Rm. Dores et al., DECIPHERING POSTTRANSLATIONAL PROCESSING EVENTS IN THE PITUITARY OF ANEOPTERYGIAN FISH - CLONING OF A GAR PROOPIOMELANOCORTIN CDNA, General and comparative endocrinology, 107(3), 1997, pp. 401-413
A cDNA that codes for the polypeptide hormone precursor proopiomelanoc
ortin (POMC) was cloned and sequenced from a gar (Lepisosteus osseus)
pituitary cDNA library. The gar POMC cDNA is 1237 bp and contains a 78
0-bp open reading frame. The deduced amino acid sequence for gar POMC
is 259 amino acids in length. The general organization of gar POMC is
very similar to that of other gnathostome POMC sequences. The beta-end
orphin sequence had 91% sequence identity with sockeye A beta-endorphi
n and 71% sequence identity with Xenopus laevis beta-endorphin. Three
melanocyte-stimulating hormone (MSH) core sequences [HFR(W)] were dete
cted. The gar alpha-MSH sequence was identical to the alpha-MSH sequen
ce in rat POMC. The gar beta-MSH sequence had 77% sequence identity wi
th salmonid forms of beta-MSH and 53% sequence identity with tetrapod
forms of beta-MSH. The gamma-MSH region of gar POMC only had 26% prima
ry sequence identity with tetrapod gamma-MSH sequences. Car gamma-MSH
had an incomplete MSH core sequence (HRF), an apparent internal deleti
on of five amino acids, and lacked flanking paired basic amino acids e
ssential for proteolytic cleavage. The apparent degenerate nature of g
ar gamma-MSH is discussed in light of the absence of this sequence in
salmonid fish. (C) 1997 Academic Press.