It was admitted that human
beta-MSH was responsible for the hyper-pigmentation observed in some syndromes associated with
ACTH hypersecretion.
beta-LPH was a pituitary
polypeptide, containing the entire sequence of
beta-MSH in its fragment 37-58, and the physiological role of which remained unknown.
alpha-MSH and
CLIP (
Corticotrophin-like Intermediary
Peptide) were thought to be specific of certain species possessing a distinct pituitary pars intermedia. Recent data give new insight upon some of these conceptions.
beta-MSH seems not to exist in man; it is almost established now that plasma "Immunoreactive
beta-MSH" (IR-
beta-MSH) is in fact beta- and/or
gamma-LPH. In
chronic renal failure plasma IR-
beta-MSH is elevated because of a decreased plasma disappearance rate, whereas
ACTH is normal. Good evidence suggests that both LPH and
ACTH are synthesized in the same pituitary cell within a common polypeptidic precursor. Endogenous
peptides with morphinomimetic activity (
Endorphins) have been isolated from brain and hypophysis; they are all made up of different fractions of
beta-LPH-C-terminal fragment 61-91; It is likely that they represent a new class of brain
neurotransmitters involved in some functions of the central nervous system, structural similarities suggest that
beta-LPH may be the biosynthetic precursor of
Endorphins, however such a hypothesis remains to be clearly demonstrated.