54.3, and 57.5% identity with the previously described human erythrocyte/HepG2, liver, and fetal muscle glucose transporter/transporter-like proteins, respectively. RNA blotting studies indicate that transcripts encoding this protein are very abundant in adult human skeletal muscle and subcutaneous fat. The adult skeletal muscle glucose transporter-like protein was expressed in vitroby cDNA-directed transcription and cell-free translation of the synthetic mRNA. The in vitro-synthesized protein reacted with a monoclonal antibody, 1F8, which recognizes the insulin-regulatable glucose transporter expressed in rat skeletal muscle, heart, and adipocytes. In contrast, in vitro-synthesized erythrocyte/HepG2 and fetal muscle glucose transporters did not react with 1F8. The high levels in adult skeletal muscle and subcutaneous fat of mRNA encoding the adult skeletal muscle glucose transporter and its specific reactivity with monoclonal antibody 1F8 suggest that this protein is the major insulin-regulatable glucose transporter expressed in skeletal muscle and other insulin-responsive tissues.
- Published
- 1989
- Full Text
- View/download PDF
4. Rapid regulation of sialidase activity in response to neural activity and sialic acid removal during memory processing in rat hippocampus.
- Author
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Minami A, Meguro Y, Ishibashi S, Ishii A, Shiratori M, Sai S, Horii Y, Shimizu H, Fukumoto H, Shimba S, Taguchi R, Takahashi T, Otsubo T, Ikeda K, and Suzuki T
- Subjects
- Animals, Brain-Derived Neurotrophic Factor metabolism, Female, Male, N-Acetylneuraminic Acid metabolism, Rats, Rats, Wistar, Receptors, N-Methyl-D-Aspartate metabolism, CA3 Region, Hippocampal enzymology, Memory physiology, Neuraminidase metabolism, Pyramidal Cells enzymology, Synaptic Transmission physiology
- Abstract
Sialidase cleaves sialic acids on the extracellular cell surface as well as inside the cell and is necessary for normal long-term potentiation (LTP) at mossy fiber-CA3 pyramidal cell synapses and for hippocampus-dependent spatial memory. Here, we investigated in detail the role of sialidase in memory processing. Sialidase activity measured with 4-methylumbelliferyl-α-d- N -acetylneuraminic acid (4MU-Neu5Ac) or 5-bromo-4-chloroindol-3-yl-α-d- N -acetylneuraminic acid (X-Neu5Ac) and Fast Red Violet LB was increased by high-K
+ -induced membrane depolarization. Sialidase activity was also increased by chemical LTP induction with forskolin and activation of BDNF signaling, non-NMDA receptors, or NMDA receptors. The increase in sialidase activity with neural excitation appears to be caused not by secreted sialidase or by an increase in sialidase expression but by a change in the subcellular localization of sialidase. Astrocytes as well as neurons are also involved in the neural activity-dependent increase in sialidase activity. Sialidase activity visualized with a benzothiazolylphenol-based sialic acid derivative (BTP3-Neu5Ac), a highly sensitive histochemical imaging probe for sialidase activity, at the CA3 stratum lucidum of rat acute hippocampal slices was immediately increased in response to LTP-inducible high-frequency stimulation on a time scale of seconds. To obtain direct evidence for sialic acid removal on the extracellular cell surface during neural excitation, the extracellular free sialic acid level in the hippocampus was monitored using in vivo microdialysis. The free sialic acid level was increased by high-K+ -induced membrane depolarization. Desialylation also occurred during hippocampus-dependent memory formation in a contextual fear-conditioning paradigm. Our results show that neural activity-dependent desialylation by sialidase may be involved in hippocampal memory processing., (© 2017 by The American Society for Biochemistry and Molecular Biology, Inc.)- Published
- 2017
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5. Notch1 competes with the amyloid precursor protein for gamma-secretase and down-regulates presenilin-1 gene expression.
