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Hideo Ohta

Researcher at Okayama University

Publications -  44
Citations -  3633

Hideo Ohta is an academic researcher from Okayama University. The author has contributed to research in topics: Receptor & Lysophosphatidic acid. The author has an hindex of 25, co-authored 44 publications receiving 3527 citations. Previous affiliations of Hideo Ohta include Gunma University & Kindai University.

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Ki16425, a Subtype-Selective Antagonist for EDG-Family Lysophosphatidic Acid Receptors

TL;DR: Ki16425 selectively inhibits LPA receptor-mediated actions, especially through LPA1 and LPA3; therefore, it may be useful in evaluating the role of LPA and its receptor subtypes involved in biological actions.
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Lysophosphatidic acid and autotaxin stimulate cell motility of neoplastic and non-neoplastic cells through LPA1.

TL;DR: It is demonstrated that LPA and ATX mediate cell motility-stimulating activity through the LPA receptor, LPA1, and the present study suggests that ATX and L PA1 represent potential targets for cancer therapy.
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Sphingosine 1-phosphate stimulates proliferation and migration of human endothelial cells possibly through the lipid receptors, Edg-1 and Edg-3.

TL;DR: The results suggest that S1P might be a novel angiogenesis factor and that the lipid-induced proliferation and migration of endothelial cells are possibly mediated through cell-surface S 1P receptors, Edg-1 and EdG-3, which are linked to signalling pathways.
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Artificial induction of maturation and fertilization in the Japanese eel, Anguilla japonica

TL;DR: Repeated injections of salmon pituitary extract induced vitellogenesis in feminized, cultivated Japanese eels, and many fertilized eggs from cultivated eels are obtained using these techniques developed for female and male eels.
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Inhibition by islet-activating protein of a chemotactic peptide-induced early breakdown of inositol phospholipids and Ca2+ mobilization in guinea pig neutrophils.

TL;DR: The IAP substrate, probably the inhibitory guanine nucleotide-binding regulatory component of adenylate cyclase (Ni) or an analogous protein, is proposed to mediate fMet-Leu-Phe receptor-linked activation of the phospholipase C in guinea pig neutrophils.