Isolation and structure of a C-terminally amidated nonopioid peptide, amidorphin-(8-26), from bovine striatum: a major product of proenkephalin in brain but not in adrenal medulla.
Isolation and structure of a C-terminally amidated nonopioid peptide, amidorphin-(8-26), from bovine striatum: a major product of proenkephalin in brain but not in adrenal medulla.
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来自牛纹状体的 C 末端酰胺化非阿片肽，amidophin-(8-26) 的分离和结构：脑啡肽原在大脑中的主要产物，但在肾上腺髓质中则不然。
DOI：
10.1073/pnas.83.6.1936
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发表时间：
1986
影响因子：
11.1
通讯作者：
Seizinger,BR
中科院分区：
文献类型：
--
作者：
Liebisch,DC;Weber,E;Kosicka,B;Gramsch,C;Herz,A;Seizinger,BR
我们已经从牛纹状体中分离出一个C-末端酰胺化肽并进行了序列测定。通过吸附至XAD-2树脂和四个不同的HPLC步骤将肽纯化至均一。氨基酸组成分析和气相序列分析表明，这种肽与前脑啡肽衍生的阿片肽amidorphin，我们最近从牛肾上腺髓质分离的残基8-26的身份。通过其对羧肽酶A消化的稳定性和放射免疫测定中的完全交叉反应性（需要C-末端酰胺基团作为识别位点的一部分）证明了牛纹状体中amidorphin-（8-26）的C-末端酰胺化。非阿片肽amidorphin-（8-26）缺乏amidorphin的N-末端[Met]脑啡肽序列，是阿片肽前体脑啡肽原在脑中的主要产物。然而，在肾上腺髓质中，由于氨基吗啡浓度非常高，因此无法检测到氨基吗啡-（8-26）。这表明脑啡肽原在不同组织中的翻译后加工存在差异。在大脑中，与肾上腺髓质相反，在两个碱性残基的典型裂解信号下，amidorphin被进一步加工，产生非阿片肽amidorphin-（8-26），并可能产生阿片肽[Met]脑啡肽。因此，脑中的前脑啡肽可能被认为是阿片肽与可能具有不同生物学功能的非阿片肽连接的前体。
We have isolated and sequenced a C-terminally amidated peptide from bovine striatum. The peptide was purified to homogeneity by adsorption to XAD-2 resins and four different HPLC steps. Amino acid composition analysis and gas-phase sequence analysis revealed identity of this peptide with residues 8-26 of the proenkephalin-derived opioid peptide amidorphin, which we have recently isolated from bovine adrenal medulla. C-terminal amidation of amidorphin-(8-26) from bovine striatum was demonstrated by its stability to carboxypeptidase A digestion and full crossreactivity in a radioimmunoassay that required the C-terminal amide group as part of the recognition site. The nonopioid peptide amidorphin-(8-26), which lacks the N-terminal [Met]enkephalin sequence of amidorphin, is a major product of the opioid peptide precursor proenkephalin in the brain. In the adrenal medulla, however, where amidorphin occurs in remarkably high concentrations, amidorphin-(8-26) could not be detected. This is indicative of differential post-translational processing of proenkephalin in different tissues. In the brain, as opposed to the adrenal medulla, amidorphin is further processed at the typical cleavage signals of two basic residues, giving rise to the nonopioid peptide amidorphin-(8-26) and, possibly, to the opioid peptide [Met]enkephalin. Thus, proenkephalin in the brain might be considered as a precursor in which an opioid peptide is linked with a nonopioid peptide of possibly different biological function.