Nucleotide sequence of cloned cDNA for bovine corticotropin-β-lipotropin precursor

Abstract

The nucleotide sequence of a 1,091-base pair cloned cDNA insert encoding bovine corticotropin-beta-lipotropin precursor mRNA is reported. The corresponding amino acid sequence indicates that the precursor protein consists of repetitive units and includes a third melanotropin sequence in its cryptic portion. Pairs of lysine and arginine residues separate the component peptides of the precursor.

Lys-gamma3-MSH: A global regulator of hormone sensitive lipase activity?

“…The cloning of the gene for POMC in 1979 (Nakanishi et al, 1979) revealed, not only that these two MSH peptides were derived from the same precursor, but that the POMC sequence also encoded a third MSH-like peptide. This peptide was named gamma-MSH (γ-MSH) and is located in the amino terminal of the molecule known as the 16KDa fragment (subsequently also known as pro-γ-MSH).…”

Specific binding of 125I-salmon calcitonin to rat brain: Regional variation and calcitonin specificity.

“…Very recently, calcitonin-like immunoactivity has been detected in the cells of the anterior and intermediate lobes of the rat pituitary gland (27,28), implying "ectopic" production of calcitonin not only by transformed cells but also by non-tranformed cells. In addition, the findings of Nakanishi et al (29) on ACTH-(3-LPH precursor of bovine pituitary provide clear evidence for the production of the hormone by the pituitary and other tissues including brain. Despite their conclusion that the precursor does not contain any other biologically active sequences other than those of ACTH, MSHs and opioid peptides, it should be pointed out that in the N terminal half of the precursor, there is a 32 amino-acid sequence corresponding to a skeletal structure which is basic to that of calcitonins.…”

A novel N‐terminal fragment of pro‐γ‐melanotropin, not containing γ‐melanotropin and generated from a cleavage site lacking the traditional two basic residues

“…Identification of tryptophan as the only N-terminal residue, the composition (below), and the results of amino acid sequence analysis (below) further show the purity. The amino acid composition, given in table 1, fits residues I-30 of the pro-y-MSH molecule [ 1,4] and suggests that the peptide constitutes that fragment.…”

“…Proteolytic processing of this precursor generates several biologically active peptides with corticotropic, lipolytic or melanotropic activity [2,3]. The N-terminal part of the precursor molecule (pro-y-MSH), remaining after the cleavages that remove ACTH and /3-LPH, consists of 103 amino acid residues [1,4] and contains the y-MSH sequence.…”