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
Peptidesjournal_title
Peptidesauthors
Balm PH,Hovens ML,Wendelaar Bonga SEdoi
10.1016/0196-9781(94)00204-jsubject
Has Abstractpub_date
1995-01-01 00:00:00pages
463-9issue
3eissn
0196-9781issn
1873-5169pii
0196-9781(94)00204-Jjournal_volume
16pub_type
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