Identification of endothelin receptors in cultured cerebellar neurons.

Abstract:

:We have described the binding of [125I]endothelin-1 (ET-1) to cultured rat cerebellar granule cells. Binding of [125I]ET-1 was specific, saturable, and time-dependent. Scatchard analysis of saturation binding data indicated a single class of high affinity binding site with a KD of 95 pM, and a Bmax of 8110 receptors/cell. Functionally, the binding of ET-1 stimulated phosphatidylinositide (PI) hydrolysis in a dose- and time-dependent fashion. PI turnover was found to be inhibitable by 1 microM phorbol dibutyrate but not by 1 microgram/ml pertussis toxin, suggesting that the ET-1-mediated response is regulated by protein kinase C and a pertussis toxin-insensitive guanine nucleotide (GTP) binding protein.

journal_name

Neuropeptides

journal_title

Neuropeptides

authors

Lysko PG,Feuerstein G,Pullen M,Wu HL,Nambi P

doi

10.1016/0143-4179(91)90005-4

subject

Has Abstract

pub_date

1991-02-01 00:00:00

pages

83-6

issue

2

eissn

0143-4179

issn

1532-2785

pii

0143-4179(91)90005-4

journal_volume

18

pub_type

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