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Croda International Plc c1p d18

Regulation of ORMDLs stability in human RPE‐1 cells and mouse BMMCs. (A) Levels of ORMDLs, SPTLC1, SPTLC2, and total <t>d18:1</t> ceramides (measured by LC‐ESI‐MS/MS) were assessed in human RPE‐1 cells and mouse BMMCs after 24‐h treatment with 10 μM myriocin or 10 μM FB 1 , and compared with untreated controls. (B) Quantification of ORMDLs, SPTLC1, SPTLC2, and the LC3‐II/LC3‐I ratio was performed in untreated RPE‐1 cells and BMMCs, and compared with cells treated for 24 h with 50 μM CQ or 10 μM MG132, as determined by immunoblotting. (C) Effects of p97/VCP inhibition by CB‐5083 on ORMDLs, SPTLC1, SPTLC2, the LC3‐II/LC3‐I ratio, ATF4, and p62 levels were assessed in RPE‐1 cells and BMMCs. Protein levels in (A‐C) were normalized to total protein loading using Ponceau S staining. Data are presented as geometric mean ± GSEM ( N = 4). Statistical analysis was performed using one‐way ANOVA with Tukey's post hoc test. Significance levels: p < 0.05 (*), p < 0.01 (**), p < 0.001 (***), p < 0.0001 (****); n.s., not significant.

C1p D18, supplied by Croda International Plc, used in various techniques. Bioz Stars score: 90/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/c1p+d18/C12+Ceramide-1-Phosphate/pmc12974560-206-46-52
Average 90 stars, based on 10 article reviews

c1p d18 - by Bioz Stars, 2026-09

90/100 stars

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1) Product Images from "ORMDL Proteins Turnover via Proteasome and Autophagy Is Cell‐Type Dependent and Tied to Ceramide Homeostasis"

Article Title: ORMDL Proteins Turnover via Proteasome and Autophagy Is Cell‐Type Dependent and Tied to Ceramide Homeostasis

Journal: The FASEB Journal

doi: 10.1096/fj.202502924RR

Regulation of ORMDLs stability in human RPE‐1 cells and mouse BMMCs. (A) Levels of ORMDLs, SPTLC1, SPTLC2, and total d18:1 ceramides (measured by LC‐ESI‐MS/MS) were assessed in human RPE‐1 cells and mouse BMMCs after 24‐h treatment with 10 μM myriocin or 10 μM FB 1 , and compared with untreated controls. (B) Quantification of ORMDLs, SPTLC1, SPTLC2, and the LC3‐II/LC3‐I ratio was performed in untreated RPE‐1 cells and BMMCs, and compared with cells treated for 24 h with 50 μM CQ or 10 μM MG132, as determined by immunoblotting. (C) Effects of p97/VCP inhibition by CB‐5083 on ORMDLs, SPTLC1, SPTLC2, the LC3‐II/LC3‐I ratio, ATF4, and p62 levels were assessed in RPE‐1 cells and BMMCs. Protein levels in (A‐C) were normalized to total protein loading using Ponceau S staining. Data are presented as geometric mean ± GSEM ( N = 4). Statistical analysis was performed using one‐way ANOVA with Tukey's post hoc test. Significance levels: p < 0.05 (*), p < 0.01 (**), p < 0.001 (***), p < 0.0001 (****); n.s., not significant.

Figure Legend Snippet: Regulation of ORMDLs stability in human RPE‐1 cells and mouse BMMCs. (A) Levels of ORMDLs, SPTLC1, SPTLC2, and total d18:1 ceramides (measured by LC‐ESI‐MS/MS) were assessed in human RPE‐1 cells and mouse BMMCs after 24‐h treatment with 10 μM myriocin or 10 μM FB 1 , and compared with untreated controls. (B) Quantification of ORMDLs, SPTLC1, SPTLC2, and the LC3‐II/LC3‐I ratio was performed in untreated RPE‐1 cells and BMMCs, and compared with cells treated for 24 h with 50 μM CQ or 10 μM MG132, as determined by immunoblotting. (C) Effects of p97/VCP inhibition by CB‐5083 on ORMDLs, SPTLC1, SPTLC2, the LC3‐II/LC3‐I ratio, ATF4, and p62 levels were assessed in RPE‐1 cells and BMMCs. Protein levels in (A‐C) were normalized to total protein loading using Ponceau S staining. Data are presented as geometric mean ± GSEM ( N = 4). Statistical analysis was performed using one‐way ANOVA with Tukey's post hoc test. Significance levels: p < 0.05 (*), p < 0.01 (**), p < 0.001 (***), p < 0.0001 (****); n.s., not significant.

