{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,4]],"date-time":"2026-09-04T22:53:17Z","timestamp":1788562397437,"version":"build-2803163510"},"reference-count":88,"publisher":"Oxford University Press (OUP)","issue":"3","license":[{"start":{"date-parts":[[2026,4,24]],"date-time":"2026-04-24T00:00:00Z","timestamp":1776988800000},"content-version":"vor","delay-in-days":113,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Blade Therapeutics Pty Ltd"},{"DOI":"10.13039\/501100000925","name":"National Health and Medical Research Council Project","doi-asserted-by":"publisher","award":["APP1146750"],"award-info":[{"award-number":["APP1146750"]}],"id":[{"id":"10.13039\/501100000925","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001230","name":"Macquarie University","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001230","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Machado Joseph Disease (MJD) Foundation"},{"DOI":"10.13039\/100016887","name":"MND Australia","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100016887","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100014669","name":"British Society for Neuroendocrinology","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100014669","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,5,5]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Calcium-activated proteases, known as calpains, cleave proteins into smaller protein fragments, altering protein structure and function. Calpain overactivity is a pathological hallmark of many human diseases, including neurodegenerative diseases, which are characterized by excessive proteolytic cleavage and formation of protein aggregates. Current methods for determining calpain activity, such as examination of the presence or absence of calpain substrates in post-mortem tissue, are low-throughput, costly and retrospective, hampering the search for potentially therapeutically efficacious calpain inhibitor compounds. Here, we describe a novel methodology that allows real-time examination of calpain activity within the brain of the awake mouse. We used an adeno-associated viral (AAV) vector to express a fluorescence resonance energy transfer (FRET)-based calpain sensor in cerebellar neurons of male mice and measured real-time changes in FRET signal as a proxy for calpain activity via an implanted fibre optic cannula. This methodology was used to compare within-animal responses to different doses and administration routes of several calpain inhibitor compounds, including calpeptin, BLD-2736 and SNJ-1945. Using our AAV-calpain sensor and fibre photometry approach, we were able to obtain high-quality FRET recordings that were reproducible both between experimental animals and within experimental animals, allowing direct comparison of different calpain inhibitor compounds, enabling identification of the most efficacious treatment strategy that could be progressed further with preclinical treatment studies. As a positive control, we also tested changes in FRET signal in response to ionomycin, a known calcium ionophore. To our knowledge, this is the first report of real-time measurement of neuronal calpain activity in vivo. Future experiments could exploit this novel methodology to obtain calpain activity measurements alongside other pharmacological and behavioural\/physiological measurements to increase the translational validity of preclinical models for drug development in diseases characterized by calpain overactivity.<\/jats:p>","DOI":"10.1093\/braincomms\/fcag150","type":"journal-article","created":{"date-parts":[[2026,4,22]],"date-time":"2026-04-22T11:46:44Z","timestamp":1776858404000},"source":"Crossref","is-referenced-by-count":1,"title":["Using fibre photometry with a fluorescence resonance energy transfer-based biosensor to test efficacy of calpain inhibitors\n                    <i>in vivo<\/i>"],"prefix":"10.1093","volume":"8","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-9603-2696","authenticated-orcid":false,"given":"Katherine J","family":"Robinson","sequence":"first","affiliation":[{"name":"Motor Neuron Disease Research Centre, Macquarie Medical