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Endorphin and MSH in concert form the corticotropic principle released by tilapia (Oreochromis mossambicus; Teleostei) melanotropes.
- Source :
-
Peptides [Peptides] 1995; Vol. 16 (3), pp. 463-9. - Publication Year :
- 1995
-
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.
- Subjects :
- Acetylation
Animals
Biological Assay
Chromatography, High Pressure Liquid
Endorphins metabolism
Female
Radioimmunoassay
Restraint, Physical
beta-Endorphin analogs & derivatives
beta-Endorphin analysis
Endorphins physiology
Melanocyte-Stimulating Hormones metabolism
Pituitary Gland metabolism
Tilapia metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0196-9781
- Volume :
- 16
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Peptides
- Publication Type :
- Academic Journal
- Accession number :
- 7651900
- Full Text :
- https://doi.org/10.1016/0196-9781(94)00204-j