Cell and muscle motility最新文献

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A periodic cytoskeletal lattice in striated muscle. 横纹肌中周期性的细胞骨架晶格

Cell and muscle motility

Pub Date : 1985-01-01 DOI: 10.1007/978-1-4757-4723-2_9

P Cooke

The axial periodicities of electron density in striated muscle fibers extend over four orders of magnitude, ranging from the sarcomere repeat (2000-3000 nm) to a residue repeat in the alpha-helix of structural proteins (0.15 nm). A prevailing idea about the regular arrangement of structures in the contractile apparatus maintains that long-range axial spacings, related to the organization of sarcomere repeats, are essentially independent of the short-range periodicities with molecular dimensions. This is a central theme of the sliding filament hypothesis but is only supported by evidence from measured spacings near the upper and lower limits in the spectrum of dimensions, leaving a wide gap in resolved structural information extending from about 460 down to 50 nm. Several independent morphological methods show an electron-dense cross-striation of low amplitude with a pseudo-period of 230 nm, out of phase with the sarcomere repeat, in myofibrils of frog twitch fibers. Averaged images of embedded muscle fibers indicate that the sarcomere repeat contains five symmetrical pairs of these striations, which are coordinated with discrete repeats of the major molecular periods in the thick and thin filaments, in register within A and I bands. The pseudo-period therefore correlates short-range molecular repeats in the filaments with long-range registry of the sarcomere repeats in myofibrils. This raises the interesting possibility that the 230-nm pseudo-periodicity identifies a replicated axial structure in myofibrils that integrates the organization of the major structural proteins into the sarcomere repeat. The density distribution in sarcomeres of isolated unstained myofibrils also establishes that symmetrical pairs of striations with intrinsically low amplitudes are independently distorted out of uniform register in stretched sarcomeres. This behavior is consistent with the properties of N lines. The out-of-phase arrangement of 230-nm striations in the sarcomere repeat of twitch fibers should produce special diffraction effects in the region of the gap in the spectrum of periodicities recorded from muscle, with maxima at spacings extending from 200 to 80 nm. Correspondence between the diffraction spectrum of myofibril models containing a 230-nm spaced axial pseudo-period and the observed very low-angle X-ray diffraction spacings from living muscle (Huxley and Brown, 1967) suggests that the 230-nm pseudo-periodicity is a regular detectable component of striated muscle, resembling the structure of naturally occurring leptomeric fibrils in extrafusal and intrafusal fibers (Karlson and Andersson-Cedergren, 1968).(ABSTRACT TRUNCATED AT 400 WORDS)

横纹肌纤维中电子密度的轴向周期性延伸超过4个数量级，范围从肌节重复(2000-3000 nm)到结构蛋白α -螺旋中的残基重复(0.15 nm)。关于收缩器官中结构的规则排列，一种流行的观点认为，与肌节重复序列的组织有关的远距离轴向间隔，本质上与分子尺度的短程周期性无关。这是滑动灯丝假说的中心主题，但只有在尺寸光谱上下限附近的测量间距的证据支持，在解决的结构信息中留下了很大的差距，从大约460到50纳米。几种独立的形态学方法显示，蛙抽搐纤维的肌原纤维中存在低振幅的电子密集交叉条纹，其伪周期为230 nm，与肌节重复不一致。嵌入肌纤维的平均图像表明，肌节重复包含五对对称的这些条纹，它们与粗丝和细丝中主要分子周期的离散重复协调，在A和I波段内登记。因此，伪周期将细丝中的短距离分子重复序列与肌原纤维中肌节重复序列的长期记录联系起来。这提出了一种有趣的可能性，即230纳米的伪周期性识别了肌原纤维中复制的轴向结构，该结构将主要结构蛋白的组织整合到肌节重复序列中。分离的未染色肌原纤维肌节中的密度分布也表明，在拉伸肌节中，具有固有低振幅的对称条纹对被独立地扭曲而不均匀。这种行为与N线的性质是一致的。抽搐纤维肌节重复序列中230nm条纹的异相排列应该会在肌肉记录的周期性频谱的间隙区域产生特殊的衍射效应，其最大值从200 nm延伸到80 nm。含有间隔230纳米轴向伪周期的肌原纤维模型的衍射光谱与从活肌肉中观察到的极低角度x射线衍射间隔之间的对应关系(Huxley和Brown, 1967)表明，230纳米伪周期是横纹肌中可检测到的规则成分，类似于肌外纤维和肌内纤维中自然产生的细纤维的结构(Karlson和Andersson-Cedergren, 1968)。(摘要删节为400字)

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引用次数: 11

Autoantibodies to the cytoskeleton in human sera. 人血清中细胞骨架的自身抗体。

Cell and muscle motility

Pub Date : 1985-01-01 DOI: 10.1007/978-1-4757-4723-2_3

J M Oliver, J L Senecal, N L Rothfield

引用次数: 5

Monoclonal antibodies to intermediate filament proteins. Use in diagnostic surgical pathology. 中间丝蛋白单克隆抗体。用于外科病理诊断。

Cell and muscle motility

Pub Date : 1984-01-01 DOI: 10.1007/978-1-4684-4592-3_11

A M Vogel, A M Gown

引用次数: 31

The dynamics of cytoskeletal organization in areas of cell contact. 细胞接触区域内细胞骨架组织的动力学。

Cell and muscle motility

Pub Date : 1984-01-01 DOI: 10.1007/978-1-4684-4592-3_5

B Geiger, Z Avnur, T E Kreis, J Schlessinger

引用次数: 68

The biochemistry of microtubules. A review. 微管生物化学。复习一下。

Cell and muscle motility

Pub Date : 1984-01-01 DOI: 10.1007/978-1-4684-4592-3_7

T W McKeithan, J L Rosenbaum

引用次数: 28

Genetic dissection of the assembly of microtubules and their role in mitosis. 微管组装的遗传解剖及其在有丝分裂中的作用。

Cell and muscle motility

Pub Date : 1984-01-01 DOI: 10.1007/978-1-4684-4592-3_9

F Cabral

引用次数: 7

The cytoskeleton. 细胞骨架。

Cell and muscle motility

Pub Date : 1984-01-01

引用次数: 0

The form and function of actin. A product of its unique design. 肌动蛋白的形态和功能。设计独特的产品。

Cell and muscle motility

Pub Date : 1984-01-01 DOI: 10.1007/978-1-4684-4592-3_3

D J DeRosier, L G Tilney

引用次数: 21

Changes in actin during cell differentiation. 细胞分化过程中肌动蛋白的变化。

Cell and muscle motility

Pub Date : 1984-01-01 DOI: 10.1007/978-1-4684-4592-3_4

K Nagata, Y Ichikawa

引用次数: 11

MAP2 (microtubule-associated protein 2). 微管相关蛋白2。

Cell and muscle motility

Pub Date : 1984-01-01 DOI: 10.1007/978-1-4684-4592-3_8

R B Vallee

引用次数: 34

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