[Discovery, anatomical mapping and biosynthesis of various families of endogenous opioid peptides].
[Discovery, anatomical mapping and biosynthesis of various families of endogenous opioid peptides].
复制标题
[内源性阿片肽各家族的发现、解剖图谱和生物合成]。
DOI:
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发表时间:
1986
期刊:
影响因子:
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通讯作者:
J. Rossier
中科院分区:
文献类型:
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作者:
G. Patey;J. Rossier
The endogenous opioid peptides all contain the enkephalin sequence Tyr-Gly-Gly-Phe (-Met/-Leu at their amino-terminus. Three distinct families of these peptides (beta-endorphins, enkephalins and dynorphins) are present in different neuronal pathways within the central nervous system. Molecular genetics have shown that these three families of opioid peptides are derived from three distinct precursors. Pro-opiomelanocortin gives rise to the endorphins, as well as adrenocorticotropic hormone (ACTH) and the melanotropic hormones (MSH's). Met-enkephalin, Leu-enkephalin and the related heptapeptide Met-enkephalin-Arg6-Phe7 and octapeptide Met-enkephalin-Arg6-Gly7-Leu8 are derived from proenkephalin. The third family is derived from prodynorphin and includes dynorphin A, dynorphin B (also known as rimorphin) and alpha- and beta-neo-endorphin. The structures of the genes coding for these precursors are similar, suggesting the possibility of one common ancestral gene. At the present time the main question concerns the physiological significance of such a great diversity of endogenous opioid peptides.