相关实验视频
Updated: Jun 4, 2025

07:52
DNA Electroporation, Isolation and Imaging of Myofibers
Published on: December 23, 2015
12.2K
在骨肌肉中,Syntaxin 4增强的血修复独立于dysferlin
Hsin-Yu Chen1, Daniel E Michele1,2
1Department of Molecular & Integrative Physiology, University of Michigan, Ann Arbor, Michigan, United States.
American journal of physiology. Cell physiology
|December 27, 2024
概括
肌肉细胞中的等离子膜修复 (PMR) 需要SNARE复杂的拆卸. 过度表达STX4增强PMR独立于dysferlin,这表明SNARE对于肌肉细胞修复至关重要.
科学领域:
- 细胞生物学 细胞生物学
- 肌肉生理学 肌肉生理学
- 膜动力学 膜动力学
背景情况:
- 血修复 (PMR) 对于细胞生存至关重要.
- 迪斯弗林是一种Ca2+结合蛋白,对骨肌肉PMR至关重要.
- 在神经传递等过程中,SNARE蛋白调解膜融合.
研究的目的:
- 为了研究肌肉细胞中SNARE介导的PMR是否需要dysferlin.
- 确定SNARE复杂拆解在PMR中的作用.
- 评估STX4过度表达对PMR的影响.
主要方法:
- 使用TAT-NSF700.00进行SNARE复合物分解的药理抑制.
- 涉及STX4和SNAP23.23过度表达的基因操纵.
- 对肌肉细胞 (hiPS-CMs和FDB纤维) 中的膜完整性和Ca2+流入的评估.
- 激光诱导的膜受伤模型.
主要成果:
- 抑制SNARE复合体分解增加了hiPS-CMs中的膜损伤.
- TAT-NSF700治疗导致Ca2+流入增加,但在受伤的FDB纤维中减少了FM1-43吸收.
- STX4或SNAP23的过度表达减少了受伤的FDB纤维中的Ca2+流入.
- 过度表达STX4甚至在缺乏dysferlin的FDB纤维中改善了PMR.
结论:
- 在肌肉细胞中,SNARE复杂分解对于高效的血膜修复至关重要.
- STX4增强了骨肌中的PMR,这种效果独立于dysferlin.
- 在骨肌中,SNARE介导的PMR机制可能独立于dysferlin运作.
相关概念视频
Satellite Stem Cells and Muscular Dystrophy
1.9K
Satellite stem cells or myosatellite cells are quiescent stem cells that Alexander Mauro first identified in 1961. These cells are located between the sarcolemma, the plasma membrane of muscle fibers, and the basal lamina, the connective tissue sheath covering it. These mononucleated cells are activated in response to muscle injury, can transform into myoblasts, and may form or repair muscle fibers. Myosatellite cells can provide additional myonuclei for muscle regeneration or return to a...
1.9K
Cross-bridge Cycle
116.8K
As muscle contracts, the overlap between the thin and thick filaments increases, decreasing the length of the sarcomere—the contractile unit of the muscle—using energy in the form of ATP. At the molecular level, this is a cyclic, multistep process that involves binding and hydrolysis of ATP, and movement of actin by myosin.
116.8K
The Sarcomere
7.6K
A sarcomere is a microscopic segment repeating in a myofibril. The sarcomere fundamentally consists of two main myofilaments: thick filaments called myosin and thin filaments called actin. These filaments interact by sliding past each other in response to stimulus. In addition to myosin and actin, several other proteins, such as tropomyosin, troponin, titin, nebulin, myomesin, α-actinin, and dystrophin, play crucial roles in regulating, structuring, and functioning of the sarcomere.
Each...
Each...
7.6K
Disassembly of Intermediate Filaments
2.0K
Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...
2.0K
Actin Filament Depolymerization
3.0K
Actin filaments (F-actin) are composed of actin subunits. The dissociation of actin monomers can occur from either end of F-actin. The rate of dissociation is faster from the minus-end or the pointed end, where the actin subunits exist with a bound ADP, together known as ADP-actin. The depolymerization of F-actin is aided by proteins, including the actin-depolymerizing factor (ADF) and cofilin family of proteins, gelsolin, and glia maturation factor (GMF).
In F-actin, the ADF/cofilin proteins...
In F-actin, the ADF/cofilin proteins...
3.0K

