CLIA 15-lipoxygenase 2,15-LOX-2,15-LOX-B,ALOX15B,Arachidonate 15-lipoxygenase B,Arachidonate 15-lipoxygenase type II,Homo sapiens,Human
- Known as:
- CLIA 15-lipoxygenase 2,15-LOX-2,15-LOX-B,ALOX15B,Arachidonate 15-lipoxygenase B,Arachidonate 15-lipoxygenase classification II,Homo sapiens,Human
- Catalog number:
- U1356h
- Product Quantity:
- 96T
- Category:
- -
- Supplier:
- EIAab
- Gene target:
- CLIA 15-lipoxygenase 2 15-LOX-2 15-LOX- ALOX15B Arachidonate type Homo sapiens Human
Related genes to: CLIA 15-lipoxygenase 2,15-LOX-2,15-LOX-B,ALOX15B,Arachidonate 15-lipoxygenase B,Arachidonate 15-lipoxygenase type II,Homo sapiens,Human
- Gene:
- ALOX15B NIH gene
- Name:
- arachidonate 15-lipoxygenase type B
- Previous symbol:
- -
- Synonyms:
- 15-LOX-2
- Chromosome:
- 17p13.1
- Locus Type:
- gene with protein product
- Date approved:
- 1998-07-22
- Date modifiied:
- 2019-01-18
Related products to: CLIA 15-lipoxygenase 2,15-LOX-2,15-LOX-B,ALOX15B,Arachidonate 15-lipoxygenase B,Arachidonate 15-lipoxygenase type II,Homo sapiens,Human
Related articles to: CLIA 15-lipoxygenase 2,15-LOX-2,15-LOX-B,ALOX15B,Arachidonate 15-lipoxygenase B,Arachidonate 15-lipoxygenase type II,Homo sapiens,Human
- Octyl (-(5-(1-indol-2-yl)-2-methoxyphenyl)sulfamoyl)carbamate has previously been characterized as substrate-specific inhibitor of the linoleic acid oxygenase activity of mammalian ALOX15 orthologs. Here we aimed at optimizing the inhibitory properties of this compound by three different chemical modifications: (i) replacement of the indole core by a phenylpyrrole; (ii) introduction of hydrophilic residues into the aliphatic hydrocarbon chain of the lead compound or by replacing this building block by a triethylene glycol moiety; (iii) replacement of the sulfamoylcarbamate group by a sulfonamide. The inhibitory potencies of the modified compounds for pure rabbit ALOX15 were quantified by in vitro inhibitory assays, and our data indicate that the replacement of the rigid indole core induced a partial loss in the inhibitor's potency. The introduction of a hydrophilic group into the aliphatic hydrocarbon chain or its replacement by a triethylene glycol moiety improved the solubility of the compound in aqueous solution, but reduced the inhibitor potency by more than one order of magnitude. Finally, the replacement of the sulfamoylcarbamate moiety by sulfonamide improved the substrate selectivity of the inhibitor for rabbit and human ALOX15. The new compounds were highly potent for human and rabbit ALOX15, but did not inhibit human ALOX15B and were less effective for mouse Alox15 (ortholog specificity). - Source: PubMed
Publication date: 2026/07/22
Gavrilyuk ViktorAksenov VladislavPetrov KirillKurchatova Angelina VBortnevskij DmitriyZhuravlev AlexanderGolovanov AlexeyKuhn HartmutIvanov Igor - Arachidonic acid lipoxygenases (ALOX-isoforms) have been implicated in cell differentiation and in the pathogenesis of various diseases. Human ALOX-isoforms prefer free polyunsaturated fatty acids as substrate but some of them are also capable of oxygenating complex ester lipids. Here we compared the reactivity of mammalian ALOX isoforms with complex lipid structures, explored the chemistry of the oxygenation products and characterized the structure of the enzyme-substrate complexes. We found that human and mouse ALOX15 orthologs as well as human ALOX15B are capable of oxidizing complex substates in the absence of adapter proteins and that the patterns of oxygenation products were similar to those of free fatty acid oxygenation. In contrast, the corresponding activities of mouse Alox15b and human ALOX12 were limited. Specific lipoxygenase products were also detected in the plasma lipids of mice with modified ALOX15 gene suggesting the in vivo activity of the enzyme on complex ester lipid substrates. - Source: PubMed
Publication date: 2026/06/08
