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肌联蛋白是一种极其长、灵活且细长的肌原纤维蛋白。

Titin is an extraordinarily long, flexible, and slender myofibrillar protein.

作者信息

Wang K, Ramirez-Mitchell R, Palter D

出版信息

Proc Natl Acad Sci U S A. 1984 Jun;81(12):3685-9. doi: 10.1073/pnas.81.12.3685.

DOI:10.1073/pnas.81.12.3685
PMID:6587383
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC345283/
Abstract

" Titin " is a term used to describe a pair of closely related megadalton polypeptides that together are the third most abundant myofibrillar protein in a wide range of striated muscles. It has been proposed that titin and another giant protein, nebulin , are the major components of an elastic cytoskeletal lattice within the sarcomere. We have now purified the leading band, titin -2 (T2), of the titin doublet in native forms by extraction with Guba -Straub solution followed by chromatography. Electron microscopy of low-angle-shadowed and negatively stained specimens revealed that T2 chains self-assembled into extremely long (from 0.1 micron to over 1.0 micron), flexible, and extensible slender strands (4-5 nm in diameter) with axial periodicity. Furthermore, these strands tended to associate to form filamentous bundles and meshworks. Thus, titin appears to be ideally suited as a component of an elastic lattice that serves as an organizing scaffold or template for thick and thin filaments.

摘要

“肌联蛋白”是一个用于描述一对紧密相关的兆道尔顿多肽的术语,这两种多肽共同构成了多种横纹肌中第三丰富的肌原纤维蛋白。有人提出,肌联蛋白和另一种巨型蛋白伴肌动蛋白是肌节内弹性细胞骨架晶格的主要成分。我们现在通过用古巴-施特劳布溶液提取,然后进行色谱分离,以天然形式纯化了肌联蛋白双峰中的前导条带,即肌联蛋白-2(T2)。对低角度阴影和负染色标本的电子显微镜观察显示,T2链自组装成极长(从0.1微米到超过1.0微米)、灵活且可伸展的细长链(直径4-5纳米),具有轴向周期性。此外,这些链倾向于结合形成丝状束和网络。因此,肌联蛋白似乎非常适合作为弹性晶格的一个组成部分,该弹性晶格作为粗细肌丝的组织支架或模板。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b704/345283/392eda62094b/pnas00613-0087-h.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b704/345283/d9f1b3f9f6ee/pnas00613-0086-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b704/345283/61323d142bdb/pnas00613-0087-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b704/345283/1d207be4137a/pnas00613-0087-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b704/345283/ff03729d7532/pnas00613-0087-c.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b704/345283/999086935aed/pnas00613-0087-d.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b704/345283/f933e0ab42dc/pnas00613-0087-e.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b704/345283/b5bc71fed9a1/pnas00613-0087-f.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b704/345283/d77023643900/pnas00613-0087-g.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b704/345283/392eda62094b/pnas00613-0087-h.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b704/345283/d9f1b3f9f6ee/pnas00613-0086-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b704/345283/61323d142bdb/pnas00613-0087-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b704/345283/1d207be4137a/pnas00613-0087-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b704/345283/ff03729d7532/pnas00613-0087-c.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b704/345283/999086935aed/pnas00613-0087-d.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b704/345283/f933e0ab42dc/pnas00613-0087-e.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b704/345283/b5bc71fed9a1/pnas00613-0087-f.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b704/345283/d77023643900/pnas00613-0087-g.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b704/345283/392eda62094b/pnas00613-0087-h.jpg

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1
Titin is an extraordinarily long, flexible, and slender myofibrillar protein.肌联蛋白是一种极其长、灵活且细长的肌原纤维蛋白。
Proc Natl Acad Sci U S A. 1984 Jun;81(12):3685-9. doi: 10.1073/pnas.81.12.3685.
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Myofibrillar interaction of blot immunoaffinity-purified antibodies against native titin as studied by direct immunofluorescence and immunogold staining.通过直接免疫荧光和免疫金染色研究针对天然肌联蛋白的斑点免疫亲和纯化抗体的肌原纤维相互作用。
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Fibronectin molecule visualized in electron microscopy: a long, thin, flexible strand.在电子显微镜下观察到的纤连蛋白分子:一条细长、柔韧的链。
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End-filaments: a new structural element of vertebrate skeletal muscle thick filaments.终丝:脊椎动物骨骼肌粗肌丝的一种新结构元件。
Int J Mol Sci. 2020 Jun 1;21(11):3974. doi: 10.3390/ijms21113974.
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Downsizing the molecular spring of the giant protein titin reveals that skeletal muscle titin determines passive stiffness and drives longitudinal hypertrophy.缩小巨型蛋白titin 的分子弹簧表明,骨骼肌 titin 决定了被动刚度并驱动了纵向肥大。
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Do Actomyosin Single-Molecule Mechanics Data Predict Mechanics of Contracting Muscle?肌球蛋白单分子力学数据能否预测收缩肌的力学性质?
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