Localization of the Elastic Proteins in the Flight Muscle of <i>Manduca sexta</i>

The flight muscle of <i>Manduca sexta</i> (DLM<sub>1</sub>) is an emerging model system for biophysical studies of muscle contraction. Unlike the well-studied indirect flight muscle of <i>Lethocerus</i> and <i>Drosophila</i>, the DLM<sub>1</su...

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Main Authors: Henry Gong, Weikang Ma, Shaoshuai Chen, Geng Wang, Ramzi Khairallah, Thomas Irving
Format: Article
Language:English
Published: MDPI AG 2020-07-01
Series:International Journal of Molecular Sciences
Subjects:
Online Access:https://www.mdpi.com/1422-0067/21/15/5504
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author Henry Gong
Weikang Ma
Shaoshuai Chen
Geng Wang
Ramzi Khairallah
Thomas Irving
author_facet Henry Gong
Weikang Ma
Shaoshuai Chen
Geng Wang
Ramzi Khairallah
Thomas Irving
author_sort Henry Gong
collection DOAJ
description The flight muscle of <i>Manduca sexta</i> (DLM<sub>1</sub>) is an emerging model system for biophysical studies of muscle contraction. Unlike the well-studied indirect flight muscle of <i>Lethocerus</i> and <i>Drosophila</i>, the DLM<sub>1</sub> of <i>Manduca</i> is a synchronous muscle, as are the vertebrate cardiac and skeletal muscles. Very little has been published regarding the ultrastructure and protein composition of this muscle. Previous studies have demonstrated that DLM<sub>1</sub> express two projectin isoform, two kettin isoforms, and two large Salimus (Sls) isoforms. Such large Sls isoforms have not been observed in the asynchronous flight muscles of <i>Lethocerus</i> and <i>Drosophila.</i> The spatial localization of these proteins was unknown. Here, immuno-localization was used to show that the N-termini of projectin and Salimus are inserted into the Z-band. Projectin spans across the I-band, and the C-terminus is attached to the thick filament in the A-band. The C-terminus of Sls was also located in the A-band. Using confocal microscopy and experimental force-length curves, thin filament lengths were estimated as ~1.5 µm and thick filament lengths were measured as ~2.5 µm. This structural information may help provide an interpretive framework for future studies using this muscle system.
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spelling doaj.art-7247f13e2a7c44ddbd5fddcf286cf0542023-11-20T08:43:07ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672020-07-012115550410.3390/ijms21155504Localization of the Elastic Proteins in the Flight Muscle of <i>Manduca sexta</i>Henry Gong0Weikang Ma1Shaoshuai Chen2Geng Wang3Ramzi Khairallah4Thomas Irving5Department of Biological Sciences, Illinois Institute of Technology, Chicago, IL 60616, USADepartment of Biological Sciences, Illinois Institute of Technology, Chicago, IL 60616, USADepartment of Biological Sciences, Illinois Institute of Technology, Chicago, IL 60616, USADepartment of Biological Sciences, Illinois Institute of Technology, Chicago, IL 60616, USADepartment of Cell and Molecular Physiology, Loyola University Chicago, Stritch School of Medicine, Maywood, IL 60153, USADepartment of Biological Sciences, Illinois Institute of Technology, Chicago, IL 60616, USAThe flight muscle of <i>Manduca sexta</i> (DLM<sub>1</sub>) is an emerging model system for biophysical studies of muscle contraction. Unlike the well-studied indirect flight muscle of <i>Lethocerus</i> and <i>Drosophila</i>, the DLM<sub>1</sub> of <i>Manduca</i> is a synchronous muscle, as are the vertebrate cardiac and skeletal muscles. Very little has been published regarding the ultrastructure and protein composition of this muscle. Previous studies have demonstrated that DLM<sub>1</sub> express two projectin isoform, two kettin isoforms, and two large Salimus (Sls) isoforms. Such large Sls isoforms have not been observed in the asynchronous flight muscles of <i>Lethocerus</i> and <i>Drosophila.</i> The spatial localization of these proteins was unknown. Here, immuno-localization was used to show that the N-termini of projectin and Salimus are inserted into the Z-band. Projectin spans across the I-band, and the C-terminus is attached to the thick filament in the A-band. The C-terminus of Sls was also located in the A-band. Using confocal microscopy and experimental force-length curves, thin filament lengths were estimated as ~1.5 µm and thick filament lengths were measured as ~2.5 µm. This structural information may help provide an interpretive framework for future studies using this muscle system.https://www.mdpi.com/1422-0067/21/15/5504<i>Manduca sexta</i>synchronous insect flight musclemyofilament lengthselastic proteinssarcomere structures
spellingShingle Henry Gong
Weikang Ma
Shaoshuai Chen
Geng Wang
Ramzi Khairallah
Thomas Irving
Localization of the Elastic Proteins in the Flight Muscle of <i>Manduca sexta</i>
International Journal of Molecular Sciences
<i>Manduca sexta</i>
synchronous insect flight muscle
myofilament lengths
elastic proteins
sarcomere structures
title Localization of the Elastic Proteins in the Flight Muscle of <i>Manduca sexta</i>
title_full Localization of the Elastic Proteins in the Flight Muscle of <i>Manduca sexta</i>
title_fullStr Localization of the Elastic Proteins in the Flight Muscle of <i>Manduca sexta</i>
title_full_unstemmed Localization of the Elastic Proteins in the Flight Muscle of <i>Manduca sexta</i>
title_short Localization of the Elastic Proteins in the Flight Muscle of <i>Manduca sexta</i>
title_sort localization of the elastic proteins in the flight muscle of i manduca sexta i
topic <i>Manduca sexta</i>
synchronous insect flight muscle
myofilament lengths
elastic proteins
sarcomere structures
url https://www.mdpi.com/1422-0067/21/15/5504
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