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The P2X7 purinoceptor in pathogenesis and treatment of dystrophino- and sarcoglycanopathies

The P2X7 purinoceptor in pathogenesis and treatment of dystrophino- and sarcoglycanopathies
The P2X7 purinoceptor in pathogenesis and treatment of dystrophino- and sarcoglycanopathies
Dystrophinopathy and sarcoglycanopathies are incurable diseases caused by mutations in the genes encoding dystrophin or members of the dystrophin associated protein complex (DAPC). Restoration of the missing dystrophin or sarcoglycans via genetic approaches is complicated by the downsides of personalised medicines and immune responses against re-expressed proteins. Thus, the targeting of disease mechanisms downstream from the mutant protein has a strong translational potential. Acute muscle damage causes release of large quantities of ATP, which activates P2X7 purinoceptors, resulting in inflammation that clears dead tissues and triggers regeneration. However, in dystrophic muscles, loss of α-sarcoglycan ecto-ATPase activity further elevates extracellular ATP (eATP) levels, exacerbating the pathology. Moreover, seemingly compensatory P2X7 upregulation in dystrophic muscle cells, combined with high eATP leads to further damage. Accordingly, P2X7 blockade alleviated dystrophic damage in mouse models of both dystrophinopathy and sarcoglycanopathy. Existing P2X7 blockers could be re-purposed for the treatment of these highly debilitating diseases.
1471-4892
Gόrecki, Dariusz C.
409eef1f-a212-4c5c-a14a-fae9552281e8
Rumney, Robin M.H.
fa3de9f8-b604-44e2-9e72-3e57980ce67f
Gόrecki, Dariusz C.
409eef1f-a212-4c5c-a14a-fae9552281e8
Rumney, Robin M.H.
fa3de9f8-b604-44e2-9e72-3e57980ce67f

Gόrecki, Dariusz C. and Rumney, Robin M.H. (2023) The P2X7 purinoceptor in pathogenesis and treatment of dystrophino- and sarcoglycanopathies. Current Opinion in Pharmacology, 69, [102357]. (doi:10.1016/j.coph.2023.102357).

Record type: Article

Abstract

Dystrophinopathy and sarcoglycanopathies are incurable diseases caused by mutations in the genes encoding dystrophin or members of the dystrophin associated protein complex (DAPC). Restoration of the missing dystrophin or sarcoglycans via genetic approaches is complicated by the downsides of personalised medicines and immune responses against re-expressed proteins. Thus, the targeting of disease mechanisms downstream from the mutant protein has a strong translational potential. Acute muscle damage causes release of large quantities of ATP, which activates P2X7 purinoceptors, resulting in inflammation that clears dead tissues and triggers regeneration. However, in dystrophic muscles, loss of α-sarcoglycan ecto-ATPase activity further elevates extracellular ATP (eATP) levels, exacerbating the pathology. Moreover, seemingly compensatory P2X7 upregulation in dystrophic muscle cells, combined with high eATP leads to further damage. Accordingly, P2X7 blockade alleviated dystrophic damage in mouse models of both dystrophinopathy and sarcoglycanopathy. Existing P2X7 blockers could be re-purposed for the treatment of these highly debilitating diseases.

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Accepted/In Press date: 29 December 2022
e-pub ahead of print date: 24 February 2023
Published date: 24 February 2023

Identifiers

Local EPrints ID: 498138
URI: http://eprints.soton.ac.uk/id/eprint/498138
ISSN: 1471-4892
PURE UUID: f24da6d8-6468-4225-9d76-ce380023ee64
ORCID for Robin M.H. Rumney: ORCID iD orcid.org/0000-0002-4266-5962

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Date deposited: 11 Feb 2025 17:31
Last modified: 12 Feb 2025 02:48

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Contributors

Author: Dariusz C. Gόrecki
Author: Robin M.H. Rumney ORCID iD

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