Search Results - (Author, Cooperation:Y. Goshima)
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1Cartilage acidic protein-1B (LOTUS), an endogenous Nogo receptor antagonist for axon tract formationY. Sato ; M. Iketani ; Y. Kurihara ; M. Yamaguchi ; N. Yamashita ; F. Nakamura ; Y. Arie ; T. Kawasaki ; T. Hirata ; T. Abe ; H. Kiyonari ; S. M. Strittmatter ; Y. Goshima ; K. Takei
American Association for the Advancement of Science (AAAS)
Published 2011Staff ViewPublication Date: 2011-08-06Publisher: American Association for the Advancement of Science (AAAS)Print ISSN: 0036-8075Electronic ISSN: 1095-9203Topics: BiologyChemistry and PharmacologyComputer ScienceMedicineNatural Sciences in GeneralPhysicsKeywords: Animals ; Axons/*physiology ; Binding Sites ; Calcium-Binding Proteins/chemistry/genetics/*metabolism ; Cell Line ; Cells, Cultured ; GPI-Linked Proteins/genetics/metabolism ; Growth Cones/metabolism ; Humans ; Immunohistochemistry ; Ligands ; Mice ; Mice, Inbred ICR ; Myelin Proteins/genetics/*metabolism ; Olfactory Pathways/*cytology/*growth & development/metabolism ; Prosencephalon/embryology/metabolism ; Protein Binding ; Receptors, Cell Surface/genetics/*metabolism ; Signal TransductionPublished by: -
2Abe, H., Jitsuki, S., Nakajima, W., Murata, Y., Jitsuki-Takahashi, A., Katsuno, Y., Tada, H., Sano, A., Suyama, K., Mochizuki, N., Komori, T., Masuyama, H., Okuda, T., Goshima, Y., Higo, N., Takahashi, T.
American Association for the Advancement of Science (AAAS)
Published 2018Staff ViewPublication Date: 2018-04-06Publisher: American Association for the Advancement of Science (AAAS)Print ISSN: 0036-8075Electronic ISSN: 1095-9203Topics: BiologyChemistry and PharmacologyGeosciencesComputer ScienceMedicineNatural Sciences in GeneralPhysicsKeywords: Medicine, Diseases, NeurosciencePublished by: -
3Nakamura, S. ; Goshima, Y. ; Yue, J. L. ; Misu, Y.
Oxford, UK : Blackwell Publishing Ltd
Published 1992Staff ViewISSN: 1471-4159Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: MedicineNotes: Abstract: Using microdialysis and HPLC, characteristics of the release of endogenous 3,4-dihydroxyphenylalanine (DOPA) from striatum in conscious rats were studied in comparison with those of 3,4-dihydroxyphenylethylamine (dopamine; DA). Purified l-aromatic amino acid decarboxylase (AADC) converted a putative peak of DOPA to DA. The retention time of DOPA differed from that of DA and major metabolites of DA and norepinephrine. The DOPA peak of dialysates comigrated with that of authentic DOPA when the pH of the HPLC buffer was modified. The ratio of the basal release of DOPA:DA was 1:2. 3-Hydroxybenzyl-hydrazine (NSD-1015; 100 mg/kg, i.p.), an AADC inhibitor, markedly increased the basal release of DOPA but produced no effect on DA. The basal release of DOPA was markedly decreased by α-methyl-p-tyrosine (200 mg/kg, i.p.), substantially tetrodotoxin (1 μM) sensitive, and Ca2+ (removal plus 12.5 mM Mg2+ addition) dependent. Fifty millimolar K+ released DOPA and this release was also Ca2+ dependent. These characteristics of the basal and evoked release of DOPA were similar to those of DA. The ratio of the evoked release of DOPA:DA was 1:3. These results indicate that DOPA is released under physiological conditions and by K+-induced depolarization in a manner similar to that for transmitter DA from striatum in freely moving rats.Type of Medium: Electronic ResourceURL: -
4Staff View
ISSN: 1471-4159Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: MedicineNotes: Abstract: Biphasic electrical field stimulation (0.5–5 Hz, 2 ms, 25 V, 3 min) and high K+ (10–30 mM, 5 min) released endogenous 3,4-dihydroxyphenylalanine (DOPA) from superfused rat striatal slices. Characteristics of the DOPA release were compared with those of 3,4-dihydroxyphenylethylamine (dopamine, DA). Electrical stimulation at 2 Hz evoked DOPA and DA over similar time courses, α-Methyl-p-tyrosine (0.2 mM) markedly reduced release of DOPA but not of DA. Maximal release (0.3 pmol) of DOPA was obtained at 2 Hz and at 15 mM K+. The impulse-evoked release of DOPA and DA was completely tetrodotoxin (0.3 μM) sensitive and Ca2+ dependent and the 15 mM K+-evoked release was also Ca2+ dependent. On l-[3,5-3H]tyrosine (1 μM) superfusion, high K+ (15 and 60 mM) released DOPA and DA together with concentration-dependent decreases in tyrosine 3-monooxygenase (EC 1.14.16.2) activity as indicated by [3H]H2O formation, followed by concentration-dependent increases after DOPA and DA release ended. These findings suggest that striatal DOPA is released by a Ca2+-dependent excitation-secretion coupling process similar to that involved in transmitter release.Type of Medium: Electronic ResourceURL: