A low-cost 2-D sarcomere model to demonstrate titin-related mechanisms for force production.

IF 1.7 4区 教育学 Q2 EDUCATION, SCIENTIFIC DISCIPLINES
Advances in Physiology Education Pub Date : 2024-03-01 Epub Date: 2023-12-07 DOI:10.1152/advan.00090.2023
Heron Baptista de Oliveira Medeiros, Heiliane de Brito Fontana, Walter Herzog
{"title":"A low-cost 2-D sarcomere model to demonstrate titin-related mechanisms for force production.","authors":"Heron Baptista de Oliveira Medeiros, Heiliane de Brito Fontana, Walter Herzog","doi":"10.1152/advan.00090.2023","DOIUrl":null,"url":null,"abstract":"<p><p>Given the recently proposed three-filament theory of muscle contraction, we present a low-cost physical sarcomere model aimed at illustrating the role of titin in the production of active force in skeletal muscle. With inexpensive materials, it is possible to illustrate actin-myosin cross-bridge interactions between the thick and thin filaments and demonstrate the two different mechanisms by which titin is thought to contribute to active and passive muscle force. Specifically, the model illustrates how titin, a molecule with springlike properties, may increase its stiffness by binding free calcium upon muscle activation and reducing its extensible length by attaching itself to actin, resulting in the greater force-generating capacity after an active than a passive elongation that has been observed experimentally. The model is simple to build and manipulate, and demonstration to high school students was shown to result in positive perception and improved understanding of the otherwise complex titin-related mechanisms of force production in skeletal and cardiac muscles.<b>NEW & NOTEWORTHY</b> Our physical sarcomere model illustrates not only the classic view of muscle contraction, the sliding filament and cross-bridge theories, but also the newly discovered role of titin in force regulation, called the three-filament theory. The model allows for easy visualization of the role of titin in muscle contraction and aids in explaining complex muscle properties that are not captured by the traditional cross-bridge theory.</p>","PeriodicalId":50852,"journal":{"name":"Advances in Physiology Education","volume":" ","pages":"92-96"},"PeriodicalIF":1.7000,"publicationDate":"2024-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Advances in Physiology Education","FirstCategoryId":"95","ListUrlMain":"https://doi.org/10.1152/advan.00090.2023","RegionNum":4,"RegionCategory":"教育学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2023/12/7 0:00:00","PubModel":"Epub","JCR":"Q2","JCRName":"EDUCATION, SCIENTIFIC DISCIPLINES","Score":null,"Total":0}
引用次数: 0

Abstract

Given the recently proposed three-filament theory of muscle contraction, we present a low-cost physical sarcomere model aimed at illustrating the role of titin in the production of active force in skeletal muscle. With inexpensive materials, it is possible to illustrate actin-myosin cross-bridge interactions between the thick and thin filaments and demonstrate the two different mechanisms by which titin is thought to contribute to active and passive muscle force. Specifically, the model illustrates how titin, a molecule with springlike properties, may increase its stiffness by binding free calcium upon muscle activation and reducing its extensible length by attaching itself to actin, resulting in the greater force-generating capacity after an active than a passive elongation that has been observed experimentally. The model is simple to build and manipulate, and demonstration to high school students was shown to result in positive perception and improved understanding of the otherwise complex titin-related mechanisms of force production in skeletal and cardiac muscles.NEW & NOTEWORTHY Our physical sarcomere model illustrates not only the classic view of muscle contraction, the sliding filament and cross-bridge theories, but also the newly discovered role of titin in force regulation, called the three-filament theory. The model allows for easy visualization of the role of titin in muscle contraction and aids in explaining complex muscle properties that are not captured by the traditional cross-bridge theory.

一个低成本的二维肌节模型,以证明力产生的相关机制。
鉴于最近提出的肌肉收缩三丝理论,我们提出了一个低成本的物理肌节模型,旨在说明titin在骨骼肌中产生活动力的作用。使用廉价的材料,可以说明肌动蛋白-肌球蛋白在粗和细纤维之间的交叉桥相互作用,并证明肌动蛋白被认为有助于主动和被动肌肉力量的两种不同机制。具体来说,该模型说明了肌动蛋白(一种具有弹簧性质的分子)如何在肌肉激活时通过结合游离钙来增加其刚度,并通过将自身附着在肌动蛋白上来减少其可扩展长度,从而在实验中观察到的主动延伸后比被动延伸后产生更大的力。该模型易于建立和操作,并向高中生演示,结果显示产生积极的感知,并提高了对骨骼肌和心肌中力产生的复杂的titin相关机制的理解。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
来源期刊
CiteScore
3.40
自引率
19.00%
发文量
100
审稿时长
>12 weeks
期刊介绍: Advances in Physiology Education promotes and disseminates educational scholarship in order to enhance teaching and learning of physiology, neuroscience and pathophysiology. The journal publishes peer-reviewed descriptions of innovations that improve teaching in the classroom and laboratory, essays on education, and review articles based on our current understanding of physiological mechanisms. Submissions that evaluate new technologies for teaching and research, and educational pedagogy, are especially welcome. The audience for the journal includes educators at all levels: K–12, undergraduate, graduate, and professional programs.
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信