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Dystroglycan

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https://www.readbyqxmd.com/read/28089719/220th-enmc-workshop-dystroglycan-and-the-dystroglycanopathies-naarden-the-netherlands-27-29-may-2016
#1
Susan C Brown, Steve J Winder
No abstract text is available yet for this article.
December 21, 2016: Neuromuscular Disorders: NMD
https://www.readbyqxmd.com/read/28057052/an-evaluation-of-the-evolution-of-the-gene-structure-of-dystroglycan
#2
Andrea Brancaccio, Josephine C Adams
BACKGROUND: Dystroglycan (DG) is an adhesion receptor complex composed of two non-covalently associated subunits, transcribed from a single gene. The extracellular α-DG is highly and heterogeneously glycosylated and binds with high affinity to laminins, and the transmembrane β-DG binds intracellular dystrophin. Multiple cellular functions have been proposed for DG, notwithstanding that its role in skeletal muscle appears central as demonstrated by both primary and secondary severe muscular dystrophic phenotypes collectively known as dystroglycanopathies...
January 3, 2017: BMC Research Notes
https://www.readbyqxmd.com/read/28049646/intermediate-filaments-and-the-plasma-membrane
#3
REVIEW
Jonathan C R Jones, Chen Yuan Kam, Robert M Harmon, Alexandra V Woychek, Susan B Hopkinson, Kathleen J Green
A variety of intermediate filament (IF) types show intricate association with plasma membrane proteins, including receptors and adhesion molecules. The molecular basis of linkage of IFs to desmosomes at sites of cell-cell interaction and hemidesmosomes at sites of cell-matrix adhesion has been elucidated and involves IF-associated proteins. However, IFs also interact with focal adhesions and cell-surface molecules, including dystroglycan. Through such membrane interactions, it is well accepted that IFs play important roles in the establishment and maintenance of tissue integrity...
January 3, 2017: Cold Spring Harbor Perspectives in Biology
https://www.readbyqxmd.com/read/28039900/evidence-of-early-defects-in-cajal-retzius-cell-localisation-during-brain-development-in-a-mouse-model-of-dystroglycanopathy
#4
H S Booler, V Pagalday-Vergara, J L Williams, M Hopkinson, S C Brown
AIMS: The secondary dystroglycanopathies represent a heterogeneous group of congenital muscular dystrophies characterised by the defective glycosylation of alpha dystroglycan. These disorders are associated with mutations in at least 17 genes, including Fukutin-related protein (FKRP). At the severe end of the clinical spectrum there is substantial brain involvement, and cobblestone lissencephaly is highly suggestive of these disorders. The precise pathogenesis of this phenotype has however, remained unclear with most attention focused on the disruption to the radial glial scaffold...
December 31, 2016: Neuropathology and Applied Neurobiology
https://www.readbyqxmd.com/read/27999160/25-hydroxycholesterol-inhibition-of-lassa-virus-infection-through-aberrant-gp1-glycosylation
#5
Punya Shrivastava-Ranjan, Éric Bergeron, Ayan K Chakrabarti, César G Albariño, Mike Flint, Stuart T Nichol, Christina F Spiropoulou
: Lassa virus (LASV) infection is a major public health concern due to high fatality rates and limited effective treatment. The interferon-stimulated gene cholesterol 25-hydroxylase (CH25H) encodes an enzyme that catalyzes the production of 25-hydroxycholesterol (25HC). 25HC is involved in regulating cholesterol biosynthesis and has recently been identified as a potent antiviral targeting enveloped virus entry. Here, we show a previously unrecognized role of CH25H in inhibiting LASV glycoprotein glycosylation and the production of infectious virus...
December 20, 2016: MBio
https://www.readbyqxmd.com/read/27977898/expansion-of-divergent-sea-domains-in-cell-surface-proteins-and-nucleoporin-54
#6
Jimin Pei, Nick V Grishin
SEA (sea urchin sperm protein, enterokinase, agrin) domains, many of which possess autoproteolysis activity, have been found in a number of cell surface and secreted proteins. Despite high sequence divergence, SEA domains were also proposed to be present in dystroglycan based on a conserved autoproteolysis motif and receptor-type protein phosphatase IA-2 based on structural similarity. The presence of a SEA domain adjacent to the transmembrane segment appears to be a recurring scheme in quite a number of type I transmembrane proteins on the cell surface, such as MUC1, dystroglycan, IA-2, and Notch receptors...
