Endorphin and MSH in concert form the corticotropic principle released by tilapia (Oreochromis mossambicus; Teleostei) melanotropes.

Abstract:

:HPLC characterization of tilapia pituitary endorphins using an antibody specific for N-terminally acetylated endorphins yielded three major peaks in the neurointermediate lobe, but none in the pars distalis. The melanotropes secreted two of the immunoreactive products in vitro, one of which coeluted with Xenopus laevis N-ac-beta-END(1-8). This immunoreactive fraction also coeluted with diacetyl-alpha-MSH. Evidence is presented that the noteworthy corticotropic potency of this HPLC fraction, previously attributed to diacetyl-alpha-MSH, results from END and MSH acting in a coordinated fashion. Confinement stress had no effect on plasma N-ac-beta-END immunoreactivity, but led to a decrease in plasma alpha-MSH levels. Therefore, it seems unlikely that the corticotropic action of the peptides regulates the elevation of cortisol production that takes place during confinement, but it may play a role during other forms of stress that are known to activate the melanotropes.

journal_name

Peptides

journal_title

Peptides

authors

Balm PH,Hovens ML,Wendelaar Bonga SE

doi

10.1016/0196-9781(94)00204-j

subject

Has Abstract

pub_date

1995-01-01 00:00:00

pages

463-9

issue

3

eissn

0196-9781

issn

1873-5169

pii

0196-9781(94)00204-J

journal_volume

16

pub_type

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