antibodies against prostaglandin e synthase pges 2  (Bioss)

Journal: Nature Communications

Article Title: Molecular basis of prostaglandin E 2 reuptake by organic anion transporter PGT

doi: 10.1038/s41467-025-67025-8

Figure Lengend Snippet: a Schematic of PGs production, function, and clearance. PGs are generated from membrane phospholipids via a series of enzymes, including COXs. Released PGs bind to their cognate GPCRs in an autocrine or paracrine manner. PGT reuptakes released PGs back into cells in exchange with a possible outward lactate flux. Subsequently, PGs are enzymatically inactivated by 15-PGDH. PGT is also suggested as a central component of the Maxi-Cl channel through oligomerization. b Topology diagram of full-length human PGT used in the study. Transmembrane helices of N-domain (green) and C-domain (blue), the Kazal-like domain within ECL5 (purple), and ECLs 1, 2, 3, 6 are labeled appropriately. The eight conserved intra- (yellow) and inter-loop (green) disulfide bridges are indicated by lines. c PGT structure in the absence of substrate viewed from the membrane plane (top) and from the extracellular domain (bottom). The coloring scheme is the same as in ( b ). N -glycosylation modification is shown as pink sticks. d 3 H-PGE 2 uptake activity of PGT variants with truncations of ECL2 (Δ135-165) and ECL5 (Δ425–508, Kazal-like domain) in stably transfected HEK293T cells. Activity values (mean ± SEM, n = 3 biologically independent experiments with 3 technical replicates each) are normalized to that of WT based on their surface protein expression level measured by surface biotinylation (Supplementary Fig. ). e Transport kinetics of WT PGT (black) and the ECL2-truncated mutant (Δ135–165) (orange). Activity values are normalized to those of WT based on the relative expression level, as in ( d ). The inset shows the expanded plot for WT. f Binding affinity for the WT and the ECL2-truncated mutant with PGE 2 measured using microscale thermophoresis assay (mean ± SEM, n = 3 independent experiments). Source data are provided as a file.

Article Snippet: Detergents including dodecylmaltoside, Lauryl Maltose Neopentyl Glycol (LMNG), and cholesteryl hemisuccinate (CHS) were purchased from Antrace Inc. PGE 2 was ordered from MedChemExpress LLC (New jersey, US).

Techniques: Generated, Membrane, Labeling, Glycoproteomics, Modification, Activity Assay, Stable Transfection, Transfection, Expressing, Mutagenesis, Binding Assay, Microscale Thermophoresis

Journal: Nature Communications

Article Title: Molecular basis of prostaglandin E 2 reuptake by organic anion transporter PGT

doi: 10.1038/s41467-025-67025-8

Figure Lengend Snippet: a Overview (left) of the PGE 2 -bound, outward-facing PGT cen structure and with the expanded view (right) of the L-shaped density that fits a PGE 2 molecule (green sticks). b Cutaway side-view of the electrostatic surface potential (negative in red, positive in blue) shows PGE 2 lipid occupying the composite hydrophobic/positive binding site. c Residues lining the central substrate binding cavity that holds PGE 2 (green). Transmembrane helices are numbered. d 3 H-PGE 2 uptake activity of PGT mutants at central binding site under 80 nM of PGE 2 . Data for residues involved in direct PGE 2 interaction were shown in dark gray, while surrounding residues were in light gray. Activities are normalized to that of WT PGT (mean ± SEM, n = 3 biologically independent experiments with 3 technical replicates each), based on the relative surface expression level assessed by surface biotinylation (Supplementary Fig. ). Source data are provided as a file.

Article Snippet: Detergents including dodecylmaltoside, Lauryl Maltose Neopentyl Glycol (LMNG), and cholesteryl hemisuccinate (CHS) were purchased from Antrace Inc. PGE 2 was ordered from MedChemExpress LLC (New jersey, US).

Techniques: Binding Assay, Activity Assay, Expressing

Journal: Nature Communications

Article Title: Molecular basis of prostaglandin E 2 reuptake by organic anion transporter PGT

doi: 10.1038/s41467-025-67025-8

Figure Lengend Snippet: a The elongated density (semi-transparent purple) that fits a PGE 2 (purple sticks) spanning the translocation funnel in PGT len . Sidechains (not well-resolved in the map) in the vicinity are shown as stick representation for illustration purpose. b Top view of the PGT molecular surface colored by residue hydrophobicity. The PGE 2 (purple) is shown as stick representation. c 3 H-PGE 2 uptake activity of mutants of Lys53 at 80 nM of PGE 2 . Activities are normalized to that of WT PGT (mean ± SEM, n = 3 biologically independent experiments with three technical replicates each), based on their relative surface expression level assessed by surface biotinylation. Source data are provided as a file.

Article Snippet: Detergents including dodecylmaltoside, Lauryl Maltose Neopentyl Glycol (LMNG), and cholesteryl hemisuccinate (CHS) were purchased from Antrace Inc. PGE 2 was ordered from MedChemExpress LLC (New jersey, US).

Techniques: Translocation Assay, Residue, Activity Assay, Expressing

Journal: Nature Communications

Article Title: Molecular basis of prostaglandin E 2 reuptake by organic anion transporter PGT

doi: 10.1038/s41467-025-67025-8

Figure Lengend Snippet: a Structural mapping of genetic variants identified in PHO and CEAS patients. b Expanded view of the region covering G222R and P219L. c Relative activity (%WT) of G222R and P219L at 80 nM of PGE2. Activities are normalized to that of WT PGT (mean ± SEM, n = 3 biologically independent experiments, with three technical replicates in each experiment), based on their relative surface expression level assessed using in-gel fluorescence (Supplementary Fig. ). d PGE 2 binding affinity measured for the two mutants (mean ± SEM, n = 3 independent experiments). Source data are provided as a file.

Article Snippet: Detergents including dodecylmaltoside, Lauryl Maltose Neopentyl Glycol (LMNG), and cholesteryl hemisuccinate (CHS) were purchased from Antrace Inc. PGE 2 was ordered from MedChemExpress LLC (New jersey, US).

Techniques: Activity Assay, Expressing, Fluorescence, Binding Assay