NDLI: Investigations of Molecular Mechanisms of Actin–Myosin Interactions in Cardiac Muscle

Content Provider	Springer Nature Link
Author	Nikitina, L. V. Kopylova, G. V. Shchepkin, D. V. Nabiev, S. R. Bershitsky, S. Y.
Copyright Year	2015
Abstract	The functional characteristics of cardiac muscle depend on the composition of protein isoforms in the cardiomyocyte contractile machinery. In the ventricular myocardium of mammals, several isoforms of contractile and regulatory proteins are expressed–two isoforms of myosin (V1 and V3) and three isoforms of tropomyosin chains (α, β, and κ). Expression of protein isoforms depends on the animal species, its age and hormonal status, and this can change with pathologies of the myocardium. Mutations in these proteins can lead to cardiomyopathies. The functional significance of the protein isoform composition has been studied mainly on intact hearts or on isolated preparations of myocardium, which could not provide a clear comprehension of the role of each particular isoform. Present-day experimental techniques such as an optical trap and in vitro motility assay make it possible to investigate the phenomena of interactions of contractile and regulatory proteins on the molecular level, thus avoiding effects associated with properties of a whole muscle or muscle tissue. These methods enable free combining of the isoforms to test the molecular mechanisms of their participation in the actin–myosin interaction. Using the optical trap and the in vitro motility assay, we have studied functional characteristics of the cardiac myosin isoforms, molecular mechanisms of the calcium-dependent regulation of actin–myosin interaction, and the role of myosin and tropomyosin isoforms in the cooperativity mechanisms in myocardium. The knowledge of molecular mechanisms underlying myocardial contractility and its regulation is necessary for comprehension of cardiac muscle functioning, its disorders in pathologies, and for development of approaches for their correction.
Starting Page	1748
Ending Page	1763
Page Count	16
File Format	PDF
ISSN	00062979
Journal	Biochemistry (Moscow)
Volume Number	80
Issue Number	13
e-ISSN	16083040
Language	English
Publisher	Pleiades Publishing
Publisher Date	2016-01-05
Publisher Place	Moscow
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	cardiac myosin isoforms tropomyosin actin–myosin interaction Ca2+ regulation optical trap in vitro motility assay Biochemistry Bioorganic Chemistry Microbiology Biomedicine general
Content Type	Text
Resource Type	Article
Subject	Biochemistry Biophysics Geriatrics and Gerontology

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Study of regulatory effect of tropomyosin on actin-myosin interaction in skeletal muscle by in vitro motility assay

Stabilization of the Central Part of Tropomyosin Molecule Alters the Ca2+-sensitivity of Actin-Myosin Interaction.

Effect of Cardiomyopathic Mutations in Tropomyosin on Calcium Regulation of the Actin—Myosin Interaction in Skeletal Muscle

Effect of Cardiac Myosin-Binding Protein C on Tropomyosin Regulation of Actin—Myosin Interaction Using In Vitro Motility Assay

Molecular mechanism of actin-myosin motor in muscle

Actomyosin systems of biological motility

Actomyosin systems of biological motility

Study of the interaction between rabbit cardiac contractile and regulatory proteins. An in vitro motility assay

Tropomyosin: Double helix from the protein world

Investigations of Molecular Mechanisms of Actin–Myosin Interactions in Cardiac Muscle

Similar Documents

Study of regulatory effect of tropomyosin on actin-myosin interaction in skeletal muscle by in vitro motility assay

Stabilization of the Central Part of Tropomyosin Molecule Alters the Ca2+-sensitivity of Actin-Myosin Interaction.

Effect of Cardiomyopathic Mutations in Tropomyosin on Calcium Regulation of the Actin—Myosin Interaction in Skeletal Muscle

Effect of Cardiac Myosin-Binding Protein C on Tropomyosin Regulation of Actin—Myosin Interaction Using In Vitro Motility Assay

Molecular mechanism of actin-myosin motor in muscle

Actomyosin systems of biological motility

Actomyosin systems of biological motility

Study of the interaction between rabbit cardiac contractile and regulatory proteins. An in vitro motility assay

Tropomyosin: Double helix from the protein world

Investigations of Molecular Mechanisms of Actin–Myosin Interactions in Cardiac Muscle