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
Peptidesjournal_title
Peptidesauthors
Cecilia Cremer M,Silvina Sanchez M,Ester Celis Mdoi
10.1016/s0196-9781(00)00211-4subject
Has Abstractpub_date
2000-06-01 00:00:00pages
803-6issue
6eissn
0196-9781issn
1873-5169pii
S0196-9781(00)00211-4journal_volume
21pub_type
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