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Search results for: Glycogenin

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#33257366   2020/11/30 To Up

Sequential spontaneous compartment syndrome in multiple limbs in a young adult with GYG1 gene mutation.

Compartment syndrome is a surgical emergency requiring immediate intervention. Majority of compartment syndromes are associated with trauma or surgery. Spontaneous compartment syndrome in multiple limbs is rare and alternative diagnosis should be sought. We report a young adult man who developed compartment syndrome in all four limbs sequentially over 4 years. On further evaluation, he was found to have a gene mutation in exon 3 of GYG1 gene. Spontaneous compartment syndrome in patients with GYG1 gene mutation does not appear to have been previously recognised. Although a direct causality cannot be confidently drawn, this gene is involved in muscle energy utilisation and is known to cause metabolic defect. Acute compartment syndrome, once diagnosed, warrants emergency surgical decompression. The subsequent management of spontaneous compartment syndrome demands a thorough medical assessment to identify any underlying metabolic or genetic predisposition.
Vinay Mathew Joseph, Mathias Thomas Nagy, Sohail Akhtar, Chye Yew Ng

1668 related Products with: Sequential spontaneous compartment syndrome in multiple limbs in a young adult with GYG1 gene mutation.

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#33219378   // To Up

Pulmonary glycogen deficiency as a new potential cause of respiratory distress syndrome.

The glycogenin knockout mouse is a model of Glycogen Storage Disease type XV. These animals show high perinatal mortality (90%) due to respiratory failure. The lungs of glycogenin-deficient embryos and P0 mice have a lower glycogen content than that of wild-type counterparts. Embryonic lungs were found to have decreased levels of mature surfactant proteins SP-B and SP-C, together with incomplete processing of precursors. Furthermore, non-surviving pups showed collapsed sacculi, which may be linked to a significantly reduced amount of surfactant proteins. A similar pattern was observed in glycogen synthase1-deficient mice, which are devoid of glycogen in the lungs and are also affected by high perinatal mortality due to atelectasis. These results indicate that glycogen availability is a key factor for the burst of surfactant production required to ensure correct lung expansion at the establishment of air breathing. Our findings confirm that glycogen deficiency in lungs can cause respiratory distress syndrome and suggest that mutations in glycogenin and glycogen synthase 1 genes may underlie cases of idiopathic neonatal death.
Giorgia Testoni, Bárbara Olmeda, Jordi Duran, Elena López-Rodríguez, Mònica Aguilera, María Isabel Hernández-Álvarez, Neus Prats, Jesús Pérez-Gil, Joan J Guinovart

1603 related Products with: Pulmonary glycogen deficiency as a new potential cause of respiratory distress syndrome.

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#33170837   2020/11/10 To Up

A differential expression of pyrethroid resistance genes in the malaria vector Anopheles funestus across Uganda is associated with patterns of gene flow.

Insecticide resistance is challenging the effectiveness of insecticide-based control interventions to reduce malaria burden in Africa. Understanding the molecular basis of insecticides resistance and patterns of gene flow in major malaria vectors such as Anopheles funestus are important steps for designing effective resistance management strategies. Here, we investigated the association between patterns of genetic structure and expression profiles of genes involved in the pyrethroid resistance in An. funestus across Uganda and neighboring Kenya.
Maurice Marcel Sandeu, Charles Mulamba, Gareth D Weedall, Charles S Wondji

2248 related Products with: A differential expression of pyrethroid resistance genes in the malaria vector Anopheles funestus across Uganda is associated with patterns of gene flow.

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#32958708   2020/10/26 To Up

Stbd1 promotes glycogen clustering during endoplasmic reticulum stress and supports survival of mouse myoblasts.

