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关于髓磷脂蛋白P0、髓鞘碱性蛋白（MBP）和P2在外周神经主致密线形成中的协同作用。

On the synergy between myelin proteins P0, MBP, and P2 in peripheral nerve major dense line formation.

作者信息

Krokengen Oda C, Raasakka Arne, Klenow Martin Berg, Pal Antara, Hetland Øystein, Mularski Anna, Ruskamo Salla, Pedersen Jan Skov, Simonsen Adam Cohen, Kursula Petri

机构信息

Department of Biomedicine, University of Bergen, Norway.

Department of Physics, Chemistry and Pharmacy, University of Southern Denmark, Odense, Denmark.

出版信息

FEBS J. 2025 Aug;292(15):3960-3985. doi: 10.1111/febs.70111. Epub 2025 Apr 29.

DOI:10.1111/febs.70111
PMID:40299727
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC12326912/
Abstract

The proper formation and function of the myelin sheath, a proteolipid membrane multilayer, relies on the coordinated action of several key myelin proteins. We studied how proteins from the peripheral myelin cytoplasmic apposition-myelin basic protein (MBP), the cytoplasmic tail of myelin protein zero (P0ct), and peripheral myelin protein 2 (P2)-interact with each other and with myelin-like membranes using various techniques, such as small-angle X-ray diffraction, differential scanning calorimetry (DSC), surface plasmon resonance (SPR), and electron and live epifluorescence microscopy. DSC revealed changes in lipid interactions depending on the protein combination, with altered membrane fluidity and stability. These results were supported by SPR, which indicated that the myelin proteins may compete for membrane surface binding. Analysis of the Bragg peaks induced by the myelin proteins in lipidic environments showed both lamellar and nonlamellar phases in protein-lipid complexes, indicating the formation of nanoscale structures that may be relevant for myelin assembly. Microscopy experiments showed the formation of new membrane structures with each of the proteins separately and together. Our data indicate both synergy and competition between the three main proteins residing in the peripheral nervous system myelin major dense line. The observed direct effects of myelin proteins on lipid membrane structure and properties may be relevant to their function in myelinating cells as well as their role in myelin disorders.

摘要

髓鞘是一种蛋白脂质膜多层结构，其正常形成和功能依赖于几种关键髓鞘蛋白的协同作用。我们使用多种技术，如小角X射线衍射、差示扫描量热法（DSC）、表面等离子体共振（SPR）以及电子显微镜和实时落射荧光显微镜，研究了来自外周髓鞘细胞质附着部位的蛋白——髓鞘碱性蛋白（MBP）、髓鞘蛋白零（P0ct）的细胞质尾巴和外周髓鞘蛋白2（P2）——如何相互作用以及与髓鞘样膜相互作用。DSC揭示了脂质相互作用随蛋白质组合的变化，膜流动性和稳定性发生改变。SPR支持了这些结果，表明髓鞘蛋白可能竞争膜表面结合。对脂质环境中髓鞘蛋白诱导的布拉格峰的分析表明，蛋白质 - 脂质复合物中同时存在层状相和非层状相，这表明形成了可能与髓鞘组装相关的纳米级结构。显微镜实验显示，每种蛋白质单独或共同作用时都会形成新的膜结构。我们的数据表明，存在于外周神经系统髓鞘主致密线中的三种主要蛋白质之间既有协同作用也有竞争。观察到的髓鞘蛋白对脂质膜结构和性质的直接影响可能与其在髓鞘形成细胞中的功能以及在髓鞘疾病中的作用有关。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c8c6/12326912/88469c858635/FEBS-292-3960-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c8c6/12326912/d1a5ef07e26d/FEBS-292-3960-g011.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c8c6/12326912/1dcb9f892e9b/FEBS-292-3960-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c8c6/12326912/e9f5338eed17/FEBS-292-3960-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c8c6/12326912/bc683faafe71/FEBS-292-3960-g012.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c8c6/12326912/88469c858635/FEBS-292-3960-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c8c6/12326912/d1a5ef07e26d/FEBS-292-3960-g011.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c8c6/12326912/d5b88a08bb89/FEBS-292-3960-g008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c8c6/12326912/9706ff2bb288/FEBS-292-3960-g009.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c8c6/12326912/a82a898d44a8/FEBS-292-3960-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c8c6/12326912/2d7aba242e2d/FEBS-292-3960-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c8c6/12326912/1dcb9f892e9b/FEBS-292-3960-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c8c6/12326912/e9f5338eed17/FEBS-292-3960-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c8c6/12326912/bc683faafe71/FEBS-292-3960-g012.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c8c6/12326912/598f6d98eff7/FEBS-292-3960-g013.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c8c6/12326912/cbf502fb1fc1/FEBS-292-3960-g004.jpg
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本文引用的文献

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The cytoplasmic tail of myelin protein zero induces morphological changes in lipid membranes.髓鞘蛋白零的细胞质尾巴诱导脂质膜发生形态变化。
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