Ask about this productRelated genes to: HGSNAT antibody
- Gene:
- HGSNAT NIH gene
- Name:
- heparan-alpha-glucosaminide N-acetyltransferase
- Previous symbol:
- TMEM76
- Synonyms:
- FLJ32731, HGNAT
- Chromosome:
- 8p11.21-p11.1
- Locus Type:
- gene with protein product
- Date approved:
- 2005-09-23
- Date modifiied:
- 2018-11-16
Related products to: HGSNAT antibody
Related articles to: HGSNAT antibody
- Moyamoya disease (MMD) is a progressive cerebrovascular disorder characterized by chronic cerebral hypoperfusion and ischemic microenvironments that critically impact brain microvascular endothelial cells. Oxygen-glucose deprivation (OGD) models have been extensively employed in MMD research to recapitulate the ischemic conditions relevant to MMD pathophysiology. This study aims to explore the functional involvement and molecular basis of HGSNAT in human brain microvascular endothelial cells (HBMECs) following OGD-induced injury, to establish a theoretical foundation for elucidating the pathogenesis of vascular endothelial injury associated with MMD. - Source: PubMed
Publication date: 2026/08/10
Wen ZhonghuiHu BinWang HaiChen ZiyuYang SenZhang FuqingTang Zhiwei - Mucopolysaccharidosis type III (MPS III), or Sanfilippo syndrome, is a group of rare autosomal recessive lysosomal storage disorders caused by deficiency of enzymes involved in heparan sulfate degradation, encoded by (type A), (type B), (type C), or (type D). Progressive lysosomal accumulation leads to neurodegeneration, cognitive decline, behavioral disturbances, and premature death. Despite a global pooled birth prevalence of ∼0.76 per 100,000 live births, MPS III remains substantially underdiagnosed in Latin America. To date, only a single MPS IIIB case has been molecularly confirmed in Mexico, with no reported cases of MPS IIIA or IIIC. - Source: PubMed
Publication date: 2026/07/27
Naal-Chan PaolaEcheverria-Ortegon ErmiloCouoh-Castañeda Jary-DavisMillet-Herrera Jose-LuisSolis-Baeza Fabiola-ConcepcionPerez-Garcia Myrna-EdithRivera-Lavalle Jorge-SantiagoCastillo-Espinola Addy-ManuelaReyes-Flores Olga-BereniceCampos-Garcia Felix-Julian - To describe the expanding genotypic and phenotypic spectrum of isolated -related retinitis pigmentosa (RP). This retrospective case series included 3 patients with -related RP who presented to the Wilmer Eye Institute. Medical records and multimodal imaging findings were reviewed. Three patients were identified, aged 39 to 66 years. Symptom duration before presentation ranged from 3 months to 5 years, and best-corrected visual acuity ranged from 20/20 to 20/125. All 3 patients harbored the c.1843G>A (p.Ala615Thr) or the novel c.1102A>T (p.Lys368*) pathogenic variants and demonstrated wide phenotypic heterogeneity. This case series illustrates the diverse clinical presentations within the spectrum of -related RP and highlights the diagnostic challenges posed by cases with minimal fundoscopic abnormalities. - Source: PubMed
Publication date: 2026/06/24
Ruggeri Maria LudovicaHalawa OmarAhmed Ishrat - Biallelic variants in the HGSNAT gene are associated with Sanfilippo syndrome, a rare lysosomal storage disorder caused by deficiency of heparan acetyl CoA glucosamine N-Acetyl-transferase enzyme(HGSNAT). The syndrome is characterized by multiple systemic findings, including progressive neurological and retinal degeneration. Retinitis pigmentosa due to HGSNAT gene variants are rarely reported without systemic manifestations. - Source: PubMed
Publication date: 2026/07/06
Haefeli Lorena MParedes Diego IWyman Celeste SCapasso Jenina EChattannavar GouraKhetan VikasTallis EranLevin Alex V - Sialic acid O-acetylation is implicated in the modulation of sialoglycan recognition and ganglioside biology. The sugar modification is catalyzed by CASD1, a Golgi membrane protein that encompasses a luminal catalytic domain and a multipass transmembrane domain. The mechanism of how acetyl-CoA is provided to the Golgi remains poorly understood. Here, we show that the acetyl-CoA transporter SLC33A1 provides acetyl-CoA to the luminal domain of CASD1 and that patient-derived SLC33A1 variants linked to inherited neurodevelopmental and neurodegenerative disorders impair ganglioside 9-O-acetylation. Under conditions that enable the formation of 7,9-di-O-acetylated sialoglycans, genetic inactivation of SLC33A1 impaired di-O-acetylation, but unexpectedly, still enabled mono-O-acetylation. Structure prediction and site-directed mutagenesis revealed a second active site in CASD1 that shares striking similarities with the catalytic acetyl-CoA binding transmembrane tunnel of the lysosomal acetyltransferase HGSNAT. Together, our data provide strong evidence that CASD1 has dual functionalities and catalyzes 7,9-di-O-acetylation through SLC33A1-dependent luminal acetylation and SLC33A1-independent transmembrane acetylation. - Source: PubMed
Publication date: 2026/04/01
Albers MalenaBosse LydiaSchröter LarissaJunemann Anna-Maria TRossdam CharlotteHartmann MaikeGrove MelanieLitfin ThomasEgger Anna-SophiaKwiatkowski MarcelThedieck KathrinZocher GeorgBuettner Falk F RMalde Alpeshkumar Kvon Itzstein MarkMühlenhoff Martina