ATPase

The mechanisms of cardiac myopathies, a kinetics approach: Leading review

Published on: 16th July, 2020

OCLC Number/Unique Identifier: 8631130997

The normal adult heart is a well maintained machine that has a mechanism for growth replacement of the sarcomere that is lost by natural degeneration. This process ensures the heart has the strength of contraction to function correctly giving blood supply to the whole body. Some of the force of contraction of the sarcomere is transmitted to its major protein titin where its strength results in unfolding of a flexible section and release of a growth stimulant. The origin of all the cardiomyopathies can be traced to errors in this system resulting from mutations in a wide variety of the sarcomeric proteins. Too much or chronic tension transfer to titin giving increased growth resulting in hypertrophic cardiomyopathy (HCM) and too little leading to muscle wastage, dilated cardiomyopathy (DCM). HCM can ultimately lead to sudden cardiac death and DCM to heart failure. In this paper I show (1) a collection of the tension/ATPase calcium dependencies of cardiac myofibrils that define the mechanism of Ca2+ cooperativity. (2) I then reintroduce the stress/strain relationship to cardiomyopathies. (3) I then review the cardiomyopathy literature that contains similar Ca2+ dependency data to throw light on the mechanisms involved in generation of the types of myopathies from the mutations involved. In the review of cardiomyopathy there are two sections on mutations, the first dealing with those disrupting the Ca2+ cooperativity, i.e. the Hill coefficient of activation, leading to incomplete relaxation in diastole, chronic tension, and increased growth. Secondly dealing with those where the Ca2+ cooperativity is not affected giving either increased or decreased tension transfer to titin and changes in sarcomere growth. 
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New insights from cardiac muscle applied to skeletal muscle

Published on: 15th January, 2021

OCLC Number/Unique Identifier: 8897946095

I have recently described the origin of the second Ca2+ binding in the triggering of contractile activity in cardiac myofibrils that is the origin of the Ca2+ Hill coefficient of 2 for the ATPase. This site is not a simple protein binding site and cannot be measured by 45Ca2+ binding. The myofibril protein unit requirements are described by me and so are the consequences of disruption of the function of these units and the related medical outcomes. The purpose of this paper is to review the topic and extend the reasoning to the function of skeletal muscle and cite the literature that supports this.
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In silico analysis and characterization of fresh water fish ATPases and homology modelling

Published on: 11th October, 2017

OCLC Number/Unique Identifier: 7317598561

ATPases is known to be a crucial in many biological activities of organisms. In this study, physicochemical properties and modeling of ATPases protein of fish was analysed using In silico approach. ATPases a protein selected from fish species, including Gold fish (Carassius auratus auratus), Zebra fish (Hypancistrus zebra), White fishes (Coregonus autumnalis), Grass carp (Ctenopharyngodon idella) and Anabas testudineus (Koi) were used in this study. Physicochemical characteristics showed with molecular weight (25045.58-25148.57Da), theoretical isoelectric point (9.30-9.97), extinction coefficient(26470-34950), aliphatic index(147.31-150.35), instability index(32.84-42.67), total number of negatively charged residues and positively charged residues (5/7-6/8), and grand average of hydropathicity (1.014-1.151) were computed. All proteins were classified as transmembrane proteins. In secondary structure prediction, all proteins were composed of random coils as predominant, followed by extended strands, alpha helix and beta turn. Three dimensional structure of protein were predicted and verified as good structures. All model structures were evaluated being accepted and reliable based on structural evaluation and stereo chemical analysis.
Cite this ArticleCrossMarkPublonsHarvard Library HOLLISGrowKudosResearchGateBase SearchOAI PMHAcademic MicrosoftScilitSemantic ScholarUniversite de ParisUW LibrariesSJSU King LibrarySJSU King LibraryNUS LibraryMcGillDET KGL BIBLiOTEKJCU DiscoveryUniversidad De LimaWorldCatVU on WorldCat