{"entity": "researcher", "timestamp": "2026-08-14T12:39:57.193Z", "family": "Oldfors", "given": "Anders", "initials": "A", "orcid": "0000-0002-5758-7397", "affiliations": ["Department of Laboratory Medicine, University of Gothenburg, Gothenburg, Sweden."], "links": {"self": {"href": "https://publications.scilifelab.se/researcher/e82034663f6647cd9827871bfca633ef.json"}, "display": {"href": "https://publications.scilifelab.se/researcher/e82034663f6647cd9827871bfca633ef"}}, "publications": [{"entity": "publication", "iuid": "36d5252e331c487cb68d957705e9c9f6", "links": {"self": {"href": "https://publications.scilifelab.se/publication/36d5252e331c487cb68d957705e9c9f6.json"}, "display": {"href": "https://publications.scilifelab.se/publication/36d5252e331c487cb68d957705e9c9f6"}}, "title": "Proteomic profiling of polyglucosan bodies associated with glycogenin-1 deficiency in skeletal muscle.", "authors": [{"family": "Visuttijai", "given": "Kittichate", "initials": "K", "orcid": "0000-0002-4800-8533", "researcher": {"href": "https://publications.scilifelab.se/researcher/f41f59ad2b0a4e1c95b0cc9cf109f6fa.json"}}, {"family": "Hedberg-Oldfors", "given": "Carola", "initials": "C", "orcid": "0000-0002-7141-4185", "researcher": {"href": "https://publications.scilifelab.se/researcher/dc67028bf0c04f1b9a73bac5e72f9897.json"}}, {"family": "Costello", "given": "Daniel J", "initials": "DJ", "orcid": "0000-0001-6023-8246", "researcher": {"href": "https://publications.scilifelab.se/researcher/07dfb1d34e394b07bf029fe1cfff028f.json"}}, {"family": "Bermingham", "given": "Niamh", "initials": "N"}, {"family": "Oldfors", "given": "Anders", "initials": "A", "orcid": "0000-0002-5758-7397", "researcher": {"href": "https://publications.scilifelab.se/researcher/e82034663f6647cd9827871bfca633ef.json"}}], "type": "journal article", "published": "2024-06-00", "journal": {"title": "Neuropathol Appl Neurobiol", "issn": "1365-2990", "volume": "50", "issue": "3", "pages": "e12995", "issn-l": null}, "abstract": "Polyglucosan storage disorders represent an emerging field within neurodegenerative and neuromuscular conditions, including Lafora disease (EPM2A, EPM2B), adult polyglucosan body disease (APBD, GBE1), polyglucosan body myopathies associated with RBCK1 deficiency (PGBM1, RBCK1) or glycogenin-1 deficiency (PGBM2, GYG1). While the storage material primarily comprises glycans, this study aimed to gain deeper insights into the protein components by proteomic profiling of the storage material in glycogenin-1 deficiency.\n\nWe employed molecular genetic analyses, quantitative mass spectrometry of laser micro-dissected polyglucosan bodies and muscle homogenate, immunohistochemistry and western blot analyses in muscle tissue from a 45-year-old patient with proximal muscle weakness from late teenage years due to polyglucosan storage myopathy.\n\nThe muscle tissue exhibited a complete absence of glycogenin-1 due to a novel homozygous deep intronic variant in GYG1 (c.7+992T>G), introducing a pseudo-exon causing frameshift and a premature stop codon. Accumulated proteins in the polyglucosan bodies constituted components of glycogen metabolism, protein quality control pathways and desmin. Muscle fibres containing polyglucosan bodies frequently exhibited depletion of normal glycogen.