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肌营养不良蛋白中央杆状结构域的进化保守性。

Evolutionary conservation of the dystrophin central rod domain.

作者信息

Sherratt T G, Vulliamy T, Strong P N

机构信息

Department of Paediatrics and Neonatal Medicine, Royal Postgraduate Medical School, Hammersmith Hospital, London, U.K.

出版信息

Biochem J. 1992 Nov 1;287 ( Pt 3)(Pt 3):755-9. doi: 10.1042/bj2870755.

DOI:10.1042/bj2870755
PMID:1280104
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1133072/
Abstract

Dystrophin cDNA fragments encoding the C-terminal repeats of the central rod region have been expressed as fusion proteins. The polyclonal antisera raised to the purified fusion proteins have been characterized and neither antiserum cross-reacted with dystrophin-related protein. Antisera detected dystrophin with molecular mass close to that of the human in all terrestrial vertebrates and amphibia studied. Experiments with antisera to the N-terminal region of the dystrophin rod confirmed that epitopes to the rod region were conserved during this evolutionary period and the length of this domain remained unaltered.

摘要

编码中央杆状区域C末端重复序列的肌营养不良蛋白cDNA片段已被表达为融合蛋白。针对纯化融合蛋白产生的多克隆抗血清已得到鉴定,且两种抗血清均未与肌营养不良蛋白相关蛋白发生交叉反应。在所研究的所有陆生脊椎动物和两栖动物中,抗血清检测到的肌营养不良蛋白分子量与人的接近。用针对肌营养不良蛋白杆状结构N末端区域的抗血清进行的实验证实,在这个进化时期,杆状区域的表位是保守的,并且该结构域的长度保持不变。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7a0d/1133072/a8ac32bcf8fc/biochemj00124-0096-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7a0d/1133072/7796a5fcb302/biochemj00124-0095-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7a0d/1133072/cf6c3c044f18/biochemj00124-0096-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7a0d/1133072/a8ac32bcf8fc/biochemj00124-0096-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7a0d/1133072/7796a5fcb302/biochemj00124-0095-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7a0d/1133072/cf6c3c044f18/biochemj00124-0096-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7a0d/1133072/a8ac32bcf8fc/biochemj00124-0096-b.jpg

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将包含 dystrophin 卷曲螺旋结构域 C 端螺旋 1 的 AAV2/9-microdystrophin 基因递送到 mdx 小鼠的骨骼肌中,可改善肌肉病理学,并恢复 α1- 连接蛋白和 α- dystrobrevin 的水平。
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