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Journal of Neuroscience, Vol 6, 837-849, Copyright © 1986 by Society for Neuroscience
Characterization of pro-ACTH/endorphin-derived peptides in rat hypothalamus
RB Emeson and BA Eipper
The proteolytic processing pattern of pro-ACTH/endorphin in rat
hypothalamus is similar to the pattern in the pars intermedia; peptides the
size of beta-endorphin, gamma-lipotropin (gamma-LPH), corticotropin- like
intermediate lobe peptide (CLIP), alpha-melanotropin (gamma-MSH), joining
peptide, and glycosylated gamma 3-MSH all represent predominant end
products. Equimolar amounts of beta-endorphin-, alpha-MSH-, CLIP-,
gamma-LPH-, and joining peptide-related immunoreactivity are found in
hypothalamic extracts (approximately 3 pmol per hypothalamus). Although the
proteolytic processing pattern in the hypothalamus is similar to that in
the pars intermedia, a tissue-specific posttranslational processing pattern
was detected. Ion-exchange analysis of beta- endorphin-sized immunoreactive
material from hypothalamic extracts resolves three major forms,
corresponding to beta-endorphin(1-31), beta- endorphin(1-27), and
beta-endorphin(1-26). The alpha-N-acetylated forms of endorphin represent
less than 10% of the total beta-endorphin immunoreactivity. Analyses of
hypothalamic alpha-MSH-sized molecules with acetyl- and amide-directed
alpha-MSH antisera suggest that hypothalamic alpha-MSH is fully amidated,
but largely not alpha-N- acetylated. Fractionation by reverse-phase
high-performance liquid chromatography (HPLC) confirms that greater than
85% of the alpha-MSH immunoreactivity corresponds to ACTH(1-13)NH2 or its
sulfoxide, and less than 10% corresponds to alpha-MSH
[alpha-N-acetyl-ACTH(1-13)NH2] or its sulfoxide. Isoelectric focusing
demonstrates that 83-93% of hypothalamic CLIP is phosphorylated.
Isoelectric focusing suggests that the majority of the hypothalamic
gamma-LPH-sized immunoreactive material is indistinguishable from gamma-LPH
synthesized by pituitary melanotropes. The minor extent of
alpha-N-acetylation of alpha-MSH and beta-endorphin, the limited
carboxyl-terminal proteolysis of beta- endorphin, and the extensive
phosphorylation of CLIP represent major differences between the
posttranslational processing patterns of pro- ACTH/endorphin in the
hypothalamus and pars intermedia.
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