Chen XinSträtker Sarah MelissaParvez SahanawazVabulas Ramunas MartinBochert AstridRothe MichaelHolzhütter Hermann-GeorgAparoy PolamarasettyKuhn Hartmut - Lipoxygenases (arachidonic acid lipoxygenase [ALOX]) are non-heme iron-containing dioxygenases that catalyze the oxygenation of polyenoic fatty acid-containing lipids to their corresponding hydroperoxy derivatives. These enzymes are widely distributed in highly developed plants and animals. In bacteria, they rarely occur, but they have not been detected in archaea and viruses. The human genome involves six functional ALOX genes (ALOX15, ALOX15B, ALOX12, ALOX12B, ALOXE3, and ALOX5) encoding for six different isoenzymes. The mouse genome carries an orthologous gene for each human ALOX gene, but in addition, an Aloxe12 gene has been identified in this species. The application of isoenzyme-specific loss-of-function strategies suggested that the coding multiplicity may not be interpreted as a sign of functional redundancy. In fact, the different isoenzymes apparently fulfill different biological functions. Mammalian ALOX15 orthologs are allosteric enzymes, but the molecular basis for their allosteric properties remains controversial. In fact, two alternative hypotheses (the presence of allosteric binding sites at enzyme monomers versus ALOX15 dimers consist of an allosteric and a catalytic monomer) have been introduced, and this review is aimed at critically evaluating the pros and cons of these two mechanistic scenarios. - Source: PubMed
Publication date: 2026/02/05
Yang JiaxingBorchert AstridKuhn Hartmut - Pulmonary arterial hypertension (PAH) is a progressive vascular disorder characterized by endothelial dysfunction, vascular remodeling, and poor prognosis. Arachidonic acid 15-lipoxygenase (ALOX15) and its isoform, arachidonic acid 15-lipoxygenase type B (ALOX15B), are lipid-metabolizing enzymes involved in inflammation, fibrosis, and vascular smooth muscle proliferation. However, their specific roles in pulmonary artery endothelial cells (PAECs), particularly in the regulation of autophagy-a key process in the pathogenesis of PAH remain unclear. This study aimed to investigate the contribution of ALOX15/15B to PAH development through modulation of autophagy in PAECs. - Source: PubMed
Publication date: 2025/11/07
Zhao XueyongYin JialianLu TingyueChen HuitingChen HongyuChen ShifanYu Xiufeng - Many questions remain unanswered regarding the implication of genetics and lipid metabolites with severe SARS-CoV-2 infections. We performed bulk RNA-seq and a total fatty acid panel analysis on PBMCs and plasma collected from 10 infected and 10 uninfected patients. Univariate comparison of lipid metabolites using the Mann-Whitney U-test revealed that six lipid metabolites were significantly increased in COVID-19 patients, including the lipid mediators arachidonic acid (AA) and eicosapentaenoic acid (EPA), which both give rise to eicosanoids. Key lipids implicated in inflammation, including AA and EPA, along with the fatty acids DHA and DPA, were significantly and positively correlated to the WHO disease severity score. Analysis of our bulk RNA-seq dataset demonstrated distinct transcriptional profiles leading to a segregation of COVID-19 patients based on the WHO score. Ontology, KEGG, and Reactome analysis identified several key pathways and nodes that were enriched for genes related to innate immunity, interactions between lymphoid and nonlymphoid cells, interleukin signaling, and subsequent DNA damage pathways. EPA levels correlated with heightened cell cycling and DNA damage pathways observed in patients with a high WHO score. We studied gene expression in nasopharyngeal swabs from 58 healthy and COVID-19 participants and identified that genes implicated in eicosanoid synthesis, such as alox5, alox12, and alox15B, were specifically up-regulated in high WHO score patients in several cell types of the nasopharynx, especially goblet cells across different viral variants (Deta and Omicron). Using published nasal scRNA-seq datasets from COVID-19 patients, we evaluated the expression of genes implicated in eicosanoid synthesis, such as ALOX5, ALOX15, and ALOX15B, across nasal cell types and COVID-19 severity groups. Altogether, our study highlights the fact that the increase in specific lipids implicated in inflammation and the genes required for their synthesis correlated with the severity of the SARS-CoV-2 infection. - Source: PubMed
Tomalka Jeffrey AOwings AnnaGaleas-Pena MichelleZiegler Carly G KRobinson Tanya OWichman Thomas GLaird HannahWilliams Haley BGhaliwal Neha SEverman StevenZafar YousafWalsh Jaclyn M LShalek Alex KHorwitz Bruce HOrdovas-Montanes JoseGlover Sarah CGibert Yann