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Valosin-containing protein (VCP) associated multisystem proteinopathy (MSP) is a rare inherited disorder with a reported incidence of 0.66/100,000 based on population data from the UK. VCP-associated MSP may result in multisystem involvement of varying presentations and phenotypes including inclusion body myopathy, Paget's disease of bone, frontotemporal dementia, parkinsonism, and amyotrophic lateral sclerosis, among others. An international multidisciplinary consortium of 50+ experts in neuromuscular disease, dementia, psychology, cardiology, pulmonology, physical therapy, occupational therapy, speech and language pathology, nutrition, genetics, and endocrinology were convened by the patient advocacy organization, Cure VCP Disease, in 2021 to elicit collaboration and development of a standard of care for this rare and under-diagnosed disease.
Source: Neuromuscular Disorders - Category: Neurology Authors: Source Type: research

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VCP disease is a rare, autosomal dominant disorder and includes combinations of hereditary Inclusion Body Myopathy (h-IBM), Paget's Disease of Bone (PDB), Frontotemporal Dementia (FTD) and amyotrophic lateral sclerosis (ALS). The disease is caused by mutations in the VCP gene located at 9p13 - p12 that encodes valosin-containing protein. VCP is a hexameric protein of the AAA (ATPases associated with diverse cellular activities) family that interacts with several cofactors and facilitates the degradation of polyubiquitylated substrates in the proteasome, endoplasmic reticulum or autophagy [1].
Source: Neuromuscular Disorders - Category: Neurology Authors: Source Type: research
Abstract p97, also known as valosin-containing protein or CDC48, is a member of the AAA+ protein family that is highly conserved in eukaryotes. It binds to various cofactors in the body to perform its protein-unfolding function and participates in DNA repair, degradation of subcellular membrane proteins, and protein quality control pathways, among other processes. Its malfunction can lead to many diseases, such as inclusion body myopathy, associated with Paget's disease of bone and/or frontotemporal dementia, amyotrophic lateral sclerosis disease, and others. In recent years, many small molecule inhibitors have be...
Source: Current Medicinal Chemistry - Category: Chemistry Authors: Tags: Curr Med Chem Source Type: research
s MH, Vorgerd M, Eichinger L, Schröder R Abstract Heterozygous missense mutations in the human VCP gene cause inclusion body myopathy associated with Paget disease of bone and fronto-temporal dementia (IBMPFD) and amyotrophic lateral sclerosis (ALS). The exact molecular mechanisms by which VCP mutations cause disease manifestation in different tissues are incompletely understood. In the present study, we report the comprehensive analysis of a newly generated R155C VCP knock-in mouse model, which expresses the ortholog of the second most frequently occurring human pathogenic VCP mutation. Heterozygous R155C VC...
Source: Biochemical and Biophysical Research communications - Category: Biochemistry Authors: Tags: Biochem Biophys Res Commun Source Type: research
t S Abstract VCP/p97 (valosin containing protein) is a key regulator of cellular proteostasis. It orchestrates protein turnover and quality control in vivo, processes fundamental for proper cell function. In humans, mutations in VCP lead to severe myo- and neuro-degenerative disorders such as inclusion body myopathy with Paget disease of the bone and frontotemporal dementia (IBMPFD), amyotrophic lateral sclerosis (ALS) or and hereditary spastic paraplegia (HSP). We analyzed here the in vivo role of Vcp and its novel interactor Washc4/Swip (WASH complex subunit 4) in the vertebrate model zebrafish (Danio rerio). We...
Source: Autophagy - Category: Cytology Authors: Tags: Autophagy Source Type: research
Le Ber I Abstract Valosin-containing protein (VCP) mutations are rare causes of autosomal dominant frontotemporal dementias associated with Paget's disease of bone, inclusion body myopathy, and amyotrophic lateral sclerosis. We analyzed the VCP gene in a cohort of 199 patients with frontotemporal dementia and identified 7 heterozygous mutations in unrelated families, including 3 novel mutations segregating with dementia. This expands the VCP mutation spectrum and suggests that although VCP mutations are rare (3.5% in this study), the gene should be analyzed even in absence of the full syndromic complex. Reporting...
Source: Neurobiology of Aging - Category: Geriatrics Authors: Tags: Neurobiol Aging Source Type: research
Inclusion Body Myopathy (IBM) associated with Paget's disease of the bone (PDB) and/or frontotemporal dementia (FTD) or Multisystem Proteinopathy (OMIM 167320) or more commonly called IBMPFD or VCP disease, was first reported by Kimonis et al. (2000) [1]. VCP disease comprises other less common phenotypes including amyotrophic lateral sclerosis (ALS), Parkinson's disease, cardiomyopathy, sensory motor axonal neuropathy, and sphincter disturbance [2 –6]. IBMPFD is an underdiagnosed disease that has been reported in greater than 100 families worldwide, but is more commonly found in the United States and Europe.
Source: Neuromuscular Disorders - Category: Neurology Authors: Source Type: research
Valosin-containing protein (VCP) is a ubiquitous protein, being broadly expressed in several human body systems [1]. More than 45 missense mutations in the VCP gene have been associated with several disease conditions, collectively known as ‘multisystem proteinopathies’: these include early-onset Paget disease of the bone (PDB), myopathy with rimmed vacuoles or inclusion body myopathy (IBM), frontotemporal dementia (FTD), and amyotrophic lateral sclerosis (ALS) [2, 3].. Myopathy is the most common clinical feature of these conditio ns, mainly affecting proximal muscles.
Source: Journal of the Neurological Sciences - Category: Neurology Authors: Tags: Letter to the Editor Source Type: research
CONCLUSIONS: hnRNPA3 pathology was identified in motor neurons of ALS patients with C9orf72 repeat expansions, implicating hnRNPA3 in the pathogenesis of C9orf72-linked ALS. hnRNPA3 warrants further investigation into the pathogenesis of ALS linked to C9orf72. This study also determined that HNRNP mutations are not a common cause of FALS and SALS in Australia. PMID: 29131108 [PubMed - as supplied by publisher]
Source: Neuro-Degenerative Diseases - Category: Neurology Authors: Tags: Neurodegener Dis Source Type: research
Conclusions: hnRNPA3 pathology was identified in motor neurons of ALS patients with C9orf72 repeat expansions, implicating hnRNPA3 in the pathogenesis ofC9orf72-linked ALS. hnRNPA3 warrants further investigation into the pathogenesis of ALS linked toC9orf72. This study also determined thatHNRNP mutations are not a common cause of FALS and SALS in Australia.Neurodegener Dis 2017;17:304-312
Source: Neurodegenerative Diseases - Category: Neurology Source Type: research
Publication date: Available online 21 September 2017 Source:Journal of Genetics and Genomics Author(s): Dwayne J. Byrne, Mark J. Harmon, Jeremy C. Simpson, Craig Blackstone, Niamh C. O'Sullivan The VCP-Ufd1-Npl4 complex regulates proteasomal processing within cells by delivering ubiquitinated proteins to the proteasome for degradation. Mutations in VCP are associated with two neurodegenerative diseases, amyotrophic lateral sclerosis (ALS) and inclusion body myopathy with Paget's disease of the bone and frontotemporal dementia (IBMPFD), and extensive study has revealed crucial functions of VCP within neurons. By contrast, ...
Source: Journal of Genetics and Genomics - Category: Genetics & Stem Cells Source Type: research
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