- Author
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Lleó A, Berezovska O, Ramdya P, Fukumoto H, Raju S, Shah T, and Hyman BT
- Subjects
- Amyloid Precursor Protein Secretases, Animals, Aspartic Acid Endopeptidases, Binding, Competitive, Blotting, Western, Cell Line, Cell Line, Tumor, Enzyme-Linked Immunosorbent Assay, Feedback, Physiological, Humans, Luciferases metabolism, Membrane Proteins genetics, Mice, Plasmids metabolism, Presenilin-1, Protein Binding, Protein Structure, Tertiary, Receptor, Notch1, Receptors, Cell Surface genetics, Reverse Transcriptase Polymerase Chain Reaction, Signal Transduction, Transfection, beta-Galactosidase metabolism, Amyloid beta-Protein Precursor metabolism, Down-Regulation, Endopeptidases metabolism, Membrane Proteins biosynthesis, Receptors, Cell Surface metabolism, Transcription Factors
- Abstract
Presenilin 1 (PS1) is a critical component of the gamma-secretase complex, which is involved in the cleavage of several substrates including the amyloid precursor protein (APP) and Notch1. Based on the fact that APP and Notch are processed by the same gamma-secretase, we postulated that APP and Notch compete for the enzyme activity. In this report, we examined the interactions between APP, Notch, and PS1 using the direct gamma-secretase substrates, Notch 1 Delta extracellular domain (N1DeltaEC) and APP carboxyl-terminal fragment of 99 amino acids, and measured the effects on amyloid-beta protein production and Notch signaling, respectively. Additionally, we tested the hypothesis that downstream effects on PS1 expression may coexist with the competition phenomenon. We observed significant competition between Notch and APP for gamma-secretase activity; transfection with either of two direct substrates of gamma-secretase led to a reduction in the gamma-cleaved products, Notch intracellular domain or amyloid-beta protein. In addition, however, we found that activation of the Notch signaling pathway, by either N1 Delta EC or Notch intracellular domain, induced down-regulation of PS1 gene expression. This finding suggests that Notch activation directly engages gamma-secretase and subsequently leads to diminished PS1 expression, suggesting a complex set of feedback interactions following Notch activation.
- Published
- 2003
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6. Induction of the cholesterol transporter ABCA1 in central nervous system cells by liver X receptor agonists increases secreted Abeta levels.
- Author
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Fukumoto H, Deng A, Irizarry MC, Fitzgerald ML, and Rebeck GW
- Subjects
- ATP Binding Cassette Transporter 1, ATP-Binding Cassette Transporters metabolism, Animals, Base Sequence, Blotting, Western, Central Nervous System cytology, DNA Primers, DNA-Binding Proteins, In Situ Hybridization, Liver X Receptors, Mice, Orphan Nuclear Receptors, Rats, Subcellular Fractions metabolism, Tumor Cells, Cultured, ATP-Binding Cassette Transporters biosynthesis, Amyloid beta-Peptides metabolism, Central Nervous System metabolism, Cholesterol metabolism, Receptors, Cytoplasmic and Nuclear metabolism
- Abstract
The expression, function, and regulation of the cholesterol efflux molecule, ABCA1, has been extensively examined in peripheral tissues but only poorly studied in the brain. Brain cholesterol metabolism is of interest because several lines of evidence suggest that elevated cholesterol increases the risk of Alzheimer's disease. We found a largely neuronal expression of ABCA1 in normal rat brain by in situ hybridization. ABCA1 message was dramatically up-regulated in neurons and glia in areas of damage by hippocampal AMPA lesion after 3-7 days. Immunoblot analysis demonstrated ABCA1 protein in cultured neuronal and glial cells, and expression was induced by ligands of the nuclear hormone receptors of the retinoid X receptor and liver X receptor family. ABCA1 was induced by treatment with retinoic acid and several oxysterols, including 22(R)-hydroxycholesterol and 24-hydroxycholesterol. Expression of an ABCA1-green fluorescent protein construct in neuroblastoma cells demonstrated fluorescence in perinuclear compartments and on the plasma membrane. Because the Abeta peptide is important in Alzheimer's disease pathogenesis, we examined whether ABCA1 induction altered Abeta levels. Treatment of neuroblastoma cells with retinoic acid and 22(R)-hydroxycholesterol caused significant increases in secreted Abeta40 (29%) and Abeta42 (65%). Treatment with a nonsteroidal liver X receptor ligand, TO-901317, similarly increased levels of secreted Abeta40 (25%) and Abeta42 (126%). The increase in secreted Abeta levels was reduced by RNAi blocking of ABCA1 expression. These data suggest that the cholesterol efflux molecule ABCA1 may also be involved in the secretion of the membrane-associated molecule, Abeta.
- Published
- 2002
- Full Text
- View/download PDF
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