Techniques Used: Tandem Mass Spectroscopy, Western Blot, Inhibition, Staining

Quantitative Proteomics:

Article Title: Serum Metabolome and Lipidome Changes in Adult Patients with Primary Dengue Infection
Article Snippet: .. Known concentrations (20–100 ng/mL) of non-naturally occurring internal standards, namely Cer d18:1/17:0, GlcCer d18:1/8:0, LacCer d18:1/8:0, SM d18:1/12:0, C1P d18:1/17:0, PA 14:0, PC 14:0, PE 14:0, PG 14:0, PS 14:0 and PI 14:0; Avanti Polar Lipids, Alabaster, Al) were verified of their low abundance in sera, spiked into extracted samples and used in absolute quantification. ..

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Journal: The FASEB Journal

Article Title: ORMDL Proteins Turnover via Proteasome and Autophagy Is Cell‐Type Dependent and Tied to Ceramide Homeostasis

doi: 10.1096/fj.202502924RR

Figure Lengend Snippet: Regulation of ORMDLs stability in human RPE‐1 cells and mouse BMMCs. (A) Levels of ORMDLs, SPTLC1, SPTLC2, and total d18:1 ceramides (measured by LC‐ESI‐MS/MS) were assessed in human RPE‐1 cells and mouse BMMCs after 24‐h treatment with 10 μM myriocin or 10 μM FB 1 , and compared with untreated controls. (B) Quantification of ORMDLs, SPTLC1, SPTLC2, and the LC3‐II/LC3‐I ratio was performed in untreated RPE‐1 cells and BMMCs, and compared with cells treated for 24 h with 50 μM CQ or 10 μM MG132, as determined by immunoblotting. (C) Effects of p97/VCP inhibition by CB‐5083 on ORMDLs, SPTLC1, SPTLC2, the LC3‐II/LC3‐I ratio, ATF4, and p62 levels were assessed in RPE‐1 cells and BMMCs. Protein levels in (A‐C) were normalized to total protein loading using Ponceau S staining. Data are presented as geometric mean ± GSEM ( N = 4). Statistical analysis was performed using one‐way ANOVA with Tukey's post hoc test. Significance levels: p < 0.05 (*), p < 0.01 (**), p < 0.001 (***), p < 0.0001 (****); n.s., not significant.

Article Snippet: Briefly, 50 μL of homogenate was transferred to a 1.5 mL microcentrifuge tube (Cat# 780420, Brand GmbH, Wertheim, Germany), mixed with 25 μL of MilliQ water, and loaded with internal standards: 50 ng dhS1P d17:0 (Cat# 860655), 50 ng S1P d17:1 (Cat# 860641), and 25 ng C1P d18:1/C12:0 (Cat# 860531), each from Avanti Polar Lipids, dissolved in 5 μL of chloroform/methanol solution (2:1, v/v).

