Search results for "protein aggregation"

Protein aggregate myopathies.

2006

Protein aggregate myopathies (PAMs) based on the morphologic phenomenon of aggregation of proteins within muscle fibers may occur in children (selenoproteinopathies, actinopathies, and myosinopathies) or adults (certain myofibrillar myopathies and myosinopathies). They may be mutation related, which includes virtually all childhood forms but certain other forms as well, or sporadic, which are largely seen in adults. Their classification as myofibrillar or desmin-related myopathies, actinopathies, or myosinopathies is based on the identification of respective mutant proteins, most of them components of the sarcomeres. Recognition of PAM requires muscle biopsy and an extensive immunohistochem…

Congenital myopathies at their molecular dawning

2003

The introduction and application of molecular techniques have commenced to influence and alter the nosology of congenital myopathies. Long-known entities such as nemaline myopathies, core diseases, and desmin-related myopathies have now been found to be caused by unequivocal mutations. Several of these mutations and their genes have been identified by analyzing aggregates of proteins within muscle fibers as a morphological hallmark as in desminopathy and actinopathy, the latter a subtype among the nemaline myopathies. Immunohistochemistry has played a crucial role in recognizing this new group of protein aggregate myopathies within the spectrum of congenital myopathies. It is to be expected…

Protein Aggregation in Muscle Fibers and Respective Neuromuscular Disorders

2007

Protein aggregation in muscle fibers may be a nonspecific phenomenon such as occurring in cores or ragged red fibers. However, it may also be a disease-specific and disease-significant phenomenon constituting protein aggregate myopathies (PAMs). These may be divided into two classes: The first one is marked by impaired extralysosomal degradation of proteins, catabolic PAM, encompassing desmin-related myopathies. Mutant proteins, that is, desmin, myotilin, or α-B crystallin, defy protein degradation, aggregate and associate with other proteins within muscle fibers, hence marking desminopathies, myotilinopathies, and α-B crystallinopathies. A second class of PAM encompasses those apparently a…

Glial and neuronal expression of polyglutamine proteins induce behavioral changes and aggregate formation inDrosophila

2004

Patients with polyglutamine expansion diseases, like Huntington's disease or several spinocerebellar ataxias, first present with neurological symptoms that can occur in the absence of neurodegeneration. Behavioral symptoms thus appear to be caused by neuronal dysfunction, rather than cell death. Pathogenesis in polyglutamine expansion diseases is largely viewed as a cell-autonomous process in neurons. It is likely, however, that this process is influenced by changes in glial physiology and, at least in the case of DRPLA glial inclusions and glial cell death, seems to be an important part in the pathogenesis. To investigate these aspects in a Drosophila model system, we expressed polyglutami…

Nucleation mechanisms and spatial hetereogeneity in insulin amyloid fibrils formation

2008

P53 Aggregates and Interacts with Tau in Alzheimer's Disease

2020

Molecular mechanisms linking amyloid β toxicity and Tau hyperphosphorylation in Alzheimer׳s disease

2015

Neurofibrillary tangles (aggregates of cytoskeletal Tau protein) and senile plaques (aggregates mainly formed by amyloid β peptide) are two landmark lesions in Alzheimer׳s disease. Some researchers have proposed tangles, whereas others have proposed plaques, as primary lesions. For a long time, these were thought of as independent mechanisms. However, experimental evidence suggests that both lesions are intimately related. We review here some molecular pathways linking amyloid β and Tau toxicities involving, among others, glycogen synthase kinase 3β, p38, Pin1, cyclin-dependent kinase 5, and regulator of calcineurin 1. Understanding amyloid β and Tau toxicities as part of a common pathophys…

156th ENMC International Workshop: desmin and protein aggregate myopathies, 9-11 November 2007, Naarden, The Netherlands.

2008

121st ENMC International Workshop on Desmin and Protein Aggregate Myopathies. 7–9 November 2003, Naarden, The Netherlands

2004

The 121st European Neuromuscular Centre (ENMC)sponsored International Workshop on ‘DESMIN and Protein Aggregate Myopathies’, attended by 16 active participants from France, Germany, Poland, Spain, Sweden, the United Kingdom and the USA, was actually the fourth one in a row addressing the pathology of the muscle fibre intermediate filament desmin, its associated and similar diseases, all four [1–3] organized by Michel Fardeau and Hans H. Goebel. In his introduction, the chairman, Hans H. Goebel (Mainz), recorded the evolution of ‘Protein Aggregate Myopathies (PAM)’ which are marked by the accumulation of diverse proteins within muscle fibres as a morphologic hallmark in separate myopathies w…

Primary desminopathies.

2007

•  Introduction •  Desmin is an essential component of the extrasarcomeric cytoskeleton in striated muscle cells •  Distal myopathy,cardiac arrhythmias,cardiomyopathy:classical criteria of primary desminopathies •  Sub-sarcolemmal and cytoplasmic desmin-positive protein aggregates:the morphological hallmark of primary and secondary desminopathies •  The spectrum of pathogenic desmin gene mutations •  The molecular pathogenesis of primary desminopathies: some answers gained,but even more questions raised •  Diagnostic work-up to distinguish primary from secondary desminopathies •  Treatment and clinical management of primary desminopathy patients Abstract Mutations of the human desmin gene o…