December 15, 2016: Protein Science: a Publication of the Protein Society
https://www.readbyqxmd.com/read/27964993/laminin-is-instructive-and-calmodulin-dependent-kinase-ii-is-non-permissive-for-the-formation-of-complex-aggregates-of-acetylcholine-receptors-on-myotubes-in-culture
#7
Raphael Vezina-Audette, Mathieu Tremblay, Salvatore Carbonetto
Previous work has shown that myotubes cultured on laminin-coated substrates form complex aggregates of synaptic proteins that are similar in shape and composition to neuromuscular junctions (NMJs). Here we show that laminin instructs the location of complex aggregates which form only on the lower surface when laminin is coated onto culture dishes but over the entire cell when laminin is added in solution. Silencing of myotubes by agents that block electrical activity (tetrodotoxin, verapamil) or by inhibitors of calmodulin dependent kinase (CaMKII) render the myotube permissive for the formation of complex aggregates...
December 10, 2016: Matrix Biology: Journal of the International Society for Matrix Biology
https://www.readbyqxmd.com/read/27932460/protein-o-linked-mannose-%C3%AE-1-4-n-acetylglucosaminyltransferase-2-pomgnt2-is-a-gatekeeper-enzyme-for-functional-glycosylation-of-%C3%AE-dystroglycan
#8
Stephanie M Halmo, Danish Singh, Sneha Patel, Shuo Wang, Melanie Edlin, Geert-Jan Boons, Kelley W Moremen, David Live, Lance Wells
Disruption of the O-mannosylation pathway involved in functional glycosylation of α-dystroglycan gives rise to congenital muscular dystrophies. Protein O-linked mannose β-1,4-N-acetylglucosaminyltransferase 2 (POMGNT2) catalyzes the first step towards the functional matriglycan structure on α-dystroglycan that is responsible for binding extracellular matrix proteins and certain arenaviruses. Alternatively, protein O-linked mannose β-1,2-N-acetylglucosaminyltransferase 1 (POMGNT1) catalyzes the first step towards other various glycan structures present on α-dystroglycan of unknown function...
December 8, 2016: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/27915985/congenital-muscular-dystrophy-1d-causes-matrix-metalloproteinase-activation-and-blood-brain-barrier-impairment
#9
Aryadnne L Schactae, Daphne Plamas, Monique Michels, Jaqueline S Generoso, Tatiana Barichello, Felipe Dal-Pizzol, Mariz Vainzof, Clarissa M Comim
Congenital Muscular Dystrophy type 1D (CMD1D) is characterized by an abnormal glycosylation of α-DG (α-dystroglycan) and associate to central nervous system (CNS) abnormalities such cognitive impairment. The purpose of the research were evaluate the blood-brain barrier permeability (BBB) permeability and matrix metalloproteinases (MMP) -2 and -9 in adult Largemyd-/- mice in order to understand the physiopathology of brain involvement during the CMD1D process. To this aim, we used adult homozygous Largemyd-/- (mutation in Large), heterozygous Largemyd+/- as well as wild-type (C57BL/6) mice...
December 1, 2016: Current Neurovascular Research
https://www.readbyqxmd.com/read/27906078/four-week-rapamycin-treatment-improves-muscular-dystrophy-in-a-fukutin-deficient-mouse-model-of-dystroglycanopathy
#10
Steven J Foltz, Junna Luan, Jarrod A Call, Ankit Patel, Kristen B Peissig, Marisa J Fortunato, Aaron M Beedle
BACKGROUND: Secondary dystroglycanopathies are a subset of muscular dystrophy caused by abnormal glycosylation of α-dystroglycan (αDG). Loss of αDG functional glycosylation prevents it from binding to laminin and other extracellular matrix receptors, causing muscular dystrophy. Mutations in a number of genes, including FKTN (fukutin), disrupt αDG glycosylation. METHODS: We analyzed conditional Fktn knockout (Fktn KO) muscle for levels of mTOR signaling pathway proteins by Western blot...
June 2, 2016: Skeletal Muscle
https://www.readbyqxmd.com/read/27880847/activation-of-both-the-calpain-and-ubiquitin-proteasome-systems-contributes-to-septic-cardiomyopathy-through-dystrophin-loss-disruption-and-mtor-inhibition
#11
Ana Caroline Silva Freitas, Maria Jose Figueiredo, Erica Carolina Campos, Danilo Figueiredo Soave, Simone Gusmao Ramos, Herbert B Tanowitz, Mara Rúbia N Celes
Cardiac dysfunction caused by the impairment of myocardial contractility has been recognized as an important factor contributing to the high mortality in sepsis. Calpain activation in the heart takes place in response to increased intracellular calcium influx resulting in proteolysis of structural and contractile proteins with subsequent myocardial dysfunction. The purpose of the present study was to test the hypothesis that increased levels of calpain in the septic heart leads to disruption of structural and contractile proteins and that administration of calpain inhibitor-1 (N-acetyl-leucinyl-leucinyl-norleucinal (ALLN)) after sepsis induced by cecal ligation and puncture prevents cardiac protein degradation...