Techniques: Tandem Mass Spectroscopy, Western Blot, Inhibition, Staining

a , b Simulated 3-dimensional docking between a human TTYH1 monomer and ceramide 1-phosphate (CerP(d18:1/22:0)). TMD transmembrane domain. Constituent residues of the docking cavity are shown in surface representation. Residues in green were predicted to form hydrophobic interactions with the docked C1P. E210, R213, and Y217 are highlighted in orange. Magnification of the docking region is shown in ( b ). c Peptide sequence alignment between TTYH1 orthologs of the indicated species. Shown are the partial sequences of the third transmembrane helix. Positions of E210, R213, and Y217 of human TTYH1 are indicated by orange dots. The evolutionarily conserved E210 and R213 are colored in red. d Quantifications of NBD-C1P pulse-chase assay. Ttyh1 WT and Ttyh1 KO astrocytes were pulsed with 2 µM NBD-C1P for 15 min, before chasing in ACSF for 0, 15, 30, and 60 min. NBD fluorescence intensities for each time-point were normalized to the mean of Ttyh1 WT values. Box plots show the median, the bounds of the box (25th and 75th percentiles) and whiskers representing minimum and maximum values. Number of astrocytes ( n ) from two independent experiments is shown in bracket underneath each box plot. Mann–Whitney test. n.s. not significant, P = 0.379. e E210 and R213 confer C1P clearance function. The two residues in human TTYH1 were substituted with nonpolar alanine to create the TTYH1 ER/AA mutant. Astrocytes expressing either wild-type TTYH1 or TTYH1 ER/AA mutant were subject to the NBD-C1P pulse-chase assay. Astrocytes were pulsed with 2 µM NBD-C1P for 15 min, followed by chasing for 60 min. Shown are quantifications of NBD fluorescence before and after the chase. Fluorescence intensities were normalized to the mean of the TTYH1-expressing Ttyh1 WT astrocytes values at 0-min chase. Box plots show the median, the bounds of the box (25th and 75th percentiles) and whiskers representing minimum and maximum values. Number of astrocytes ( n ) from two independent experiments is shown in brackets underneath each box plot. One-way ANOVA ( F = 19.3, df = 188) followed by Bonferroni’s multiple comparisons post hoc test. n.s. not significant, P > 0.9999. Source data are provided as a Source Data file.

Journal: Nature Communications

Article Title: Endolysosomal processing of neuron-derived signaling lipids regulates autophagy and lipid droplet degradation in astrocytes

doi: 10.1038/s41467-025-60402-3

Figure Lengend Snippet: a , b Simulated 3-dimensional docking between a human TTYH1 monomer and ceramide 1-phosphate (CerP(d18:1/22:0)). TMD transmembrane domain. Constituent residues of the docking cavity are shown in surface representation. Residues in green were predicted to form hydrophobic interactions with the docked C1P. E210, R213, and Y217 are highlighted in orange. Magnification of the docking region is shown in ( b ). c Peptide sequence alignment between TTYH1 orthologs of the indicated species. Shown are the partial sequences of the third transmembrane helix. Positions of E210, R213, and Y217 of human TTYH1 are indicated by orange dots. The evolutionarily conserved E210 and R213 are colored in red. d Quantifications of NBD-C1P pulse-chase assay. Ttyh1 WT and Ttyh1 KO astrocytes were pulsed with 2 µM NBD-C1P for 15 min, before chasing in ACSF for 0, 15, 30, and 60 min. NBD fluorescence intensities for each time-point were normalized to the mean of Ttyh1 WT values. Box plots show the median, the bounds of the box (25th and 75th percentiles) and whiskers representing minimum and maximum values. Number of astrocytes ( n ) from two independent experiments is shown in bracket underneath each box plot. Mann–Whitney test. n.s. not significant, P = 0.379. e E210 and R213 confer C1P clearance function. The two residues in human TTYH1 were substituted with nonpolar alanine to create the TTYH1 ER/AA mutant. Astrocytes expressing either wild-type TTYH1 or TTYH1 ER/AA mutant were subject to the NBD-C1P pulse-chase assay. Astrocytes were pulsed with 2 µM NBD-C1P for 15 min, followed by chasing for 60 min. Shown are quantifications of NBD fluorescence before and after the chase. Fluorescence intensities were normalized to the mean of the TTYH1-expressing Ttyh1 WT astrocytes values at 0-min chase. Box plots show the median, the bounds of the box (25th and 75th percentiles) and whiskers representing minimum and maximum values. Number of astrocytes ( n ) from two independent experiments is shown in brackets underneath each box plot. One-way ANOVA ( F = 19.3, df = 188) followed by Bonferroni’s multiple comparisons post hoc test. n.s. not significant, P > 0.9999. Source data are provided as a Source Data file.

Article Snippet: Chemicals: Ceramide 1-phosphate (d18:1/16:0) (C1P; 22542; Cayman); bafilomycin A1 (BafA1; B1793; Sigma-Aldrich); NVP-231 (HY-13945; MedChem Express); human IL-1β (SRP3083; Sigma-Aldrich); biotinylated human IL-1β (ILB-H82E9; Acro Biosystem); bicuculine (Bic; HY-N0219; MedChem Express); 4-aminopyridine (4AP; 275875; Sigma-Aldrich); methyl tert-butyl ether (MTBE; 34875; Sigma-Aldrich).

