心筋動中の電気機械的渦状フィラメント
J Christoph1,2,3, M Chebbok2,4, C Richter1,2,4
1Max Planck Institute for Dynamics and Self-Organization, Göttingen, Germany.
Nature
|February 22, 2018
まとめ
この研究では 超音波を用いて心臓の3D機械的スクロール波を視覚化し 電気信号と共に心臓の動におけるその役割を明らかにしました これらの発見は 心律不整の診断と治療に 新たな道を開きます
科学分野:
- 心臓病科
- バイオ物理学
- 医療用イメージング
背景:
- 渦のような回転する波が 刺激可能なシステムで複雑なパターンを駆動します
- 3Dスクロール波のフィラメントのような相異性は 心拍不良の鍵です
- 心臓組織におけるスクロール波の 3Dダイナミクスを理解することは 極めて重要なことですが 難しいことです
研究 の 目的:
- 収縮する心臓の壁の中の 機械的な回転波の3D空間空間動態を 視覚化するために
- 心筋動中の 機械的および電気的相異変の共存と相互作用を調査する.
- メカニカル・フェーズ・シンギュラリティのダイナミクスを用いて心臓発作を特徴づける.
主な方法:
- 高解像度4D超音波ベースのストレインイメージングを使用して,3D機械スクロール波を観察しました.
- 膜ポテンシャル,細胞内カルシウム,および機械的収縮を同時に測定した.
- 分析された軌跡,トポロジカルチャージ,および電気的および機械的相奇異の寿命.
主要な成果:
- 心臓の壁の奥深くにある 3D 機械的なスクロール波と ファイラメントのような相の特異性を 視覚化しました
- 観測された機械的相異性と,心動中の電気的相異性.
- 電気と機械の相異性との複雑な相互作用を証明した.
結論:
- 心筋動は,心室壁から発生する機械的相奇異の3D空間時間動態によって特徴付けられます.
- 電気と機械の相異性は ダイナミックに相互作用します
- この発見は,心臓動脈不律に対する新しい非侵襲的診断および治療戦略につながる可能性があります.
関連する概念動画
Amyloid Fibrils
12.1K
Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
12.1K
Amyloid Fibrils
6.5K
6.5K
Fibril-associated Collagen
3.4K
Fibril-associated collagens are a type of collagens present in the extracellular matrix with interrupted triple helices or FACIT (Fibril-associated collagens interrupted triple-helices). FACIT help connect and attach the collagen fibrils with each other as well as with other proteins of the extracellular matrix.
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...
3.4K
Disassembly of Intermediate Filaments
2.7K
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...
2.7K
Adaptability of Cytoskeletal Filaments
6.1K
The cytoskeleton is a complex dynamic structure performing varied functions based on cellular requirements. The adaptability of the individual filaments in the cytoskeleton determines their ability to perform various functions within the cell. It can undergo rapid reorganization during processes like cell division or remain stable for several hours as in the interphase. The adaptability of these filaments depends on stringent regulatory mechanisms. The microfilament and microtubules of the...
6.1K
Assembly of Cytoskeletal Filaments
28.0K
Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
28.0K


