Evidence that N-acetylation regulates the behavioral activity of alpha-MSH in the rat and human central nervous system.

Abstract:

:alpha-MSH immunoreactive peptides were fractionated and characterized in rat and human brain and rat pituitary by reversed phase high pressure liquid chromatographic techniques. alpha-MSH and deacetylated alpha-MSH were two major naturally existing peptides in both brain and pituitary gland. Subsequent experiments examined the roles of these two peptides in neuronal function. The alpha-MSH was clearly more effective than deacetylated alpha-MSH in improving performance on a visual discrimination task after intraperitoneal administration and in inducing excessive grooming after intraventricular administration. The difference in behavioral potency may be explained by the fact that alpha-MSH was much more resistant to peptidase degradation than was deacetylated alpha-MSH. N-acetylation of alpha-MSH may be an effective regulatory process for modulating the behavioral potency of the secretory product of alpha-MSH-containing pituitary cells and neurons.

journal_name

Peptides

journal_title

Peptides

authors

O'Donohue TL,Handelmann GE,Chaconas T,Miller RL,Jacobowitz DM

doi

10.1016/s0196-9781(81)80126-x

subject

Has Abstract

pub_date

1981-10-01 00:00:00

pages

333-44

issue

3

eissn

0196-9781

issn

1873-5169

pii

S0196-9781(81)80126-X

journal_volume

2

pub_type

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