Lipotropin: Precursor to two biologically active peptides

Lipotropin appears to be the common precursor to β-MSH, a peptide with lipolytic activity, and C-Fragment, a peptide with potent opiate activity. The product formed is determined by the specificity of the activating enzymes. The amino acid sequence of β-MSH, the 18 residue melanocyte stimulating hor...

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Veröffentlicht in:Biochemical and biophysical research communications 1976-04, Vol.69 (4), p.950-956
Hauptverfasser: Bradbury, A.F., Smyth, D.G., Snell, C.R.
Format: Artikel
Sprache:eng
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Zusammenfassung:Lipotropin appears to be the common precursor to β-MSH, a peptide with lipolytic activity, and C-Fragment, a peptide with potent opiate activity. The product formed is determined by the specificity of the activating enzymes. The amino acid sequence of β-MSH, the 18 residue melanocyte stimulating hormone, is contained within the central region of lipotropin (LPH), a 91 residue polypeptide. On this basis Li and his colleagues 1 suggested that LPH might be the prohormone of β-MSH. Bertagna, Lis and Gilardeau 2, on the other hand, were unable to demonstrate conversion of LPH to β-MSH in vitro using pulse labelling techniques. If LPH is the precursor of β-MSH, formation of the hormone should be accompanied by release of the contiguous fragments of the prohormone and the fragments remain in the secretory particle of the gland. To obtain evidence on the biosynthetic origin of β-MSH, we have isolated peptides from pituitary in a search for the N- and C-fragments of the prohormone.
ISSN:0006-291X
1090-2104
DOI:10.1016/0006-291X(76)90465-4