Ask about this productRelated genes to: GYG1 antibody
- Gene:
- GYG1 NIH gene
- Name:
- glycogenin 1
- Previous symbol:
- GYG
- Synonyms:
- -
- Chromosome:
- 3q24
- Locus Type:
- gene with protein product
- Date approved:
- 1997-07-22
- Date modifiied:
- 2016-10-05
Related products to: GYG1 antibody
Related articles to: GYG1 antibody
- Glycogen storage disease Type XV (GSD-XV; OMIM #613507) is an ultra-rare autosomal recessive disorder caused by biallelic pathogenic variants in GYG1, typically presenting with late-onset skeletal myopathy, while predominant cardiac involvement is exceptional. We report a 31-year-old man with chest pain, fatigue, and exertional dyspnea whose electrocardiogram demonstrated a spontaneous Type-1 Brugada pattern with complete right bundle branch block. Transthoracic echocardiography revealed nonobstructive left ventricular hypertrophy with preserved ejection fraction, whereas speckle-tracking showed markedly reduced global longitudinal strain with a heterogeneous distribution and absence of apical sparing. Cardiac magnetic resonance demonstrated mid-to-apical hypertrophy and patchy nonischemic late gadolinium enhancement consistent with myocardial fibrosis. Clinical exome sequencing identified a homozygous pathogenic GYG1 variant (NM_004130.4:c.304G>C; p.(Asp102His)) supported by functional evidence and familial segregation consistent with autosomal recessive inheritance. No pathogenic variants were detected in genes classically associated with Brugada syndrome, supporting a substrate-related Brugada phenocopy. Neurological examination, serum creatine kinase levels, and systemic evaluation were unremarkable. This case further expands the recognized cardiac phenotype associated with GYG1 deficiency by illustrating the coexistence of metabolic hypertrophic cardiomyopathy, myocardial fibrosis, and a Brugada phenocopy pattern, while highlighting a potential link between structural remodeling and arrhythmogenic electrical manifestations. - Source: PubMed
Publication date: 2026/07/22
Arat NurcanCetincelik UmranGülten Zümrüt ArslanSisman Sevil Tokdemir - Pathogenic biallelic variants in , encoding for glycogenin-1, are associated with polyglucosan bodies myopathy characterized by muscle accumulation of deposits of amylopectin-like polysaccharides (MIM 616199). So far, only few cases (<50) with molecular defects in have been reported. The proband is a 79-year-old Italian woman presenting with subacute onset of diffuse soreness, weakness in the upper limbs and diffuse muscle atrophy without cardiac or respiratory involvement. Electromyography showed myopathic features. Muscle biopsy revealed several type I muscle fibers containing intensely PAS-positive, diastase-resistant vacuoles of variable dimension. Ultrastructural analysis showed vacuoles with granular-fibrillar storage material localized in subsarcolemmal and intermyofibrillar areas, small amounts of free glycogen and jagged Z-line appearance of some sarcomeres. Clinical exome sequencing revealed two heterozygous pathogenic variants in . Our findings provide clinical and molecular characterization of a novel case of -related polyglucosan bodies myopathy and highlight the histological clues leading to the diagnosis of this rare clinical phenotype. - Source: PubMed
Publication date: 2026/05/29
Molitierno NicolaVelardo DanieleSalvucci GiuliaAbati ElenaTumminello GabrieleRipolone MichelaZanotti SimonaNapoli LauraCiscato PatriziaSciacco MonicaComi Giacomo PietroCorti StefaniaRonchi Dario - Glycogen storage diseases are inherited disorders of glycogen metabolism and are commonly associated with hypoglycaemia, hepatic dysfunction, or skeletal and cardiac myopathy, depending on the affected enzyme. Glycogen storage disease type 15 (GSD15) is caused by pathogenic variants in GYG1, which encodes glycogenin-1, the auto-glucosylating primer required for glycogen synthesis. GSD15 is characterized by cardiomyopathy and storage of abnormal glycogen and polyglucosan in cardiomyocytes. - Source: PubMed
Publication date: 2026/05/21
