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Endocytosis of the lutropin receptor is mediated by a low affinity binding site.

Abstract：

:Porcine Leydig cells in primary culture were incubated to equilibrium with increasing doses of either porcine luteinizing hormone (pLH) or human chorionic gonadotropin (hCG). Then, free and total high affinity gonadotropin receptors on the cell surface were dosed with [125I]hCG as tracer. In isotonic high salt medium, the pLH concentration for half receptor occupancy (Kocc) and for half receptor endocytosis (Kendo) were nearly indistinguishable (1-3 x 10(-7) M). But, when the medium was changed to an isotonic low salt buffer, Kocc shifted to 1.2 x 10(-9) M and Kendo to 1.5 x 10(-8) M. However, with hCG, both values were largely independent of the ionic strength (Kocc = 10(-10) M and Kendo = 10(-8) M). The fact that Kendo is higher than Kocc suggests that the endocytosis of the high affinity gonadotropin receptor is controlled by the hormone binding to another lower affinity site.

journal_name

Mol Cell Endocrinol

journal_title

Molecular and cellular endocrinology

authors

Genty N,Salesse R,Jallal B,Garnier J

doi

10.1016/0303-7207(91)90263-r

subject

Has Abstract

pub_date

1991-04-01 00:00:00

pages

89-94

issue

1-3

eissn

0303-7207

issn

1872-8057

pii

0303-7207(91)90263-R

journal_volume

76

pub_type

杂志文章

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