Techniques: Sequencing, Pulse Chase, Fluorescence, MANN-WHITNEY, Mutagenesis, Expressing

a Schematic representation of TTYH1-mediated endolysosomal clearance of C1P. b Ttyh1 deficiency exacerbates autophagic flux inhibition by exogenous C1P. Levels of p62 and LC3 in cKO astrocytes in response to exogenous C1P were analyzed. Astrocytes were treated with 0 (0.1% DMSO), 0.1, or 0.5 µM of C1P in 0.1% BSA-supplemented culture media for 2 h. Shown are representative immunoblot images and quantifications of three independent experiments. Values were normalized to those of Ttyh1 WT, 0 µ M C1P condition on the same blot. Data were presented as mean ± SEM. Number of biological replicates ( n ) is shown in brackets at the bottom of each bar. *** P < 0.001, ** P < 0.01, One-way ANOVA ( p62/αTub : F = 56.91, df = 17; LC3-II/I : F = 42.95, df = 23) followed by Bonferroni’s multiple comparisons post hoc test. c Human TTYH1 rescues C1P-induced autophagic flux blockage in Ttyh1 KO astrocytes. Levels of LC3 and p62 in Ttyh1 KO astrocytes in response to C1P (0.5 µM) were analyzed. Shown are representative immunoblot images and quantifications of four independent experiments. Values were normalized to those of the untreated mock-transfected control on the same blot. Data are presented as mean ± SEM. Number of biological replicates ( n ) is shown in brackets at the bottom of each bar. One-way ANOVA ( p62/αTub : F = 15.43, df = 23; LC3-II/I : F = 40.88, df = 23) followed by Bonferroni’s multiple comparisons post hoc test. n.s. not significant, P > 0.9999. d Overexpression of TTYH1 in astrocytes restores autophagic flux upon C1P. Levels of LC3 and p62 in primary human brain astrocytes in response to C1P (50 µM) were analyzed. Shown are representative immunoblot images and quantifications of four independent experiments. Values were normalized to those of the untreated mock-transfected control on the same blot. Data were presented as mean ± SEM. Number of biological replicates ( n ) is shown in brackets at the bottom of each bar. One-way ANOVA ( p62/αTub : F = 17.98, df = 23; LC3-II/I : F = 117.5, df = 23) followed by Bonferroni’s multiple comparisons post hoc test. n.s. not significant, P > 0.9999. Source data are provided as a Source Data file.

Journal: Nature Communications

Article Title: Endolysosomal processing of neuron-derived signaling lipids regulates autophagy and lipid droplet degradation in astrocytes

doi: 10.1038/s41467-025-60402-3

Figure Lengend Snippet: a Schematic representation of TTYH1-mediated endolysosomal clearance of C1P. b Ttyh1 deficiency exacerbates autophagic flux inhibition by exogenous C1P. Levels of p62 and LC3 in cKO astrocytes in response to exogenous C1P were analyzed. Astrocytes were treated with 0 (0.1% DMSO), 0.1, or 0.5 µM of C1P in 0.1% BSA-supplemented culture media for 2 h. Shown are representative immunoblot images and quantifications of three independent experiments. Values were normalized to those of Ttyh1 WT, 0 µ M C1P condition on the same blot. Data were presented as mean ± SEM. Number of biological replicates ( n ) is shown in brackets at the bottom of each bar. *** P < 0.001, ** P < 0.01, One-way ANOVA ( p62/αTub : F = 56.91, df = 17; LC3-II/I : F = 42.95, df = 23) followed by Bonferroni’s multiple comparisons post hoc test. c Human TTYH1 rescues C1P-induced autophagic flux blockage in Ttyh1 KO astrocytes. Levels of LC3 and p62 in Ttyh1 KO astrocytes in response to C1P (0.5 µM) were analyzed. Shown are representative immunoblot images and quantifications of four independent experiments. Values were normalized to those of the untreated mock-transfected control on the same blot. Data are presented as mean ± SEM. Number of biological replicates ( n ) is shown in brackets at the bottom of each bar. One-way ANOVA ( p62/αTub : F = 15.43, df = 23; LC3-II/I : F = 40.88, df = 23) followed by Bonferroni’s multiple comparisons post hoc test. n.s. not significant, P > 0.9999. d Overexpression of TTYH1 in astrocytes restores autophagic flux upon C1P. Levels of LC3 and p62 in primary human brain astrocytes in response to C1P (50 µM) were analyzed. Shown are representative immunoblot images and quantifications of four independent experiments. Values were normalized to those of the untreated mock-transfected control on the same blot. Data were presented as mean ± SEM. Number of biological replicates ( n ) is shown in brackets at the bottom of each bar. One-way ANOVA ( p62/αTub : F = 17.98, df = 23; LC3-II/I : F = 117.5, df = 23) followed by Bonferroni’s multiple comparisons post hoc test. n.s. not significant, P > 0.9999. Source data are provided as a Source Data file.