Imbalances in endoplasmic reticulum (ER) homeostasis provoke a condition known as ER stress and activate the unfolded protein response (UPR) pathway, an evolutionarily conserved cell survival mechanism. Here, we show that mouse myoblasts respond to UPR activation by stimulating glycogenesis and the formation of α-amylase-degradable, glycogen-containing ER structures. We demonstrate that the glycogen-binding protein Stbd1 is markedly upregulated through the PERK signalling branch of the UPR pathway and is required for the build-up of glycogen structures in response to ER stress activation. In the absence of ER stress, Stbd1 overexpression is sufficient to induce glycogen clustering but does not stimulate glycogenesis. Glycogen structures induced by ER stress are degraded under conditions of glucose restriction through a process that does not depend on autophagosome-lysosome fusion. Furthermore, we provide evidence that failure to induce glycogen clustering during ER stress is associated with enhanced activation of the apoptotic pathway. Our results reveal a so far unknown response of mouse myoblasts to ER stress and uncover a novel specific function of Stbd1 in this process, which may have physiological implications during myogenic differentiation.This article has an associated First Person interview with the first author of the paper.
Andria A Lytridou, Anthi Demetriadou, Melina Christou, Louiza Potamiti, Nikolas P Mastroyiannopoulos, Kyriacos Kyriacou, Leonidas A Phylactou, Anthi Drousiotou, Petros P Petrou

2379 related Products with: Stbd1 promotes glycogen clustering during endoplasmic reticulum stress and supports survival of mouse myoblasts.

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#32905144   2020/05/13 To Up

: A distal myopathy with polyglucosan bodies.

Mutations in glycogenin-1 () cause an adult-onset polyglucosan body myopathy. We report here a patient presenting with late-onset distal myopathy. We wish to highlight this rare clinical phenotype of -related myopathy and the histological clues leading to its diagnosis.
Stefan Nicolau, Jennifer A Tracy, David J Pisapia, Kurenai Tanji, Margherita Milone

2868 related Products with: : A distal myopathy with polyglucosan bodies.

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#32751097   2020/07/29 To Up

Metastasis of Uveal Melanoma with Monosomy-3 Is Associated with a Less Glycogenetic Gene Expression Profile and the Dysregulation of Glycogen Storage.

The prolonged storage of glucose as glycogen can promote the quiescence of tumor cells, whereas the accumulation of an aberrant form of glycogen without the primer protein glycogenin can induce the metabolic switch towards a glycolytic phenotype. Here, we analyzed the expression of = 67 genes involved in glycogen metabolism on the uveal melanoma (UM) cohort of the Cancer Genome Atlas (TCGA) study and validated the differentially expressed genes in an independent cohort. We also evaluated the glycogen levels with regard to the prognostic factors via a differential periodic acid-Schiff (PAS) staining. UMs with monosomy-3 exhibited a less glycogenetic and more insulin-resistant gene expression profile, together with the reduction of glycogen levels, which were associated with the metastases. Expression of glycogenin-1 (Locus: 3q24) was lower in the monosomy-3 tumors, whereas the complementary isoform glycogenin-2 (Locus: Xp22.33) was upregulated in females. Remarkably, glycogen was more abundant in the monosomy-3 tumors of male versus female patients. We therefore provide the first evidence to the dysregulation of glycogen metabolism as a novel factor that may be aggravating the course of UM particularly in males.
Siranush Vardanyan, Anton Brosig, Hartmut Merz, Mahdy Ranjbar, Vinodh Kakkassery, Salvatore Grisanti, Aysegül Tura

2608 related Products with: Metastasis of Uveal Melanoma with Monosomy-3 Is Associated with a Less Glycogenetic Gene Expression Profile and the Dysregulation of Glycogen Storage.

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#32477874   2020/05/24 To Up

Glycogenin-1 deficiency mimicking limb-girdle muscular dystrophy.

Glycogen storage disease type XV (GSD XV) is a recently described muscle glycogenosis due to glycogenin-1 () deficiency characterized by the presence of polyglucosan bodies on muscle biopsy (Polyglucosan body myopathy-2, PGBM2). Here we describe a 44 year-old man with limb-girdle muscle weakness mimicking a limb-girdle muscular dystrophy (LGMD), and early onset exertional myalgia. Neurologic examination revealed a waddling gait with hyperlordosis, bilateral asymmetric scapular winging, mild asymmetric deltoid and biceps brachii weakness, and pelvic-girdle weakness involving the gluteal muscles and, to a lesser extent, the quadriceps. Serum creatine kinase levels were slightly elevated. Electrophysiological examination showed a myopathic pattern. There was no cardiac or respiratory involvement. Whole-body muscle MRI revealed atrophy and fat replacement of the tongue, biceps brachii, pelvic girdle and erector spinae. A deltoid muscle biopsy showed the presence of PAS-positive inclusions that remained non-digested with alpha-amylase treatment. Electron microscopy studies confirmed the presence of polyglucosan bodies. A diagnostic gene panel designed by the Genetic Diagnosis Laboratory of Strasbourg University Hospital (France) for 210 muscular disorders genes disclosed two heterozygous, pathogenic gene mutations (c.304G>C;p.(Asp102His) + c.164_165del). Considering the clinical heterogeneity found in the previously described 38 GYG-1 deficient patients, we suggest that should be systematically included in targeted NGS gene panels for LGMDs, distal myopathies, and metabolic myopathies.
Claire Lefeuvre, Stéphane Schaeffer, Robert-Yves Carlier, Maxime Fournier, Françoise Chapon, Valérie Biancalana, Guillaume Nicolas, Edoardo Malfatti, Pascal Laforêt

