Ask about this productRelated genes to: Man2a2 antibody
- Gene:
- MAN2A2 NIH gene
- Name:
- mannosidase alpha class 2A member 2
- Previous symbol:
- -
- Synonyms:
- MANA2X, HsT19662
- Chromosome:
- 15q25
- Locus Type:
- gene with protein product
- Date approved:
- 1997-07-01
- Date modifiied:
- 2016-01-22
Related products to: Man2a2 antibody
Related articles to: Man2a2 antibody
- Idiopathic pulmonary fibrosis (IPF) is a complex disease without clear etiology or effective therapy. While DNA methylation has been implicated in IPF pathogenesis, the tissue-specific causal effects of the epigenetic factors on IPF remain undetermined. Here, we perform epigenome-wide Mendelian randomization using blood-based methylation quantitative trait loci of 420,509 CpG sites and genome-wide association study for IPF to elucidate the causal effects of the CpG sites on IPF. Totally, 452 CpG sites has shown putative causal effects on IPF risk after Bonferroni correction. Among them, 13 CpG sites have shown strong colocalization evidence with genetic factors associated with IPF. Specifically, DNA methylation at CpG sites within MAN2A2 and TRIM27 shows significant differences between IPF lungs and controls, correlating with altered mRNA expressions of these genes in lung tissues. The CpG site in MAN2A2 is a binding site of ZNF384 according to transcription factor databases. RNA sequencing in the TGFβ1-induced alveolar epithelia confirms significantly reduced expression of MAN2A2 and ZNF384 comparing to the controls. Collectively, our study suggests a putative causal link between DNA methylation within MAN2A2 and IPF risk, wherein lung-specific DNA methylation in MAN2A2 may perturb the interaction between ZNF384 and MAN2A2, revealing novel roles for these genes in IPF pathogenesis. - Source: PubMed
Publication date: 2026/04/11
Li ZhaoqiHong LunaLv XingyuYang ShuangyuYe FengzhanHuang LinjieJiang ShanpingZhao Huiying - Neuronal development relies on cell-surface glycoconjugates that function as complex bioinformational codes. Recently, altered glycosylation has emerged as a central mechanistic theme in the pathophysiology of autism spectrum disorder (ASD). Critically, the brain maintains a distinctively restricted glycan profile through strict biosynthetic regulation, creating a specialized landscape highly susceptible to homeostatic perturbation. This "membrane-centric vulnerability" spans both glycoproteins and glycolipids; however, evidence remains fragmented, obscuring their pathogenic interplay. To bridge this gap, this review synthesizes evidence for these two primary classes of membrane glycoconjugates into a unified framework. We examine how defects in key glycoproteins (such as NCAM1 and neuroligins) directly impair synaptic signaling, trafficking, and plasticity. We then demonstrate how these defects are functionally coupled to the glycolipid (ganglioside) environment, which organizes the lipid raft platforms essential for glycoprotein function. We propose that these two systems are not independent but represent a final common pathway for diverse etiological drivers. Genetic variants (e.g., MAN2A2), environmental factors (e.g., valproic acid), and epigenetic dysregulation (e.g., miRNAs) all converge on this mechanism of impaired glycan maturation. This model elucidates how distinct upstream causes can produce a common downstream synaptic pathology by compromising the integrity of the membrane signaling platform. - Source: PubMed
Publication date: 2026/01/01
Osterne Vinicius J SOliveira Messias VPinto-Junior Vanir RMota Francisco S BCavada Benildo SNascimento Kyria S - Egg-laying and growth traits play a critical role in determining the economic value of geese. This study integrates a genome-wide association study with functional analyses to elucidate the genetic basis of these traits in the Jilin White Goose. We systematically phenotyped 200 geese for key egg-laying traits, such as total egg number and average egg-laying interval, as well as growth traits, including body weight and tibia length. The GWAS, utilizing whole-genome resequencing, identified 766 significant single nucleotide polymorphisms. Notably, a non-synonymous mutation (chr19:361983:C:A) within the MAN2A2 gene was strongly associated with average egg-laying interval. Other significant loci included UBE2R2, which is associated with body weight, and NTN1/SLC2A9, linked to tibia length. Functional validation in goose follicular granulosa cells demonstrated that the knockdown of MAN2A2 activated the mitochondrial apoptosis pathway, as indicated by increased levels of Caspase-3 and an elevated BAX/Bcl-2 ratio, while suppressing CDK4, thereby promoting apoptosis and cell cycle arrest. In contrast, overexpression of MAN2A2 enhanced cell proliferation and exhibited anti-apoptotic effects. Additionally, silencing of MAN2A2 induced upregulation of MYC, suggesting its involvement in a complex stress-response network. These findings identify MAN2A2 as a key regulator of granulosa cell homeostasis, influencing both follicular development and the egg-laying interval. This study provides valuable genetic markers and insights for breeding improvements in Jilin White Goose. - Source: PubMed
