Ask about this productRelated genes to: GNPTAB Blocking Peptide
- Gene:
- GNPTAB NIH gene
- Name:
- N-acetylglucosamine-1-phosphate transferase subunits alpha and beta
- Previous symbol:
- GNPTA
- Synonyms:
- KIAA1208, MGC4170
- Chromosome:
- 12q23.2
- Locus Type:
- gene with protein product
- Date approved:
- 2005-09-11
- Date modifiied:
- 2018-04-23
Related products to: GNPTAB Blocking Peptide
Related articles to: GNPTAB Blocking Peptide
- Mucolipidosis type III (ML-III) alpha/beta and gamma are uncommon lysosomal storage diseases caused by a partial deficiency of the N-acetylglucosaminyl-1-phosphotransferase enzyme. Biallelic mutations in the GNPTAB gene are responsible for ML-III alpha/beta, whereas mutations in GNPTG lead to ML-III gamma. This study aims to thoroughly investigate the clinical manifestations and diagnostic clues of ML-III, with the goal of preventing misdiagnosis and delays in diagnosis. - Source: PubMed
Publication date: 2026/04/24
Burgac EzgiKaplan İremBulut Fatma DeryaKara EsraKöseci BurcuTuğ Bozdoğan SevcanCoşkun Benlidayı İlkeKor DenizÖnenli Mungan Neslihan - Inclusion cell disease (I-cell disease/Mucolipiodsis Type II) is an autosomal recessive lysosomal storage disorder that results in accumulation of substrates (cholesterol, phospholipids, and glycosaminoglycans) in various tissues. The clinical presentation of I-cell disease includes hepatomegaly, splenomegaly, cardiomegaly, upper respiratory infections, skeletal deformities, developmental delay, abnormal facies, and failure to thrive. We describe a case of I-cell disease in a neonate admitted to the Neonatal Intensive Care Unit for respiratory distress with initial suspicion of infection. Placental histopathological findings included syncytiotrophoblast vacuolization and positive lipid vacuoles highlighted with the special stain, Oil Red-O. Ultra-rapid whole genome sequencing from buccal swab identified compound heterozygous variants consistent with I-cell disease. Whole exome sequencing of placental tissue showed concordant pathogenic variants. To our knowledge, this is the first report of Oil Red-O staining of intracytoplasmic lipids within syncytiotrophoblast and successfully identifying variants by sequencing placental DNA in the setting of I-cell disease. - Source: PubMed
Publication date: 2026/04/20
LaScala NicolasRose LauraSanchez JenniferChousal Jennifer NMurray SarahParast ManaPham BettyAisagbonhi Omonigho - Lysosomes are multifunctional organelles that play important roles in cellular recycling, signaling, and homeostasis, relying on precise trafficking and activation of lysosomal enzymes. While the Golgi apparatus plays a central role in lysosomal enzyme sorting, the mechanisms linking Golgi function to lysosomal activity remain incompletely understood. Here, we identify the Golgi-resident protein GRASP55, but not its paralog GRASP65, as necessary for lysosome function. Loss of GRASP55 expression leads to missorting and secretion of lysosomal enzymes, lysosomal dysfunction and bloating. GRASP55 deficiency also disrupts lysosomal mTORC1 signaling, reducing the phosphorylation of its lysosomal substrates TFEB/TFE3, while sparing its non-lysosomal targets. Mechanistically, GRASP55 binds and maintains the COPI adaptor GOLPH3 protein at the Golgi, thereby controlling the Golgi localization and stability of LYSET and GNPTAB that are required for mannose 6-phosphate (M6P) tagging of lysosomal enzymes. These findings reveal an essential role for GRASP55 in Golgi-lysosome communication and lysosomal enzyme trafficking and underscore the importance of Golgi-mediated protein sorting in lysosome function and lysosomal mTORC1 signaling. - Source: PubMed
Publication date: 2026/04/16
Nüchel JulianOmidi MaryamFernandes Stephanie ATauber MarinaPohl SandraPlomann MarkusDemetriades Constantinos - Mucolipidosis type II alpha/beta (ML II) (OMIM # 252500), alternatively referred to as Inclusion Cell (I-cell) Disease, is a relatively rare lysosomal storage disorder that is autosomal recessive in inheritance due to the mutation of the GNPTAB (N-acetylglucosamine-1-phosphate transferase sub-units alpha and beta) gene present on chromosome 12q23.3. Currently, there is no cure for this disorder; treatment is both symptomatic and palliative. This report describes the case of a five-year-old patient with ML II with pathogenic variant (t c.3335+1G>A) who presented with aspiration pneumonia and renal insufficiency. The child was born to a consanguineous couple and had a sibling with a similar clinical presentation who passed away at age four due to cardiovascular complications. The patient was treated with continuous positive airway pressure (CPAP) and IV Tazobactam, Piperacillin, and Vancomycin. On follow-up, she was started on Spironolactone 20mg and Captopril 12.5mg daily for mitral regurgitation. - Source: PubMed
Anwar KhadijaKumar Darshan - Developmental stuttering (DS) is a complex neurodevelopmental disorder affecting approximately 5% of children, characterized by involuntary disruptions in speech fluency. Despite its prevalence, the precise pathophysiology remains elusive, and current behavioral and pharmacological interventions often yield variable long-term efficacy. This scoping review evaluates the therapeutic potential of transcranial photobiomodulation (t-PBM), a non-invasive neuromodulation technique, by summarizing its mechanisms of action with the known neurophysiological deficits of DS. Evidence indicates that DS is associated with reduced regional cerebral blood flow (rCBF) in Broca's area, mitochondrial dysfunction, and impaired neural connectivity. t-PBM may address these deficits by stimulating cytochrome c oxidase, thereby increasing ATP production and triggering nitric oxide-mediated vasodilation to enhance rCBF. Furthermore, t-PBM promotes neuroplasticity, modulates astrocyte function-potentially counteracting GNPTAB-related deficits-and exhibits anxiolytic effects that may alleviate the secondary psychological burden of DS. By targeting these multifactorial underpinnings, t-PBM may represent a promising, low-risk adjunct or primary intervention for DS, though this remains to be tested empirically. While the theoretical framework is robust, clinical trials are needed to determine whether t-PBM has therapeutic utility, to optimize treatment parameters, establish longitudinal efficacy, and explore synergistic effects with established speech-language therapies. - Source: PubMed
Publication date: 2026/03/07
Ferreras Borja IgnacioGoyeneche ManuelaCassano PaoloGuenther Frank HTumanova Victoria