ArticleArchives of biochemistry and biophysics2015
Elastic proteins in the flight muscle of Manduca sexta.
Article in Archives of biochemistry and biophysics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 14 citations in OpenAlex.
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- Nanometer scale difference in myofilament lattice structure of muscle alters muscle function in a spatially explicit model.PLoS computational biology · 2025Article
- The effect of muscle ultrastructure on the force, displacement and work capacity of skeletal muscle.Journal of the Royal Society, Interface · 2024Article
- Shotgun and TMT-Labeled Proteomic Analysis of the Ovarian Proteins of an Insect Vector, Aedes aegypti (Diptera: Culicidae).Journal of insect science (Online) · 2022Article
- A mechanism for sarcomere breathing: volume change and advective flow within the myofilament lattice.Biophysical journal · 2021Article
- Article
- Localization of the Elastic Proteins in the Flight Muscle ofInternational journal of molecular sciences · 2020Article
- Nanometer-scale structure differences in the myofilament lattice spacing of two cockroach leg muscles correspond to their different functions.The Journal of experimental biology · 2020Article
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
The flight muscles (DLM1) of the Hawkmoth, Manduca sexta are synchronous, requiring a neural spike for each contraction. Stress/strain curves of skinned DLM1 showed hysteresis indicating the presence of titin-like elastic proteins. Projectin and kettin are titin-like proteins previously identified in Lethocerus and Drosophila flight muscles. Analysis of Manduca muscles with 1% SDS-agarose gels and western blots showed two bands near 1 MDa that cross-reacted with antibodies to Drosophila projectin. Antibodies to Drosophila kettin cross-reacted to bands at ∼500 and ∼700 kDa, but also to bands at ∼1.6 and ∼2.1 MDa, that had not been previously observed in insect flight muscles. Mass spectrometry identified the 2.1 MDa protein as a product of the Sallimus (sls) gene. Analysis of the gene sequence showed that all 4 putative Sallimus and kettin isoforms could be explained as products of alternative splicing of the single sls gene. Both projectin and sallimus isoforms were expressed to higher levels in ventrally located DLM1 subunits, primarily responsible for active work production, as compared to dorsally located subunits, which may act as damped springs. The different expression levels of the 2 projectin isoforms and 4 sallimus/kettin isoforms may be adaptations to the specific requirements of individual muscle subunits.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.