Diseases of Muscle and the Neuromuscular Junction
John W. Scadding, Nicholas A. Losseff in Clinical Neurology, 2011
There are six types of Emery–Dreifuss muscular dystrophy (EDMD). The classic form, or Emery–Dreifuss muscular dystrophy type 1 is linked to Xq28, the STA gene, whose product is called emerin. This is a 34-kDa protein, which is ubiquitously expressed at the nuclear membrane, but the precise function of which remains unclear. Antibodies are available to emerin and a mutation in the emerin gene usually leads to loss of immunoreactivity. The diagnosis of Emery–Dreifuss muscular dystrophy may be made by observing the absence of immunostaining for emerin protein in peripheral whole blood cells or muscle biopsy.
Neuromuscular disorders
Angus Clarke, Alex Murray, Julian Sampson in Harper's Practical Genetic Counselling, 2019
This is often X-linked, determined by a specific gene for the protein ‘emerin’, allowing specific mutation testing in some families. Affected males and some carrier females are at risk of serious cardiac conduction defects, even though weakness is often mild. Some clinically similar families follow autosomal dominant inheritance, and the disorder is due to defects in the gene LMNA, encoding the muscle proteins lamin A and lamin C. This is an unusual gene in which mutations can cause a very wide range of different phenotypes including lipodystrophy and progeria as well as muscular dystrophy.
Muscular Dystrophy Diseases
Maher Kurdi in Neuromuscular Pathology Made Easy, 2021
CMD group 1, Bethlem myopathy and Emery-Dreifuss dystrophy (EDD) all share slightly similar clinical and morphological features in muscle biopsy. However, EDD is commonly associated with joint contracture. Several variants with different inheritance patterns are categorized under EDD (Table 16.1). Because the pathological features of EDD resemble all types of muscular dystrophies, IHC is considered the best differential tool to detect the protein deficiency. Emerin and lamin are commercially available antibodies and their sensitivity and specificity are high (Figure 16.4).
What can we learn from senescent platelets, their transcriptomes and proteomes?
Published in Platelets, 2023
Harriet E. Allan, Ami Vadgama, Paul C. Armstrong, Timothy D. Warner
Against a background of protein loss, a number of cytoskeletal-associated proteins such as Emerin, Gelsolin and Twinfilin-2 were lost to a greater extent.5 This accelerated loss of cytoskeletal proteins is of particular interest as the cytoskeleton is fundamental during platelet activation and its rearrangement underpins all stages of adhesion and aggregation. Furthermore, a platelet-specific knockout mouse model of Twinfilin-2a showed an increase in platelet turnover, suggesting that the cytoskeleton and associated proteins are important in determining platelet life span.48 In addition, aged platelets also have a significant reduction in mitochondrial-associated proteins, suggesting that platelet aging may be accompanied by changes in metabolism.5 Consistent with a loss of organelles in aged platelets, a number of proteins traditionally associated with the endoplasmic reticulum and Golgi apparatus including Reticulon-1, Inverted Formin-2 and Extended Synaptotagmin-1 were found to be reduced in aged platelets, indicating their inheritance from precursor megakaryocytes as these structures are largely lacking from platelets.5
Related Knowledge Centers
- Adherens Junction
- Intercalated Disc
- Protein
- Transmembrane Protein
- Cell Nucleus
- Cardiac Muscle
- Skeletal Muscle
- Inner Nuclear Membrane Protein
- Catenin Beta-1
- X-Linked Recessive Inheritance