Ask about this productRelated genes to: GMPPA antibody
- Gene:
- GMPPA NIH gene
- Name:
- GDP-mannose pyrophosphorylase A
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 2q35
- Locus Type:
- gene with protein product
- Date approved:
- 2005-01-10
- Date modifiied:
- 2016-10-05
Related products to: GMPPA antibody
Related articles to: GMPPA antibody
- Supramolecular hydrogels coassembled from drugs and natural low-molecular-weight gelators (LMWGs) offer favorable physicochemical properties, tunable mechanics, and controlled drug release; however, elucidating their in situ fibrillar architecture remains a major challenge. Here, we report a fully natural G-quadruplex hydrogel formed by coassembling 5'-guanosine monophosphate (GMP) with phytic acid (PA), which serves as both a natural cross-linker and a bioactive therapeutic molecule. Systematic modulation of the GMP/PA ratio revealed a delicate compositional balance governing gel formation, mechanical strength, and pH-dependent molecular interactions. Small- and wide-angle X-ray scattering (SWAXS) combined with CRYSOL-assisted atomistic modeling resolved the hierarchical organization of GMP fibrils and demonstrated that PA promotes surface clustering and interfibril bundling through multivalent electrostatic interactions. Molecular dynamics simulations further confirmed PA-mediated stabilization of the G-quadruplex assemblies under hydrated conditions. Kinetic analysis revealed that densification of fibrillar networks effectively slowed scaffold degradation and enabled sustained PA release, transitioning from zero- to first-order kinetics with increasing structural order. Collectively, this study establishes a direct correlation between molecular architecture, mechanical strength, and release dynamics, presenting a structural framework for the rational design of bioactive, G-quadruplex-based hydrogels for advanced drug delivery applications. - Source: PubMed
Publication date: 2026/05/05
Yen Yu-ShengSu Kuan-HsuanZhang Chia-WeiHuang Yu-ChiaoYu Shu-ChunYu Dong-YenJeng U-SerSu Chun-JenChuang Wei-TsungShih OrionHsu Hsin-Yun - BACKGROUND: Non-small cell lung cancer (NSCLC) represents a major global health burden with complex genetic etiology. While observational studies have identified numerous potential risk factors, establishing causal relationships remains challenging due to confounding and reverse causation. METHODS: We conducted a comprehensive Mendelian randomization (MR) analysis to investigate causal relationships between circulating biomarkers, lung tissue gene expression levels, and NSCLC risk. The analysis employed three complementary MR methods: inverse variance weighted (IVW), MR Egger, and weighted median approaches. Genetic instruments were selected from 10 to 26 single nucleotide polymorphisms (SNPs) significantly associated with exposure variables. We validated key findings through quantitative real-time PCR (qRT-PCR) analysis in A549 and H1299 NSCLC cell lines. We examined multiple biomarkers including inflammatory mediators, immune-related proteins, and particularly focused on the HLA region within the major histocompatibility complex. RESULTS: Among circulating biomarkers, thymic stromal lymphopoietin demonstrated a statistically significant positive association with increased NSCLC risk (OR: 1.240, 95% CI: 1.073–1.433, p = 0.003). Gene expression analysis identified 18 genes with significant causal associations (FDR < 0.05), revealing a complex pattern of protective and risk-associated effects. qRT-PCR validation in A549 and H1299 cell lines confirmed differential expression patterns, with protective genes (HLA-DQB2, GMPPA) showing lower expression and risk-associated genes (VDR, P4HTM) showing higher expression in cancer cells compared to normal bronchial epithelial cells. Notable protective genes included HLA-DQB2 (OR: 0.917), HLA-DRB9 (OR: 0.875), and GMPPA (OR: 0.697), while risk-associated genes included VDR (OR: 1.825), P4HTM (OR: 1.520), and multiple HLA variants. Regional association analysis of the HLA-DQB2 locus revealed extremely high significance levels (p-values > 10^-135) within the MHC region on chromosome 6. CONCLUSIONS: This MR analysis provides robust genetic evidence for causal relationships between immune system regulation, inflammatory pathways, and NSCLC development, with experimental validation supporting the functional relevance of identified genetic associations. - Source: PubMed
Publication date: 2026/03/14
Gu ZexinMa TianyuanLi CuicuiTang HanxuLiu JianingZhao Weiwei - - Source: PubMed
Publication date: 2025/09/19
Qiu XiaoxiaYe ZiqingHuang Ying - GMPPA-Congenital Disorder of Glycosylation (CDG) is an ultra-rare autosomal recessive CDG caused by pathogenic variants in GMPPA that affects the N-linked glycosylation pathway. Affected individuals present with three major symptoms: achalasia, alacrima, and impaired intellectual development during infancy. Current management of GMPPA-CDG is targeted to address patients' symptoms. To date, 23 individuals have been reported with GMPPA-CDG. This paper reviews the clinical, biochemical and genetic characteristics of the reported 23 patients and adds 3 patients with GMPPA-CDG. We also describe the effect of oral N-acetylglucosamine (GlcNAc) supplementation in 3 patients. Besides alacrima, achalasia and developmental/ intellectual disability, we noted in these patients also variable growth impairment, facial dysmorphism, hyperkeratosis, hypohidrosis, anodontia, and hearing deficit. Under treatment with GlcNAc (4-6 g/day), we noted improved tear production in our 3 patients. Given its effect on different developmental pathways, we emphasize the need for multidisciplinary care for this multisystem disorder. We did not find a genotype/phenotype correlation in our cohort of 26 patients. - Source: PubMed
Publication date: 2025/07/18
Altassan RuqaiahAldhahri Sarah KMacdonald GeorgiaShah RameenMorava Eva - GDP-mannose pyrophosphorylase B (GMPPB) loss-of-function is associated with muscular dystrophy and variable additional neurological symptoms. GMPPB facilitates the catalytic conversion of mannose-1-phosphate and GTP to GDP-mannose, which serves as a mannose donor for glycosylation. The activity of GMPPB is regulated by its non-catalytic paralogue GMPPA, which can bind GDP-mannose and interact with GMPPB, thereby acting as an allosteric feedback inhibitor of GMPPB. Using pulldown, immunoprecipitation, turnover experiments as well as immunolabeling and enzyme activity assays, we provide first direct evidence that GMPPB activity is regulated by ubiquitination. We further show that the E3 ubiquitin ligase TRIM67 interacts with GMPPB and that knockdown of TRM67 reduces ubiquitination of GMPPB, thus reflecting a candidate E3 ligase for the ubiquitination of GMPPB. While the inhibition of GMPPB ubiquitination decreases its enzymatic activity, its ubiquitination neither affects its interaction with GMPPA nor its turnover. Taken together, we show that the ubiquitination of GMPPB represents another level of regulation of GDP-mannose supply. - Source: PubMed
Publication date: 2024/06/24
Franzka PatriciaMittag SonnhildChakraborty AbhijnanHuber OtmarHübner Christian A