Structure-activity studies of alpha-melanotropin fragments on cAMP production in striatal slices.

Abstract:

:In this work, we characterized the active site in the alpha-melanotropin hormone (alpha-MSH) sequence responsible for the enhancement of cAMP production in incubated striatal slices by using different alpha-MSH fragments. We also analyzed the effects of the co-incubation of the SCH23390, a dopaminergic D(1) antagonist, with the MSH fragments, to study the involvement of the D(1) receptor on this induction. A rise was observed in the levels of cAMP after addition of the 6 microM fragments MSH((1-10)), and 0.6 and 6 microM MSH((5-13)); however, the values were lower than those induced by 6 microM alpha-MSH. On the contrary, the addition of MSH((9-13)), MSH((7-11)), or MSH((6-9)) did not affect the cAMP content. The presence of 10 microM SCH23390 blocked the effect of the fragments on cAMP production. We conclude that the biologic activity of alpha-MSH, as observed through the levels of cAMP, declines when the length of its polypeptide chain is shortened, and that the presence of glutamic acid in the molecule, as well as the core sequence, are of importance for fragments' activity.

journal_name

Peptides

journal_title

Peptides

authors

Cecilia Cremer M,Silvina Sanchez M,Ester Celis M

doi

10.1016/s0196-9781(00)00211-4

subject

Has Abstract

pub_date

2000-06-01 00:00:00

pages

803-6

issue

6

eissn

0196-9781

issn

1873-5169

pii

S0196-9781(00)00211-4

journal_volume

21

pub_type

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