Results 11 to 20 of about 5,143 (201)

A Novel Dysferlin-Binding Kinase CK2α Promotes Plasma Membrane Repair in Dysferlinopathy. [PDF]

FASEB J
When the cell membrane is injured, extracellular calcium enters the cell, triggering the accumulation of dysferlin at the lesion site. In the presence of dysferlin, CK2 is efficiently recruited to the damaged membrane and maintains its kinase activity through interaction with dysferlin.
Nakamura N, Suzuki N, Kanno SI, Yamanaka R, Ono H, Izumi R, Muliang R, Borgo C, Ohno A, Harada R, Saito S, Funayama Y, Ikeda K, Mitsuzawa S, Watanabe Y, Shijo T, Akiyama T, Takahashi T, Kanzaki M, Osana S, Warita H, Aoki Y, Ebihara S, Salvi M, Nagatomi R, Yasui A, Miyake K, Aoki M.   +27 more
europepmc   +2 more sources

Enhancing the Performance of a Blood-Based Diagnostic Screening Tool for Dysferlinopathy: Optimising an Immunoassay Across Continents. [PDF]

Neuropathol Appl Neurobiol
We validated an immunohistochemical method for detecting dysferlin in neutrophils from peripheral blood films (PBFs), offering a minimally invasive alternative to muscle biopsy. In an Indian cohort, the assay showed 100% sensitivity. Specificity depended on sample quality and storage conditions.
D'Este G, Cox D, Maistrello L, Emmons SS, Gaitonde P, Dastur R, Barresi R.   +6 more
europepmc   +2 more sources

Comprehensive Profiling of Annexins in Neuromuscular Disorders Reveals a Unique Signature in Dysferlinopathy. [PDF]

Eur J Neurol
Muscle biopsies from patients across eight neuromuscular disorders and healthy controls were analyzed using immunofluorescence (IF) and immunoblot (WB) to evaluate the expression and localization of seven annexin proteins (A1, A2, A4, A5, A6, A7, A11).
He QF, Lin YH, Zheng ZL, Zeng MH, Lin X, Liu XY, Kang-Yang, Zhang QI, Lin MT, Wang N, Wang ZQ, Lin F.   +11 more
europepmc   +2 more sources

Contribution of dysferlin deficiency to skeletal muscle pathology in asymptomatic and severe dystroglycanopathy models: generation of a new model for Fukuyama congenital muscular dystrophy. [PDF]

PLoS ONE, 2014
Defects in dystroglycan glycosylation are associated with a group of muscular dystrophies, termed dystroglycanopathies, that include Fukuyama congenital muscular dystrophy (FCMD). It is widely believed that abnormal glycosylation of dystroglycan leads to
Motoi Kanagawa, Zhongpeng Lu, Chiyomi Ito, Chie Matsuda, Katsuya Miyake, Tatsushi Toda   +5 more
doaj   +1 more source

Myopathy With Exercise-Induced Intolerance due to Novel Biallelic Variants in OBSCN-A Clinical, Morphological and Molecular Analysis. [PDF]

Neuropathol Appl Neurobiol
The phenotype of OBSCN variants consists of exercise intolerance ranging from myalgia and cramps to rhabdomyolysis. Symptoms are mainly induced by high‐intensity sports. Molecular analysis showing a deregulation of muscle processes associated with Ca2+ regulation, extrasarcolemmal integrity and autophagy emphasised the critical role of obscurin in ...
Krämer-Best HH, Reis MC, Hentschel A, Weiß M, Schaiter A, Böhm KD, Roos A, Nolte D, Schänzer A.   +8 more
europepmc   +2 more sources

High-Density Lipoprotein-Associated Cholesterol Abnormalities in a Clinical Outcomes Study of Dysferlin-Deficient Limb-Girdle Muscular Dystrophy Type R2. [PDF]

J Cachexia Sarcopenia Muscle
ABSTRACT Background Limb–girdle muscular dystrophy (MD) type R2 (LGMDR2, formerly LGMD2B) is an autosomal recessive form of MD caused by variants in the dysferlin gene, DYSF. It leads to slow proximal and distal muscle weakening that generally results in loss of ambulation around early adulthood but without the lethal cardiorespiratory dysfunction ...
White Z, Rufibach L, Dressman HG, Hilsden H, Cox D, Spuler S, Day JW, Jones KJ, Bharucha-Goebel DX, Salort-Campana E, Pestronk A, Walter MC, Paradas C, Stojkovic T, Mori-Yoshimura M, Bravver E, Diaz-Manera J, Pegoraro E, Mendell JR, Jain COS Consortium, Straub V, Bernatchez P.   +21 more
europepmc   +2 more sources

Proteomic analysis of the dysferlin protein complex unveils its importance for sarcolemmal maintenance and integrity. [PDF]

PLoS ONE, 2010
Dysferlin is critical for repair of muscle membranes after damage. Mutations in dysferlin lead to a progressive muscular dystrophy. Recent studies suggest additional roles for dysferlin.
Antoine de Morrée, Paul J Hensbergen, Herman H H B M van Haagen, Irina Dragan, André M Deelder, Peter A C 't Hoen, Rune R Frants, Silvère M van der Maarel   +7 more
doaj   +1 more source

Effect of Dysferlin Deficiency on Atherosclerosis and Plasma Lipoprotein Composition Under Normal and Hyperlipidemic Conditions

Frontiers in Physiology, 2021
Dysferlinopathies are a group of muscle disorders caused by mutations to dysferlin, a transmembrane protein involved in membrane patching events following physical damage to skeletal myofibers.
Zoe White, Zoe White, Nadia Milad, Nadia Milad, Stephanie L. Sellers, Stephanie L. Sellers, Pascal Bernatchez, Pascal Bernatchez   +7 more
doaj   +1 more source

Dysferlin forms a dimer mediated by the C2 domains and the transmembrane domain in vitro and in living cells. [PDF]

PLoS ONE, 2011
Dysferlin was previously identified as a key player in muscle membrane repair and its deficiency leads to the development of muscular dystrophy and cardiomyopathy. However, little is known about the oligomerization of this protein in the plasma membrane.
Li Xu, Sandeep Pallikkuth, Zhanjia Hou, Gregory A Mignery, Seth L Robia, Renzhi Han   +5 more
doaj   +1 more source

Modular Dispensability of Dysferlin C2 Domains Reveals Rational Design for Mini-dysferlin Molecules [PDF]

Journal of Biological Chemistry, 2012
Dysferlin is a large transmembrane protein composed of a C-terminal transmembrane domain, two DysF domains, and seven C2 domains that mediate lipid- and protein-binding interactions. Recessive loss-of-function mutations in dysferlin lead to muscular dystrophies, for which no treatment is currently available.
Azakir, B. A., Di Fulvio, S., Salomon, S., Brockhoff, M., Therrien, C., Sinnreich, M.   +5 more
openaire   +6 more sources