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H Aratake

Publications and source records attributed to H Aratake.

4 recordsLinked to original sources
PubMed1995

Differential expression of ARIA isoforms in the rat brain.

ARIA, heregulin, neu differentiation factor, and glial growth factor are members of a new family of growth and differentiation factors whose effects have been assayed on Schwann cells, skeletal muscle cells, and mammary tumor cell lines. To gain insight into their roles in the CNS, we studied the expression of ARIA in the rat brain. We found ARIA mRNA in all cholinergic neurons throughout the CNS, including motor neurons and cells of the medial septal nucleus and the nucleus basalis of Meynert. We also found that ARIA induces tyrosine phosphorylation of a 185 kDa protein in central and peripheral targets of these cholinergic neurons. ARIA mRNA, however, is not restricted to cholinergic neurons, suggesting that it may also play a role at other types of synapses. Its distribution in germinal layers of the telencephalon and cerebellum suggests that it may also play a role in the proliferation and/or migration of neuronal and glial precursor cells.

Animals↗
PubMed1995

A new compound (AZ36041) promotes the survival of the neurons and reduces neurotoxicity of Alzheimer's beta-amyloid protein.

Alzheimer's beta-amyloid protein (A beta) is the main component of senile plaques, which are characteristic hallmarks of the Alzheimer's disease brain. Recently, there have been several reports that A beta has toxic effects on both cultured neurons and in the brain. We confirmed the neurotoxicity of A beta in vitro and found a new compound, called AZ36041 (4-chloro-N-(5-nitro-2-tiazoyl)benzenesulfone amide), which dramatically reduced A beta neurotoxicity. This compound was also found to have a neuroprotective effect against toxicity of glutamate and enhanced neuronal survival in the absence of neurotoxic compounds. AZ36041 may be a useful tool for investigating the mechanism of A beta neurotoxicity in vitro and in vivo.

Amyloid beta-Peptides↗
PubMed1991

Trophic effect of beta-amyloid precursor protein on cerebral cortical neurons in culture.

We investigated the effect of human beta-amyloid precursor protein (APP) on rat primary cerebral cortical neurons cultured in a serum-free medium. Two secretory APP species (APP667 and APP592) with and without the protease inhibitor domain were produced by COS-1 cells transfected with APP cDNAs, which encode the N-terminal portions of APP770 and APP695. Both highly purified APP species, when added to the medium, enhanced neuronal survival and neurite extension in a dose-dependent manner with a maximum effect at approximately 100 nM. These results suggest that secreted forms of APP have trophic activity for cerebral cortical neurons.

Amyloid beta-Protein Precursor↗