\n\nThe absence of glycogenin-1, a protein important for glycogen synthesis initiation, causes storage of polyglucosan that displays accumulation of several proteins, including those essential for glycogen synthesis, sequestosome 1/p62 and desmin, mirroring findings in RBCK1 deficiency. These results suggest shared pathogenic pathways across different diseases exhibiting polyglucosan storage. Such insights have implications for therapy in these rare yet devastating and presently untreatable disorders.", "doi": "10.1111/nan.12995", "pmid": "38923610", "labels": {"Clinical Genomics Gothenburg": "Service", "Integrated Microscopy Technologies Gothenburg": "Service", "Glycoproteomics and MS Proteomics": "Service", "Clinical Genomics": "Service"}, "xrefs": [], "notes": [], "created": "2024-11-01T08:17:11.069Z", "modified": "2024-11-27T15:36:56.743Z"}, {"entity": "publication", "iuid": "c836a1ebbd1e43cd802e84c5d141e527", "links": {"self": {"href": "https://publications.scilifelab.se/publication/c836a1ebbd1e43cd802e84c5d141e527.json"}, "display": {"href": "https://publications.scilifelab.se/publication/c836a1ebbd1e43cd802e84c5d141e527"}}, "title": "Inclusion body myositis with early onset: a population-based study.", "authors": [{"family": "Lindgren", "given": "Ulrika", "initials": "U", "orcid": "0000-0002-3474-4492", "researcher": {"href": "https://publications.scilifelab.se/researcher/b843f1fe15914626a4eb09a2b0abfe82.json"}}, {"family": "Hedberg-Oldfors", "given": "Carola", "initials": "C", "orcid": "0000-0002-7141-4185", "researcher": {"href": "https://publications.scilifelab.se/researcher/dc67028bf0c04f1b9a73bac5e72f9897.json"}}, {"family": "Pullerits", "given": "Rille", "initials": "R", "orcid": "0000-0002-5383-9817", "researcher": {"href": "https://publications.scilifelab.se/researcher/a731c41419924b259d32139f0efecbbd.json"}}, {"family": "Lindberg", "given": "Christopher", "initials": "C", "orcid": "0000-0002-2254-3597", "researcher": {"href": "https://publications.scilifelab.se/researcher/469ad301df334405b66a09b63f74641e.json"}}, {"family": "Oldfors", "given": "Anders", "initials": "A", "orcid": "0000-0002-5758-7397", "researcher": {"href": "https://publications.scilifelab.se/researcher/e82034663f6647cd9827871bfca633ef.json"}}], "type": "journal article", "published": "2023-11-00", "journal": {"title": "J. Neurol.", "issn": "1432-1459", "volume": "270", "issue": "11", "pages": "5483-5492", "issn-l": "0340-5354"}, "abstract": "Inclusion body myositis (IBM), an inflammatory myopathy with progressive weakness without efficient treatment, typically presents after 45 years of age and younger patients are sparsely studied.\n\nIn a population-based study during a 33-year period, 142 patients with IBM were identified in western Sweden. Six patients fell outside the European Neuromuscular Centre 2011 criteria for IBM due to young age at symptom onset, verified by a muscle biopsy < 50 years of age. These were defined as early-onset IBM and included in this study. Medical records, muscle strength, comorbidities, muscle biopsies, and nuclear- and mitochondrial DNA were examined and compared with patients with IBM and age matched controls from the same population.\n\nThe median age at symptom onset was 36 (range 34-45) years and at diagnosis 43 (range 38-58) years. Four patients were deceased at a median age of 59 (range 50-75) years. The median survival from diagnosis was 14 (range 10-18) years. The prevalence December 31 2017 was 1.2 per million inhabitants and the mean incidence 0.12 patients per million inhabitants and year. The mean decline in quadriceps strength \u00b1 1 standard deviation was 1.21 \u00b1 0.2 Newton or 0.91 \u00b1 0.2% per month and correlated to time from diagnosis (p < 0.001). Five patients had swallowing difficulties. All patients displayed mitochondrial changes in muscle including cytochrome c oxidase deficiency and the mitochondrial DNA mutation load was high.