Publication date: 2025/12/09
Song YupuMa JingyunMabrouk IchrafLiu QiuyuanHua GuoqingMa XiaomingXu JingCao HengWang JingboLi JiachengLiu JiayuZhang JialinZhang XinwenSun Yongfeng - Glycosylation is a post-translational modification essential for proper protein folding and function, with significant roles in diverse biological processes, including neurogenesis. MAN2A2 enzyme is required for proper N-glycan trimming/maturation in the N-glycosylation pathway. Whole-exome sequencing of a trio revealed two potentially causative variants in the MAN2A2 gene in a patient with autism spectrum disorder (ASD) and cognitive delay. The first variant, c.1679G > A (p.Arg560Gln), was inherited from the unaffected father. It is located within the alpha-mannosidase middle functional domain, a region essential for mannose metabolism and alpha-mannosidase enzymatic activity. The second variant, c.3292C > T (p.Gln1098Ter), was inherited from the mother and it generated a premature stop codon. These variants resulted in a compound heterozygous condition in the patient. Prediction using the DOMINO tool suggested an autosomal recessive inheritance pattern. Notably, the MAN2A2 gene is highly expressed in several brain regions. The encoded enzyme, an alpha-mannosidase, is localized to the Golgi apparatus, the cellular organelle where the processing and maturation of N-glycans occurs. In silico analyses consistently classified both variants as likely pathogenic, supported by structural prediction analyses that indicated significant disruptions in protein architecture. Glycosylation analyses demonstrated impaired N-glycosylation, evidenced by the accumulation of immature serum glycoprotein N-glycans including disease-specific hybrid-type species. Further investigations are essential to elucidate the role of this gene in ASD and cognitive delay. - Source: PubMed
Publication date: 2025/07/08
Treccarichi SimoneVinci MirellaCirnigliaro LaraMessina AngelaPalmigiano AngeloPettinato FabioMusumeci AntoninoChiavetta ValeriaSaccone SalvatoreSturiale LuisaCalì FrancescoBarone Rita - Microglia are the immune cells in the central nervous system (CNS) and become pro-inflammatory/activated in Alzheimer's disease (AD). Cell surface glycosylation plays an important role in immune cells; however, the N-glycosylation and glycosphingolipid (GSL) signatures of activated microglia are poorly understood. Here, we study comprehensively combined transcriptomic and glycomic profiles using human induced pluripotent stem cells-derived microglia (hiMG). Distinct changes in N-glycosylation patterns in amyloid-β oligomer (AβO) and LPS-treated hiMG were observed. In AβO-treated cells, the relative abundance of bisecting N-acetylglucosamine (GlcNAc) N-glycans decreased, corresponding with a downregulation of MGAT3. The sialylation of N-glycans increased in response to AβO, accompanied by an upregulation of genes involved in N-glycan sialylation (ST3GAL4 and 6). Unlike AβO-induced hiMG, LPS-induced hiMG exhibited a decreased abundance of complex-type N-glycans, aligned with downregulation of mannosidase genes (MAN1A1, MAN2A2, and MAN1C1) and upregulation of ER degradation related-mannosidases (EDEM1-3). Fucosylation increased in LPS-induced hiMG, aligned with upregulated fucosyltransferase 4 (FUT4) and downregulated alpha-L-fucosidase 1 (FUCA1) gene expression, while sialofucosylation decreased, aligned with upregulated neuraminidase 4 (NEU4). Inhibition of sialylation and fucosylation in AβO- and LPS-induced hiMG alleviated pro-inflammatory responses. However, the GSL profile did not exhibit significant changes in response to AβO or LPS activation, at least in the 24-hour stimulation timeframe. AβO- and LPS- specific glycosylation changes could contribute to impaired microglia function, highlighting glycosylation pathways as potential therapeutic targets for AD. - Source: PubMed
Publication date: 2025/04/10
Tang XinyuSchindler Ryan LeeDi Lucente JacopoOloumi ArminTena JennyferHarvey DanielleLebrilla Carlito BZivkovic Angela MJin Lee-WayMaezawa Izumi