School, Faculty of Medicine, Health and Human Sciences, Macquarie University , Sydney 2109 ,","place":["Australia"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anita J","family":"Turner","sequence":"additional","affiliation":[{"name":"Macquarie Medical School, Faculty of Medicine, Health and Human Sciences, Macquarie University , Sydney 2109 ,","place":["Australia"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Holly I","family":"Ahel","sequence":"additional","affiliation":[{"name":"Motor Neuron Disease Research Centre, Macquarie Medical School, Faculty of Medicine, Health and Human Sciences, Macquarie University , Sydney 2109 ,","place":["Australia"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrea","family":"Kuriakose","sequence":"additional","affiliation":[{"name":"Motor Neuron Disease Research Centre, Macquarie Medical School, Faculty of Medicine, Health and Human Sciences, Macquarie University , Sydney 2109 ,","place":["Australia"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anastasiya","family":"Potapenko","sequence":"additional","affiliation":[{"name":"Motor Neuron Disease Research Centre, Macquarie Medical School, Faculty of Medicine, Health and Human Sciences, Macquarie University , Sydney 2109 ,","place":["Australia"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maxinne","family":"Watchon","sequence":"additional","affiliation":[{"name":"Motor Neuron Disease Research Centre, Macquarie Medical School, Faculty of Medicine, Health and Human Sciences, Macquarie University , Sydney 2109 ,","place":["Australia"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stuart K","family":"Plenderleith","sequence":"additional","affiliation":[{"name":"Motor Neuron Disease Research Centre, Macquarie Medical School, Faculty of Medicine, Health and Human Sciences, Macquarie University , Sydney 2109 ,","place":["Australia"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9226-6153","authenticated-orcid":false,"given":"Nicholas A","family":"Everett","sequence":"additional","affiliation":[{"name":"Brain and Mind Centre, School of Psychology, Faculty of Science, The University of Sydney , Sydney 2006 ,","place":["Australia"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9854-1029","authenticated-orcid":false,"given":"Simon","family":"McMullan","sequence":"additional","affiliation":[{"name":"Macquarie Medical School, Faculty of Medicine, Health and Human Sciences, Macquarie University , Sydney 2109 ,","place":["Australia"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6860-9192","authenticated-orcid":false,"given":"Angela S","family":"Laird","sequence":"additional","affiliation":[{"name":"Motor Neuron Disease Research Centre, Macquarie Medical School, Faculty of Medicine, Health and Human Sciences, Macquarie University , Sydney 2109 ,","place":["Australia"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2026,4,24]]},"reference":[{"issue":"45","key":"2026051510120175600_fcag150-B1","doi-asserted-by":"crossref","first-page":"30433","DOI":"10.1074\/jbc.R800035200","article-title":"Proteases: Multifunctional enzymes in life and disease","volume":"283","author":"L\u00f3pez-Ot\u00edn","year":"2008","journal-title":"J Biol Chem"},{"issue":"9","key":"2026051510120175600_fcag150-B2","doi-asserted-by":"crossref","first-page":"785","DOI":"10.1038\/nrd2092","article-title":"Targeting proteases: Successes, failures and future prospects","volume":"5","author":"Turk","year":"2006","journal-title":"Nat Rev Drug Discov"},{"issue":"1","key":"2026051510120175600_fcag150-B3","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1007\/s12035-008-8036-x","article-title":"Calpain-mediated signaling mechanisms in neuronal injury and neurodegeneration","volume":"38","author":"Vosler","year":"2008","journal-title":"Mol Neurobiol"},{"issue":"9","key":"2026051510120175600_fcag150-B4","doi-asserted-by":"crossref","first-page":"2013","DOI":"10.2337\/diabetes.50.9.2013","article-title":"Calpains play a role in insulin secretion and action","volume":"50","author":"Sreenan","year":"2001","journal-title":"Diabetes"},{"issue":"11","key":"2026051510120175600_fcag150-B5","doi-asserted-by":"crossref","first-page":"2985","DOI":"10.2337\/db10-1333","article-title":"Targeted