\n\nEarly-onset IBM is a severe disease, causing progressive muscle weakness, high muscle mitochondrial DNA mutation load and a reduced cumulative survival in young and middle-aged individuals.", "doi": "10.1007/s00415-023-11878-w", "pmid": "37498322", "labels": {"Clinical Genomics Gothenburg": "Service", "Clinical Genomics": "Service"}, "xrefs": [{"db": "pmc", "key": "PMC10576680"}, {"db": "pii", "key": "10.1007/s00415-023-11878-w"}], "notes": [], "created": "2023-11-30T22:35:04.436Z", "modified": "2023-11-30T22:35:04.547Z"}, {"entity": "publication", "iuid": "3d784932a3d947f999ea5ca837c358d2", "links": {"self": {"href": "https://publications.scilifelab.se/publication/3d784932a3d947f999ea5ca837c358d2.json"}, "display": {"href": "https://publications.scilifelab.se/publication/3d784932a3d947f999ea5ca837c358d2"}}, "title": "Proteomic characterisation of polyglucosan bodies in skeletal muscle in RBCK1 deficiency.", "authors": [{"family": "Thomsen", "given": "Christer", "initials": "C", "orcid": "0000-0001-5416-552X", "researcher": {"href": "https://publications.scilifelab.se/researcher/2ba5b39b720d44e386085fc0e67be556.json"}}, {"family": "Malfatti", "given": "Edoardo", "initials": "E"}, {"family": "Jovanovic", "given": "Ana", "initials": "A"}, {"family": "Roberts", "given": "Mark", "initials": "M"}, {"family": "Kalev", "given": "Ognian", "initials": "O"}, {"family": "Lindberg", "given": "Christopher", "initials": "C"}, {"family": "Oldfors", "given": "Anders", "initials": "A", "orcid": "0000-0002-5758-7397", "researcher": {"href": "https://publications.scilifelab.se/researcher/e82034663f6647cd9827871bfca633ef.json"}}], "type": "journal article", "published": "2022-02-00", "journal": {"title": "Neuropathol Appl Neurobiol", "issn": "1365-2990", "volume": "48", "issue": "1", "pages": "e12761", "issn-l": null}, "abstract": "Several neurodegenerative and neuromuscular disorders are characterised by storage of polyglucosan, consisting of proteins and amylopectin-like polysaccharides, which are less branched than in normal glycogen. Such diseases include Lafora disease, branching enzyme deficiency, glycogenin-1 deficiency, polyglucosan body myopathy type 1 (PGBM1) due to RBCK1 deficiency and others. The protein composition of polyglucosan bodies is largely unknown.\n\nWe combined quantitative mass spectrometry, immunohistochemical and western blot analyses to identify the principal protein components of polyglucosan bodies in PGBM1. Histologically stained tissue sections of skeletal muscle from four patients were used to isolate polyglucosan deposits and control regions by laser microdissection. Prior to mass spectrometry, samples were labelled with tandem mass tags that enable quantitative comparison and multiplexed analysis of dissected samples. To study the distribution and expression of the accumulated proteins, immunohistochemical and western blot analyses were performed.\n\nAccumulated proteins were mainly components of glycogen metabolism and protein quality control pathways. The majority of fibres showed depletion of glycogen and redistribution of key enzymes of glycogen metabolism to the polyglucosan bodies. The polyglucosan bodies also showed accumulation of proteins involved in the ubiquitin-proteasome and autophagocytosis systems and protein chaperones.