2016: PloS One
https://www.readbyqxmd.com/read/27879205/structure-of-protein-o-mannose-kinase-reveals-a-unique-active-site-architecture
#12
Qinyu Zhu, David Venzke, Ameya S Walimbe, Mary E Anderson, Qiuyu Fu, Lisa N Kinch, Wei Wang, Xing Chen, Nick V Grishin, Niu Huang, Liping Yu, Jack E Dixon, Kevin P Campbell, Junyu Xiao
The 'pseudokinase' SgK196 is a protein O-mannose kinase (POMK) that catalyzes an essential phosphorylation step during biosynthesis of the laminin-binding glycan on α-dystroglycan. However, the catalytic mechanism underlying this activity remains elusive. Here we present the crystal structure of Danio rerio POMK in complex with Mg(2+) ions, ADP, aluminum fluoride, and the GalNAc-β3-GlcNAc-β4-Man trisaccharide substrate, thereby providing a snapshot of the catalytic transition state of this unusual kinase...
November 23, 2016: ELife
https://www.readbyqxmd.com/read/27854211/n-terminal-%C3%AE-dystroglycan-%C3%AE-dg-n-a%C3%A2-potential-serum-biomarker-for-duchenne-muscular-dystrophy
#13
Kelly E Crowe, Guohong Shao, Kevin M Flanigan, Paul T Martin
BACKGROUND: Duchenne Muscular Dystrophy (DMD) is a severe, progressive, neuromuscular disorder of childhood. While a number of serum factors have been identified as potential biomarkers of DMD, none, as yet, are proteins within the dystrophin-associated glycoprotein (DAG) complex. OBJECTIVE: We have developed an immobilized serum ELISA assay to measure the expression of a constitutively cleaved and secreted component of the DAG complex, the N-terminal domain of α dystroglycan (αDG-N), and assayed relative expression in serum from muscular dystrophy patients and normal controls...
May 27, 2016: Journal of Neuromuscular Diseases
https://www.readbyqxmd.com/read/27807076/a-poglut1-mutation-causes-a-muscular-dystrophy-with-reduced-notch-signaling-and-satellite-cell-loss
#14
Emilia Servián-Morilla, Hideyuki Takeuchi, Tom V Lee, Jordi Clarimon, Fabiola Mavillard, Estela Area-Gómez, Eloy Rivas, Jose L Nieto-González, Maria C Rivero, Macarena Cabrera-Serrano, Leonardo Gómez-Sánchez, Jose A Martínez-López, Beatriz Estrada, Celedonio Márquez, Yolanda Morgado, Xavier Suárez-Calvet, Guillermo Pita, Anne Bigot, Eduard Gallardo, Rafael Fernández-Chacón, Michio Hirano, Robert S Haltiwanger, Hamed Jafar-Nejad, Carmen Paradas
Skeletal muscle regeneration by muscle satellite cells is a physiological mechanism activated upon muscle damage and regulated by Notch signaling. In a family with autosomal recessive limb-girdle muscular dystrophy, we identified a missense mutation in POGLUT1 (protein O-glucosyltransferase 1), an enzyme involved in Notch posttranslational modification and function. In vitro and in vivo experiments demonstrated that the mutation reduces O-glucosyltransferase activity on Notch and impairs muscle development...
November 2, 2016: EMBO Molecular Medicine
https://www.readbyqxmd.com/read/27788222/aquaporin-4-cell-surface-expression-and-turnover-are-regulated-by-dystroglycan-dynamin-and-the-extracellular-matrix-in-astrocytes
#15
Daniel Kai Long Tham, Bharat Joshi, Hakima Moukhles
The water-permeable channel aquaporin-4 (AQP4) is highly expressed in perivascular astrocytes of the mammalian brain and represents the major conduit for water across the blood-brain barrier. Within these cells, AQP4 is found in great quantities at perivascular endfoot sites but is detected in lesser amounts at the membrane domains within the brain parenchyma. We had previously established that this polarization was regulated by the interaction between dystroglycan (DG), an extracellular matrix receptor that is co-expressed with AQP4, and the laminin that is contained within the perivascular basal lamina...
