Quantitative imaging of the dystrophin-glycoprotein complex

Goncalves de Mello, Monique

Quantitative imaging of the dystrophin-glycoprotein complex

Goncalves de Mello, Monique

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Publication Type:: Thesis
Issue Date:: 2024

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Field	Value	Language
dc.contributor.author	Goncalves de Mello, Monique
dc.date.accessioned	2024-12-02T22:41:08Z
dc.date.available	2024-12-02T22:41:08Z
dc.date.issued	2024
dc.identifier.uri	http://hdl.handle.net/10453/182312
dc.description	University of Technology Sydney. Faculty of Science.	en_US.UTF-8
dc.description.abstract	Dystrophin, an essential protein for muscle fibre function, is part of the dystrophin-glycoprotein complex (DGC), which stabilizes muscle contraction by linking the cytoskeletal actin network to the extracellular matrix. The DGC interacts with dystrophin-associated proteins to maintain muscle fibre structure and neuromuscular synapse stability. Mutations in the dystrophin gene can cause Duchenne and Becker's muscular dystrophy. This thesis advances techniques for studying the DGC, mainly using laser ablation-inductively coupled plasma-mass spectrometry (LA-ICP-MS) and immuno-mass spectrometry imaging (iMSI). The initial chapters review DGC structure and protein-protein interaction techniques, highlighting the limitations of previous methods in quantitative spatial imaging. Subsequent chapters address the impact of sample preparation steps on imaging accuracy and introduce protocols for improving reproducible antibody binding in iMSI. Additionally, the thesis explores enhancing bio-imaging sensitivity with N2 flow in the ICP carrier gas. A highly multiplexed iMSI method analysing ten biomolecules provided insights into healthy and Becker's muscular dystrophy (BMD) muscle tissues, impacting the traditional BMD assessment methods. The research emphasizes advanced imaging techniques' potential for understanding dystrophin-related disorders and developing therapies.	en_US.UTF-8
dc.format	Thesis (PhD)
dc.language.iso	en_US	en_US.UTF-8
dc.relation	https://opus.lib.uts.edu.au/bitstream/10453/182312/1/thesis.pdf
dc.rights	info:eu-repo/semantics/openAccess
dc.rights	The author owns the copyright in this thesis including all reproduction and reuse rights for the work. The work may not be altered without the permission of the copyright owner. Attribution is essential when quoting or paraphrasing from this thesis.
dc.rights	© 2024 Monique Goncalves de Mello
dc.rights	au.edu.uts.lib/cph
dc.title	Quantitative imaging of the dystrophin-glycoprotein complex	en_US.UTF-8
dc.type	Thesis
utslib.copyright.status	open_access	*

Abstract:

Dystrophin, an essential protein for muscle fibre function, is part of the dystrophin-glycoprotein complex (DGC), which stabilizes muscle contraction by linking the cytoskeletal actin network to the extracellular matrix. The DGC interacts with dystrophin-associated proteins to maintain muscle fibre structure and neuromuscular synapse stability. Mutations in the dystrophin gene can cause Duchenne and Becker's muscular dystrophy. This thesis advances techniques for studying the DGC, mainly using laser ablation-inductively coupled plasma-mass spectrometry (LA-ICP-MS) and immuno-mass spectrometry imaging (iMSI). The initial chapters review DGC structure and protein-protein interaction techniques, highlighting the limitations of previous methods in quantitative spatial imaging. Subsequent chapters address the impact of sample preparation steps on imaging accuracy and introduce protocols for improving reproducible antibody binding in iMSI. Additionally, the thesis explores enhancing bio-imaging sensitivity with N2 flow in the ICP carrier gas. A highly multiplexed iMSI method analysing ten biomolecules provided insights into healthy and Becker's muscular dystrophy (BMD) muscle tissues, impacting the traditional BMD assessment methods. The research emphasizes advanced imaging techniques' potential for understanding dystrophin-related disorders and developing therapies.

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http://hdl.handle.net/10453/182312