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Fumihiko Okada, MD
Health Administration Center Hokkaido University Sapporo, Japan

Takeshi Murakami, MD, PhD; Yukiko Tokumitsu, PhD
Sapporo

Arch Gen Psychiatry. 1995;52(4):319.

	Since this article does not have an abstract, we have provided the first 150 words of the full text PDF and any section headings.

The family of guanosine triphosphate—binding proteins (G proteins) plays a key role in the transmembrane signaling pathway in a variety of cells: Gs and Gi stimulate and inhibit adenylate cyclase, respectively; Gp activates polyphosphoinositide phosphodiesterase; Gk activates K⁺ channels; and Go inhibits the voltage-dependent Ca²⁺ channel.¹ Recently, Hepler and Gilman² reviewed further advances of G protein research; they described how the task of unraveling the complexity of the G protein—regulated cellular switchboard expands exponentially as the number of identified G protein subunits continues to grow.

Measurements of the level of Gi/Go in the schizophrenic brain utilizing pertussis toxin (islet-activating protein)-catalyzed adenosine diphosphate (ADP) ribosylation showed that the amount of Gi/Go was significantly decreased in the putamen³ and hippocampus⁴ of the left hemisphere in schizophrenic patients compared with controls. Unfortunately, these experiments with isletactivating protein could not distinguish multiple species of subunits of pertussis toxin—sensitive G . . . [Full Text PDF of this Article]

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