2016: PloS One
https://www.readbyqxmd.com/read/27773428/biallelic-mutations-in-tmtc3-encoding-a-transmembrane-and-tpr-containing-protein-lead-to-cobblestone-lissencephaly
#16
Julie Jerber, Maha S Zaki, Jumana Y Al-Aama, Rasim Ozgur Rosti, Tawfeg Ben-Omran, Esra Dikoglu, Jennifer L Silhavy, Caner Caglar, Damir Musaev, Beate Albrecht, Kevin P Campbell, Tobias Willer, Mariam Almuriekhi, Ahmet Okay Çağlayan, Jiri Vajsar, Kaya Bilgüvar, Gonul Ogur, Rami Abou Jamra, Murat Günel, Joseph G Gleeson
Cobblestone lissencephaly (COB) is a severe brain malformation in which overmigration of neurons and glial cells into the arachnoid space results in the formation of cortical dysplasia. COB occurs in a wide range of genetic disorders known as dystroglycanopathies, which are congenital muscular dystrophies associated with brain and eye anomalies and range from Walker-Warburg syndrome to Fukuyama congenital muscular dystrophy. Each of these conditions has been associated with alpha-dystroglycan defects or with mutations in genes encoding basement membrane components, which are known to interact with alpha-dystroglycan...
November 3, 2016: American Journal of Human Genetics
https://www.readbyqxmd.com/read/27766311/muscle-involvement-in-limb-girdle-muscular-dystrophy-with-gmppb-deficiency-lgmd2t
#17
S T Oestergaard, T Stojkovic, J R Dahlqvist, C Bouchet-Seraphin, J Nectoux, F Leturcq, M Cossée, G Solé, C Thomsen, T O Krag, J Vissing
OBJECTIVE: In this study, muscle involvement assessed by MRI and levels of GMPPB and glycosylation of α-dystroglycan expression in muscle were examined in patients with limb-girdle muscular dystrophy (LGMD) type 2T. METHODS: Six new patients with genetically verified mutations in GMPPB were studied. T1-weighted magnetic resonance images were obtained in 4 participants. Muscle strength and potential involvement of extramuscular organs were examined. Glycosylation of α-dystroglycan in muscle was studied, and GMPPB and α-dystroglycan expression was analyzed by Western blotting...
December 2016: Neurology. Genetics
https://www.readbyqxmd.com/read/27733679/the-muscular-dystrophy-gene-tmem5-encodes-a-ribitol-%C3%AE-1-4-xylosyltransferase-required-for-the-functional-glycosylation-of-dystroglycan
#18
Hiroshi Manya, Yoshiki Yamaguchi, Motoi Kanagawa, Kazuhiro Kobayashi, Michiko Tajiri, Keiko Akasaka-Manya, Hiroko Kawakami, Mamoru Mizuno, Yoshinao Wada, Tatsushi Toda, Tamao Endo
A defect in O-mannosyl glycan is the cause of α-dystroglycanopathy, a group of congenital muscular dystrophies caused by aberrant α-dystroglycan (α-DG) glycosylation. Recently, the entire structure of O-mannosyl glycan, [3GlcAβ1-3Xylα1]n-3GlcAβ1-4Xyl-Rbo5P-1Rbo5P-3GalNAcβ1-3GlcNAcβ1-4 (phospho-6)Manα1-, which is required for the binding of α-DG to extracellular matrix ligands, has been proposed. However, the linkage of the first Xyl residue to ribitol 5-phosphate (Rbo5P) is not clear. TMEM5 is a gene product responsible for α-dystroglycanopathy and was reported as a potential enzyme involved in this linkage formation, although the experimental evidence is still incomplete...
November 18, 2016: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/27711214/progressive-dystrophic-pathology-in-diaphragm-and-impairment-of-cardiac-function-in-fkrp-p448l-mutant-mice
#19
Anthony Blaeser, Hiroyuki Awano, Bo Wu, Qi-Long Lu
Mutations in the gene for fukutin-related protein represent a subset of muscular dystrophies known as dystroglycanopathies characterized by loss of functionally-glycosylated-alpha-dystroglycan and a wide range of dystrophic phenotypes. Mice generated by our lab containing the P448L mutation in the fukutin-related protein gene demonstrate the dystrophic phenotype similar to that of LGMD2I. Here we examined the morphology of the heart and diaphragm, focusing on pathology of diaphragm and cardiac function of the mutant mice for up to 12 months...
2016: PloS One
https://www.readbyqxmd.com/read/27707967/neuronal-dystroglycan-is-necessary-for-formation-and-maintenance-of-functional-cck-positive-basket-cell-terminals-on-pyramidal-cells
#20
Simon Früh, Jennifer Romanos, Patrizia Panzanelli, Daniela Bürgisser, Shiva K Tyagarajan, Kevin P Campbell, Mirko Santello, Jean-Marc Fritschy
: Distinct types of GABAergic interneurons target different subcellular domains of pyramidal cells, thereby shaping pyramidal cell activity patterns. Whether the presynaptic heterogeneity of GABAergic innervation is mirrored by specific postsynaptic factors is largely unexplored. Here we show that dystroglycan, a protein responsible for the majority of congenital muscular dystrophies when dysfunctional, has a function at postsynaptic sites restricted to a subset of GABAergic interneurons...
October 5, 2016: Journal of Neuroscience: the Official Journal of the Society for Neuroscience
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