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首页> 外文期刊>European Journal of Cell Biology: Journal of Deutsche Gesellschaft fur Elektronenmikroskopie: Journal of Deutsche Gesellschaft fur Zellbiologie >Post-translational amino acid racemization in the frog skin peptide deltorphin I in the secretion granules of cutaneous serous glands
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Post-translational amino acid racemization in the frog skin peptide deltorphin I in the secretion granules of cutaneous serous glands

机译：皮肤浆液腺分泌颗粒中蛙皮肽deltorphin I的翻译后氨基酸外消旋作用

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摘要

The dermal glands of the South American hylid frog Phyllomedusa bicolor synthesize and expel huge amounts of cationic, alpha-helical, 24- to 33-residue antimicrobial peptides, the dermaseptins B. These glands also produce a wide array of peptides that are similar to mammalian hormones and neuropeptides, including a heptapeptide opioid containing a D-amino acid, deltorphin I (Tyr-DAla-Phe-Asp-Val-Val-Gly NH2). Its biological activity is due to the racemization of L-Ala2 to D-Ala. The dermaseptins B and deltorphins are all derived from a single family of precursor polypeptides that have an N-terminal preprosequence that is remarkably well conserved, although the progenitor sequences giving rise to mature opioid or antimicrobial peptides are markedly different. Monoclonal and polyclonal antibodies were used to examine the cellular and ultrastructural distributions of deltorphin I and dermaseptin B in the serous glands by immunofluoresence confocal microscopy and immunogold-electron microscopy. Preprodeltorphin I and preprodermaseptins B are sorted into the regulated pathway of secretion, where they are processed to give the mature products. Deltorphin I, [l-Ala2]-deltorphin I and dermaseptin B are all stored together in secretion granules which accumulate in the cytoplasm of all serous glands. We conclude that the L- to D-amino acid isomerization of the deltorphin I occurs in the secretory granules as a post-translational event. Thus the specificity of isomerization depends on the presence of structural and/or conformational determinants in the peptide N-terminus surrounding the isomerization site.
机译：南美脂蛙Phyllomedusa bicolor的真皮腺体合成并排出了大量的阳离子，α-螺旋，24至33个残基的抗菌肽，即dermaseptinsB。这些腺体还产生多种类似于哺乳动物的肽激素和神经肽，包括含有D-氨基酸的七肽类阿片，deltorphin I（Tyr-DAla-Phe-Asp-Val-Val-Gly NH2）。其生物学活性归因于L-Ala2外消旋化为D-Ala。尽管产生成熟阿片样物质或抗微生物肽的祖先序列明显不同，但皮肤肽素B和deltorphins均衍生自具有显着良好保守性的N末端前序的单个前体多肽家族。单克隆和多克隆抗体被用于通过免疫荧光共聚焦显微镜和免疫金电子显微镜检查浆液性腺中的deltorphin I和dermaseptin B的细胞和超微结构分布。将前原卟啉I和前原皮肤抑素B分类到调节的分泌途径中，在其中进行加工以得到成熟的产物。 Deltorphin I，[1-Ala2] -deltorphin I和dermaseptin B一起储存在分泌颗粒中，这些颗粒在所有浆液腺的细胞质中积累。我们得出结论，deltorphin I的L-至D-氨基酸异构化发生在分泌颗粒中，作为翻译后事件。因此，异构化的特异性取决于在异构化位点周围的肽N-末端中结构和/或构象决定簇的存在。

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