ASAH1 ELISA kit
- Known as:
- ASAH1 Enzyme-linked immunosorbent assay test reagent
- Catalog number:
- DL-ASAH1-Hu
- Product Quantity:
- 96T
- Category:
- Elisa Kits
- Supplier:
- WDSTD
- Gene target:
- ASAH1 ELISA kit
Related genes to: ASAH1 ELISA kit
- Gene:
- ASAH1 NIH gene
- Name:
- N-acylsphingosine amidohydrolase 1
- Previous symbol:
- ASAH
- Synonyms:
- AC, PHP32, FLJ21558, ACDase
- Chromosome:
- 8p22
- Locus Type:
- gene with protein product
- Date approved:
- 1997-08-22
- Date modifiied:
- 2016-06-21
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- - Source: PubMed
Publication date: 2026/04/10
Mustafa FarsanaSha ShariqMacken Wiliam LWilson Lindsay AGarg AjayGupta NeerjaBhatia RohitRajan RoopaGupta AnuSingh Mamta BPitceathly Robert D SReilly Mary MHanna Michael GVishnu Venugopalan V - Lysosomal dysfunction is central to Parkinson's disease pathogenesis, with as the strongest established genetic risk factor. Numerous other genes involved in lysosomal sphingolipid, glycosphingolipid and ceramide metabolism have been proposed as contributors to Parkinson's disease, underscoring the need for comprehensive genetic analyses across these pathways. We analysed rare variants (minor allele frequency < 0.01) across 36 lysosomal genes (excluding ) in 8,267 individuals with Parkinson's disease and 68,208 controls, including a subset of 793 early-onset Parkinson's disease (≤50 years) cases. Targeted sequencing was performed in four cohorts at McGill University (3,456 Parkinson's disease patients and 2,664 controls) and results were combined with whole-genome sequencing data from the UK Biobank (2,848 cases, 62,451 controls), and from the Accelerating Medicines Partnership - Parkinson's Disease (1,963 cases, 3,093 controls). We analysed the association of rare variants in these genes with Parkinson's disease using Sequence Kernel Association Test-Optimal (SKAT-O) across variant classes (all rare variants, nonsynonymous, loss-of-function and predicted damaging variants with a Combined Annotation Dependent Depletion (CADD) score >20), with meta-analysis across cohorts. We additionally performed per-domain analyses for variants in gene segments encoding functional domains. False discovery rate correction was applied. Meta-analysis identified a significant association between rare variants in and Parkinson's disease (Pfdr=0.04). Several additional lysosomal genes showed nominal associations (P<0.05), including and . Domain-based analyses identified a strong enrichment of nonsynonymous variants within the beta-acetyl-hexosaminidase-like domain of HEXA (P = 8.0 × 10), although this signal did not survive correction for multiple testing (Pfdr=0.154). In early-onset Parkinson's disease, domain-based analyses revealed significant associations in (Pfdr=7.3×10) and (Pfdr=0.03). Together, these results provide genetic evidence that rare variants across multiple lysosomal pathways, particularly those related to sialylation, ganglioside metabolism, ceramide biology, and lysosomal proteolysis, may contribute to Parkinson's disease susceptibility beyond , highlighting biologically coherent pathways for future replication and functional investigation. - Source: PubMed
Publication date: 2026/02/18
Senkevich KonstantinParlar Sitki CemChantereault CloeLiu LangYu EricRudakou UladzislauAhmad JamilRuskey Jennifer AAsayesh FarnazSpiegelman DanWaters CherylMonchi OuryDauvilliers YvesDupré NicolasGreenbaum LiorHassin-Baer SharonMiliukhina IrinaTimofeeva AllaEmelyanov AntonPchelina SofyaAlcalay Roy NGan-Or Ziv - Maintenance of appropriate ceramide levels and composition in the stratum corneum of the epidermis is essential for skin barrier function. Although ceramide homeostasis is regulated by both synthesis and degradation, the extent of ceramide degradation in the epidermis, as well as the ceramidase responsible for this degradation, has thus far remained unclear. Here, we found that the acid ceramidase ASAH1 is strongly expressed in differentiated human keratinocytes. To investigate its role, we generated ASAH1 KO cells using immortalized human keratinocytes and analyzed their ceramide levels. Under differentiation conditions, ASAH1 KO keratinocytes exhibited a marked accumulation of ceramide classes composed of sphingosine (S) or dihydrosphingosine (dS) and nonhydroxy fatty acid (N) (ceramides NS and NdS). In contrast, ceramides with (an) additional hydroxyl group(s)-such as those containing phytosphingosine (P) or 6-hydroxysphingosine (H) and N or α-hydroxy fatty acid (A) (ceramides NP, NH, AP, and AH)-showed a moderate or no increase. Similar results were obtained upon treatment with SABRAC, a specific ASAH1 inhibitor. In vitro enzyme assays revealed that ASAH1 exhibited strong activity toward NS and NdS, weak activity toward NP and NH, and no activity toward AP. These results indicate that ASAH1-mediated ceramide class-dependent degradation occurs in differentiated human keratinocytes. This degradation likely plays an important role in maintaining appropriate ceramide levels and class composition in the stratum corneum, thereby contributing to the integrity of the skin barrier. - Source: PubMed
Publication date: 2026/01/20
Nobumoto WakanaNaganuma TatsuroNozaka NanaOhno YusukeNojiri KokiKihara Akio - Gaucher disease (GD) is a lysosomal storage disorder caused by mutations in the gene, leading to deficient glucocerebrosidase activity and accumulation of glucosylceramide in macrophages. Beyond lysosomal dysfunction, GD is associated with widespread metabolic abnormalities, yet the molecular basis of these changes remains incompletely understood. This study employed constraint-based genome-scale metabolic modelling to investigate systemic metabolic reprogramming in GD macrophages, aiming to uncover disrupted pathways and mechanistic drivers of disease phenotypes. - Source: PubMed
Publication date: 2026/01/20
Liu YanjunLuo XiRanjbar SamiraAerts Johannes M F Gvan der Lienden MartijnDardis AndreaFleming Ronan M T - Patients with inflammatory bowel disease (IBD) exhibit elevated expression of acid ceramidase (AC), a sphingolipid metabolism enzyme. Recent studies have shown that myeloid cells contribute to the elevated expression of AC, such that the conditional loss of AC is protective in IBD. - Source: PubMed
Publication date: 2026/01/06
Espinoza Keila SDahl Brandon KWysong Jessica NRyan Ella MGordon Mary RDoll Chelsea LMarron Marilyn TBeard Cameron ADey Pujarini DSimpson Richard JSnider Justin MWilson Justin EKiela Pawel RSnider Ashley J