\n\nThe sequestration of key enzymes of glycogen metabolism to the polyglucosan bodies may explain the glycogen depletion in the fibres and muscle function impairment. The accumulation of components of the protein quality control systems and other proteins frequently found in protein aggregate disorders indicates that protein aggregation may be an essential part of the pathobiology of polyglucosan storage.", "doi": "10.1111/nan.12761", "pmid": "34405429", "labels": {"Clinical Genomics Gothenburg": "Service", "Integrated Microscopy Technologies Gothenburg": "Service", "Glycoproteomics and MS Proteomics": "Service", "Clinical Genomics": "Service"}, "xrefs": [], "notes": [], "created": "2022-12-02T12:22:17.396Z", "modified": "2024-01-16T13:46:29.630Z"}, {"entity": "publication", "iuid": "5bd96c5ba07a441284381c33d5ac429b", "links": {"self": {"href": "https://publications.scilifelab.se/publication/5bd96c5ba07a441284381c33d5ac429b.json"}, "display": {"href": "https://publications.scilifelab.se/publication/5bd96c5ba07a441284381c33d5ac429b"}}, "title": "The localization of amyloid precursor protein to ependymal cilia in vertebrates and its role in ciliogenesis and brain development in zebrafish.", "authors": [{"family": "Chebli", "given": "Jasmine", "initials": "J", "orcid": "0000-0003-0791-3198", "researcher": {"href": "https://publications.scilifelab.se/researcher/0b0dd51631ce4c3c89a98b9d6c7d3d35.json"}}, {"family": "Rahmati", "given": "Maryam", "initials": "M"}, {"family": "Lashley", "given": "Tammaryn", "initials": "T", "orcid": "0000-0001-7389-0348", "researcher": {"href": "https://publications.scilifelab.se/researcher/533fe74a716840b2a55fddf0452f2a23.json"}}, {"family": "Edeman", "given": "Brigitta", "initials": "B"}, {"family": "Oldfors", "given": "Anders", "initials": "A", "orcid": "0000-0002-5758-7397", "researcher": {"href": "https://publications.scilifelab.se/researcher/e82034663f6647cd9827871bfca633ef.json"}}, {"family": "Zetterberg", "given": "Henrik", "initials": "H", "orcid": "0000-0003-3930-4354", "researcher": {"href": "https://publications.scilifelab.se/researcher/85efee74eb4a4b38b63cf2823d204529.json"}}, {"family": "Abramsson", "given": "Alexandra", "initials": "A", "orcid": "0000-0002-4715-9225", "researcher": {"href": "https://publications.scilifelab.se/researcher/7abde12dab2e4d338bc6e55933f07531.json"}}], "type": "journal article", "published": "2021-09-27", "journal": {"title": "Sci Rep", "issn": "2045-2322", "volume": "11", "issue": "1", "pages": "19115", "issn-l": "2045-2322"}, "abstract": "Amyloid precursor protein (APP) is expressed in many tissues in human, mice and in zebrafish. In zebrafish, there are two orthologues, Appa and Appb. Interestingly, some cellular processes associated with APP overlap with cilia-mediated functions. Whereas the localization of APP to primary cilia of in vitro-cultured cells has been reported, we addressed the presence of APP in motile and in non-motile sensory cilia and its potential implication for ciliogenesis using zebrafish, mouse, and human samples. We report that Appa and Appb are expressed by ciliated cells and become localized at the membrane of cilia in the olfactory epithelium, otic vesicle and in the brain ventricles of zebrafish embryos. App in ependymal cilia persisted in adult zebrafish and was also detected in mouse and human brain. Finally, we found morphologically abnormal ependymal cilia and smaller brain ventricles in appa-/-appb-/- mutant zebrafish. Our findings demonstrate an evolutionary conserved localisation of APP to cilia and suggest a role of App in ciliogenesis and cilia-related functions.", "doi": "10.1038/s41598-021-98487-7", "pmid": "34580355", "labels": {"Integrated Microscopy Technologies Gothenburg": "Service"}, "xrefs": [{"db": "pmc", "key": "PMC8476544"}, {"db": "pii", "key": "10.1038/s41598-021-98487-7"}], "notes": [], "created": "2023-02-16T08:14:17.553Z", "modified": "2023-02-16T08:14:17.703Z"}]}