Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1994-3-11
pubmed:abstractText
We have previously reported that hypophysial neurointermediate lobe peptides, di-acetylated alpha-melanocyte-stimulating hormone (di-ac-alpha-MSH) and N-acetylated beta-endorphin (N-ac-beta-END), can acutely increase the relative number of prolactin-secreting cells in anterior pituitary cell cultures from ovariectomized rats. Inasmuch as the des-acetylated forms of these peptides (des-ac-alpha-MSH and beta-END) were not effective in this regard, we concluded that acetylation was an absolute requirement for manifestation of the recruitment response. The aim of the present study was to determine whether these des-acetylated variants could antagonize the mammotrope-recruiting activity of their acetylated congeners. Treatment of anterior pituitary cell cultures with di-ac-alpha-MSH and N-ac-beta-END increased the relative amount of prolactin secretors above control values. Interestingly, des-acetylated variants of alpha-MSH and beta-END blocked the mammotrope-recruitment activity of their respective acetylated forms. In addition, beta-END antagonized the mammotrope-recruitment activity of di-ac-alpha-MSH while des-ac-alpha-MSH did not attenuate the stimulatory effect of N-ac-beta-END. Given that mammotropes maintained in vivo are exposed to all these peptides, it is possible that these acetylated and non-acetylated congeners may act in an opposing manner to regulate dynamic prolactin release.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0022-0795
pubmed:author
pubmed:issnType
Print
pubmed:volume
139
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
295-300
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Des-acetylated variants of alpha-melanocyte-stimulating hormone and beta-endorphin can antagonize the mammotrope-recruiting activity of their acetylated forms.
pubmed:affiliation
Department of Cell Biology and Anatomy, Medical University of South Carolina, Charleston 29425.
pubmed:publicationType
Journal Article