1459 related Products with: Glycogenin-1 deficiency mimicking limb-girdle muscular dystrophy.

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#32419263   2020/06/15 To Up

Differential diagnosis of vacuolar myopathies in the NGS era.

Altered autophagy accompanied by abnormal autophagic (rimmed) vacuoles detectable by light and electron microscopy is a common denominator of many familial and sporadic non-inflammatory muscle diseases. Even in the era of next generation sequencing (NGS), late-onset vacuolar myopathies remain a diagnostic challenge. We identified 32 adult vacuolar myopathy patients from 30 unrelated families, studied their clinical, histopathological and ultrastructural characteristics and performed genetic testing in index patients and relatives using Sanger sequencing and NGS including whole exome sequencing (WES). We established a molecular genetic diagnosis in 17 patients. Pathogenic mutations were found in genes typically linked to vacuolar myopathy (GNE, LDB3/ZASP, MYOT, DES and GAA), but also in genes not regularly associated with severely altered autophagy (FKRP, DYSF, CAV3, COL6A2, GYG1 and TRIM32) and in the digenic facioscapulohumeral muscular dystrophy 2. Characteristic histopathological features including distinct patterns of myofibrillar disarray and evidence of exocytosis proved to be helpful to distinguish causes of vacuolar myopathies. Biopsy validated the pathogenicity of the novel mutations p.(Phe55*) and p.(Arg216*) in GYG1 and of the p.(Leu156Pro) TRIM32 mutation combined with compound heterozygous deletion of exon 2 of TRIM32 and expanded the phenotype of Ala93Thr-caveolinopathy and of limb-girdle muscular dystrophy 2i caused by FKRP mutation. In 15 patients no causal variants were detected by Sanger sequencing and NGS panel analysis. In 12 of these cases, WES was performed, but did not yield any definite mutation or likely candidate gene. In one of these patients with a family history of muscle weakness, the vacuolar myopathy was eventually linked to chloroquine therapy. Our study illustrates the wide phenotypic and genotypic heterogeneity of vacuolar myopathies and validates the role of histopathology in assessing the pathogenicity of novel mutations detected by NGS. In a sizable portion of vacuolar myopathy cases, it remains to be shown whether the cause is hereditary or degenerative.
Dorothea Mair, Saskia Biskup, Wolfram Kress, Angela Abicht, Wolfgang Brück, Sabrina Zechel, Karl Christian Knop, Fatima Barbara Koenig, Shelisa Tey, Stefan Nikolin, Katja Eggermann, Ingo Kurth, Andreas Ferbert, Joachim Weis

2250 related Products with: Differential diagnosis of vacuolar myopathies in the NGS era.

1100 μg1 g50mg

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#32414843   2020/05/15 To Up

A terminal α3-galactose modification regulates an E3 ubiquitin ligase subunit in .