inhibition of calpain reduces myocardial hypertrophy and fibrosis in mouse models of type 1 diabetes","volume":"60","author":"Li","year":"2011","journal-title":"Diabetes"},{"issue":"1","key":"2026051510120175600_fcag150-B6","doi-asserted-by":"crossref","first-page":"255","DOI":"10.2337\/db15-0963","article-title":"Mitochondrial calpain-1 disrupts ATP synthase and induces superoxide generation in type 1 diabetic hearts: A novel mechanism contributing to diabetic cardiomyopathy","volume":"65","author":"Ni","year":"2016","journal-title":"Diabetes"},{"issue":"5","key":"2026051510120175600_fcag150-B7","doi-asserted-by":"crossref","first-page":"364","DOI":"10.1038\/nrc3050","article-title":"The calpain system and cancer","volume":"11","author":"Storr","year":"2011","journal-title":"Nat Rev Cancer"},{"issue":"19","key":"2026051510120175600_fcag150-B8","doi-asserted-by":"crossref","first-page":"3464","DOI":"10.1091\/mbc.E14-12-1584","article-title":"Ezrin regulates focal adhesion and invadopodia dynamics by altering calpain activity to promote breast cancer cell invasion","volume":"26","author":"Hoskin","year":"2015","journal-title":"Mol Biol Cell"},{"issue":"15","key":"2026051510120175600_fcag150-B9","doi-asserted-by":"crossref","first-page":"2078","DOI":"10.1128\/MCB.01062-15","article-title":"Calpain genetic disruption and HSP90 inhibition combine to attenuate mammary tumorigenesis","volume":"36","author":"Grieve","year":"2016","journal-title":"Mol Cell Biol"},{"issue":"3","key":"2026051510120175600_fcag150-B10","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1517\/14728222.2011.553611","article-title":"Calpains as potential anti-cancer targets","volume":"15","author":"Leloup","year":"2011","journal-title":"Expert Opin Ther Targets"},{"issue":"1","key":"2026051510120175600_fcag150-B11","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1016\/j.molbiopara.2007.05.004","article-title":"BDA-410: A novel synthetic calpain inhibitor active against blood stage malaria","volume":"155","author":"Li","year":"2007","journal-title":"Mol Biochem Parasitol"},{"issue":"2","key":"2026051510120175600_fcag150-B12","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1111\/j.1365-2990.2006.00777.x","article-title":"Cerebral calpain in fatal falciparum malaria","volume":"33","author":"Medana","year":"2007","journal-title":"Neuropathol Appl Neurobiol"},{"issue":"2","key":"2026051510120175600_fcag150-B13","doi-asserted-by":"crossref","first-page":"108","DOI":"10.1016\/j.neuint.2005.09.001","article-title":"Activation of calpains, calpastatin and spectrin cleavage in the brain during the pathology of fatal murine cerebral malaria","volume":"48","author":"Shukla","year":"2006","journal-title":"Neurochem Int"},{"issue":"3","key":"2026051510120175600_fcag150-B14","doi-asserted-by":"crossref","first-page":"940","DOI":"10.1016\/S0006-291X(03)00447-9","article-title":"Calpain is involved in the HIV replication from the latently infected OM10.1 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(SCA3)","volume":"22","author":"H\u00fcbener","year":"2013","journal-title":"Hum Mol Genet"},{"issue":"5","key":"2026051510120175600_fcag150-B47","doi-asserted-by":"crossref","first-page":"1280","DOI":"10.1093\/brain\/awx039","article-title":"A combinatorial approach to identify calpain cleavage sites in the Machado-Joseph disease protein ataxin-3","volume":"140","author":"Weber","year":"2017","journal-title":"Brain"},{"issue":"26","key":"2026051510120175600_fcag150-B48","doi-asserted-by":"crossref","first-page":"18851","DOI":"10.1074\/jbc.M611914200","article-title":"Calpain inhibition is sufficient to suppress aggregation of polyglutamine-expanded ataxin-3","volume":"282","author":"Haacke","year":"2007","journal-title":"J Biol Chem"},{"issue":"4","key":"2026051510120175600_fcag150-B49","doi-asserted-by":"crossref","first-page":"555","DOI":"10.1093\/hmg\/ddi472","article-title":"Proteolytic cleavage of polyglutamine-expanded ataxin-3 is critical for aggregation and sequestration of 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