Visuttijai KittichateHedberg-Oldfors CarolaBraun OscarEnglund ElisabetGlamuzina EmmaTurner ClintonVukusic KristinaSandstedt JoakimDellgren GöranKarason KristjanOldfors Anders - Polyglucosan body myopathy type 2 (PGBM2; OMIM #616199) is an autosomal recessive myopathy caused by biallelic variants in GYG1, which encodes glycogenin-1. It is characterized by progressive muscle weakness and PAS-positive, diastase-resistant polyglucosan inclusions on muscle biopsy. We report a 64-year-old woman who developed progressive proximal weakness beginning in her early 50s, with polyglucosan bodies identified on muscle histopathology. Genome sequencing (GS) detected a single heterozygous pathogenic splice-site variant, NM_004130.4(GYG1):c.143+3G>C. Given strong histopathologic evidence of PGBM2, GS data were reanalyzed, revealing an additional rare deep intronic variant, NM_004130.4(GYG1):c.7+992T>G, predicted to activate a cryptic exon. RNA sequencing (RNA-seq) confirmed aberrant splicing from both variants, demonstrating exon 2 skipping associated with c.143+3G>C and cryptic exon inclusion caused by c.7+992T>G. Variant phasing posed a diagnostic challenge due to unavailable parental DNA, and long-range PCR results were inconclusive. Long-read GS definitively demonstrated that the two variants were in trans, establishing compound heterozygosity and confirming the molecular diagnosis. These findings enabled reclassification of the deep intronic variant as likely pathogenic. This case highlights the diagnostic limitations of conventional phasing approaches in adult-onset recessive disorders and demonstrates the clinical utility of integrating genome reanalysis, RNA-seq, and long-read GS for resolving complex phasing challenges. - Source: PubMed
Publication date: 2026/04/23
Panwar DeepakFarris Joseph DSchmidt DanielleBlake Emily JTan Jia WNaddaf ElieSonnen JoshuaVairo Filippo Pinto ELambert Laura JWierenga Klaas JMuthusamy KarthikKlee Eric W - 1 (GyG1) can infect a variety of animals and humans, but prevention and control strategies are limited, which endangers the healthy development of the poultry breeding industry and has a potential impact on public health safety. The live poultry market (LPM) connects the production and consumption ends, and the pathogen may spread across regions through transportation and personnel flow. To understand the prevalence of GyG1 in Guangxi, 3482 samples from LPMs, namely, 2693 chicken throat and cloacal swabs and 789 environmental samples collected in Guangxi from December 2019 to December 2024, were assayed by PCR. The results revealed that GyG1 was present in chicken and environmental samples from LPMs in Guangxi, China, with positivity rates of 17.08% and 13.31%, respectively. Eight GyG1-positive samples were randomly selected, including 5 chicken swab samples and 3 environmental samples for whole-genome amplification. The amino acids encoded by the three ORFs were analysed, and some mutation sites unique to these 8 variants were found. The homology between the 8 GyG1 genomes and 36 reference sequences was 96.8-99.8%. The homology of the VP1 gene sequence was 96.5-99.9%, and the homology of the amino acid sequence was 99.4-100%. A phylogenetic tree was constructed on the basis of the 8 GyG1 genomes and 36 GyG1 reference genome sequences from 14 different species (8 from zoos) in this study. The 44 sequences were divided into three branches constituting groups A, B and C, with the 8 novel strains classified into group A2. Recombination analysis predicted that two recombination events in the GyG1 sequence were associated with the emergence of Guangxi strain GX-AGV2-202109-5. This study clarified the prevalence and molecular characteristics of GyG1 in LPMs in Guangxi, China, were clarified for the first time, providing important data supporting the prevention and control of GyG1 infection and providing a reference for further understanding the epidemiology and genetic diversity of GyG1. - Source: PubMed
Publication date: 2026/02/09
Zhang YanfangXie ZhixunXie ZhiqinXie LijiLi MengYan MingWu AiqiongZhang MinxiuFan QingZeng TingtingHuang JiaolingWang ShengWan LijunLi XiaofengWei YouLuo Sisi