Skp1, a subunit of E3 Skp1/Cullin-1/F-box protein ubiquitin ligases, is modified by a prolyl hydroxylase that mediates O regulation of the social amoeba and the parasite The full effect of hydroxylation requires modification of the hydroxyproline by a pentasaccharide that, in , influences Skp1 structure to favor assembly of Skp1/F-box protein subcomplexes. In , the presence of a contrasting penultimate sugar assembled by a different glycosyltransferase enables testing of the conformational control model. To define the final sugar and its linkage, here we identified the glycosyltransferase that completes the glycan and found that it is closely related to glycogenin, an enzyme that may prime glycogen synthesis in yeast and animals. However, the enzyme catalyzes formation of a Galα1,3Glcα linkage rather than the Glcα1,4Glcα linkage formed by glycogenin. Kinetic and crystallographic experiments showed that the glycosyltransferase Gat1 is specific for Skp1 in and also in another protist, the crop pathogen The fifth sugar is important for glycan function as indicated by the slow-growth phenotype of Δ parasites. Computational analyses indicated that, despite the sequence difference, the glycan still assumes an ordered conformation that controls Skp1 structure and revealed the importance of nonpolar packing interactions of the fifth sugar. The substitution of glycosyltransferases in and by an unrelated bifunctional enzyme that assembles a distinct but structurally compatible glycan in is a remarkable case of convergent evolution, which emphasizes the importance of the terminal α-galactose and establishes the phylogenetic breadth of Skp1 glycoregulation.
Msano Mandalasi, Hyun W Kim, David Thieker, M Osman Sheikh, Elisabet Gas-Pascual, Kazi Rahman, Peng Zhao, Nitin G Daniel, Hanke van der Wel, H Travis Ichikawa, John N Glushka, Lance Wells, Robert J Woods, Zachary A Wood, Christopher M West

2130 related Products with: A terminal α3-galactose modification regulates an E3 ubiquitin ligase subunit in .

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#32392978   // To Up

[Loss of autophagy in condylar chondrocytes causes increased apoptosis rate in temporomandibular joint osteoarthritis of rats].

To observe the effect of autophagy of condylar chondrocytes on apoptosis in temporomandibular joint osteoarthritis (TMJOA) of rats. Fourty male 2-month-old SPF SD rats were equally divided into sham group (20) and experimental group (20). UAC metal prosthesis was cemented to the left incisors of maxilla and mandible of the rats in experimental group rats. After 8 weeks, all rats were sacrificed and the temporomandibular joint was taken. Two groups of rat condylar chondrocytes were extracted and cultured in vitro to the third generation. Immunofluorescence technique was used to detect the levels of collagen Ⅱ and matrix metalloproteinase-13 (MMP-13) in chondrocytes. The level of light chain-3 (LC-3), an autophagy marker of chondrocytes, was detected. Immunohistochemical technique was used to detect the level glycogenin-1, a glycogen formation marker of chondrocyte, was detected. The level of caspase-3, an apoptosis marker of chondrocyte, was also detected. Tunel technique was used to detect the apoptosis rate of the two groups at 72 h. Cracking cell extraction of total protein, Western-blotting (WB) technology to detect the levels of collagen Ⅱ, MMP -13, LC-3, glycogenin-1, caspase-3 and make gray analysis. Compared with sham group, the level of collagen Ⅱ decreased, MMP-13 increased, LC-3 decreased, glycogenin-1 increased and caspase-3 increased in experimental group. The apoptosis rate of chondrocytes in experimentaal group [ (17.3±4.4) %] at 72h was higher than that in control group [ (5.6±2.1) %](10.732, 0.001) .WB bands gray statistical results show that the level of collagen Ⅱ in chondrocytes of experimental group (0.43±0.21) was lower than that of control group (0.71±0.26) (2.409, 0.043) , the level of MMP-13 in chondrocytes of experimental group (0.73±0.31) was higher than that of control group (0.24±0.10) (3.364, 0.010) , the level of LC-3 in chondrocytes of experimental group (0.09±0.04) was lower than that of control group (0.39±0.18) (3.638, 0.007) , the level of glycogenin-1 in chondrocytes of experimental group (0.68±0.30) was higher than that of control group (0.29±0.17) (2.529, 0.035) , the level of caspase-3 in chondrocytes of experimental group (0.19±0.08) was higher than that of control group (0.05±0.02) (3.796, 0.005) . The level of autophagy of condylar chondrocytes in temporomandibular joint of rats decreased, glycogen accumulation increased, the rate of chondrocyte apoptosis increased, and the number of chondrocytes decreased, resulting in degeneration of condylar cartilage tissue.
J Y Gao, X J Wang, J P Yu, X J An, Z W Jia, X S Guo

2016 related Products with: [Loss of autophagy in condylar chondrocytes causes increased apoptosis rate in temporomandibular joint osteoarthritis of rats].

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