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Calcium sites in MSH stimulation of xenopus melanophores: studies with photoreactive alpha-MSH.

Abstract：

:Photo-affinity labelling of MSH receptors on tail-fin melanophores of Xenopus tadpoles with p-azidophenylalanine 13-alpha-MSH (Pap13)-alpha-MSH) or p-azidophenylacetyl-serine1-alpha-MSH ([Apac-Ser1]-alpha-MSH) resulted in a long-lasting stimulation of the melanophores which cannot be reversed despite continuous washing. The generation of this irreversible response is inhibited when photo-affinity labelling is performed in a Ca2+-free medium or in the presence of Ca2+ antagonists. The irreversible stimulation produced in normal medium is completely reversed upon removal of Ca2+ , but is not affected by Ca2+ antagonists or melatonin. Re-addition of Ca2+ after temporary removal restores to irreversible stimulation, even in the presence of Ca2+ antagonists or melatonin. This proves that covalent alpha-MSH-receptor complexes remain fully functional despite temporary deprivation of ca2+. Racemized alpha-MSH, which binds 'tightly' to the receptor and produces a long-lasting effect, is removed from the receptor in Ca2+-free medium, but not by Ca2+ antagonists or melatonin. These results confirm earlier results showing that at least 2 Ca2+ sites are involved in alpha-MSH action, one associated with MSH-receptor binding and the other with the subsequent generation of the effect. The dual role of Ca2+ is not the result of EGTA present; it is specific (Mg2+ has no effect) and is identical for the two different photoreactive alpha-MSH derivatives.

journal_name

Mol Cell Endocrinol

journal_title

Molecular and cellular endocrinology

authors

de Graan PN,Eberle AN,van de Veerdonk FC

doi

10.1016/0303-7207(82)90121-6

subject

Has Abstract

pub_date

1982-05-01 00:00:00

pages

327-9

issue

3

eissn

0303-7207

issn

1872-8057

journal_volume

26

pub_type

杂志文章

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