Techniques: Inhibition, Western Blot, Transfection, Control, Over Expression

a Loss of Ttyh1 sensitizes C1P-induced TAG accumulation in astrocytes. Cellular TAG contents in cKO astrocytes were measured after treatment with 0 (0.1% DMSO), 0.5, or 5 µM of C1P in 0.1% BSA-supplemented culture media for 2 h. Data were presented as mean ± SEM. Number of independent lipid extracts ( n ) is shown at the bottom of each bar. One-way ANOVA ( F = 581.7; df = 20) followed by Bonferroni’s multiple comparisons post hoc test. b , c Loss of Ttyh1 exacerbates C1P-induced LD buildup in astrocytes. Representative confocal images in ( b ) show cKO astrocytes stained with BODIPY ( green ) and DAPI ( blue ) after indicated treatments. Quantifications of BODIPY signals in ( c ) reveal LD contents in Ttyh1 WT and KO astrocytes. BODIPY-positive area per cell values were normalized to the mean values of Ttyh1 WT control. Violin plots show median (solid line), interquartile range (dotted line), and probability density of data (smoothed shape). Number of astrocytes ( n ) from ≥3 independent experiments is shown underneath each violin plot. Mann–Whitney test. Source data are provided as a Source Data file.

Journal: Nature Communications

Article Title: Endolysosomal processing of neuron-derived signaling lipids regulates autophagy and lipid droplet degradation in astrocytes

doi: 10.1038/s41467-025-60402-3

Figure Lengend Snippet: a Loss of Ttyh1 sensitizes C1P-induced TAG accumulation in astrocytes. Cellular TAG contents in cKO astrocytes were measured after treatment with 0 (0.1% DMSO), 0.5, or 5 µM of C1P in 0.1% BSA-supplemented culture media for 2 h. Data were presented as mean ± SEM. Number of independent lipid extracts ( n ) is shown at the bottom of each bar. One-way ANOVA ( F = 581.7; df = 20) followed by Bonferroni’s multiple comparisons post hoc test. b , c Loss of Ttyh1 exacerbates C1P-induced LD buildup in astrocytes. Representative confocal images in ( b ) show cKO astrocytes stained with BODIPY ( green ) and DAPI ( blue ) after indicated treatments. Quantifications of BODIPY signals in ( c ) reveal LD contents in Ttyh1 WT and KO astrocytes. BODIPY-positive area per cell values were normalized to the mean values of Ttyh1 WT control. Violin plots show median (solid line), interquartile range (dotted line), and probability density of data (smoothed shape). Number of astrocytes ( n ) from ≥3 independent experiments is shown underneath each violin plot. Mann–Whitney test. Source data are provided as a Source Data file.

Techniques: Staining, Control, MANN-WHITNEY

a IL-1β induces C1P production and secretion in mouse cortical neurons. Data were presented as mean ± SEM. Number of independent lipid samples ( n ) is shown in bracket at the bottom of each bar. One-way ANOVA (Intracellular: F = 33.81, df = 8; Extracellular: F = 3214, df = 11) followed by Tukey’s multiple comparisons post hoc test. b Schematic representation of extracting lipids from neuronal conditioned medium (NCM). NCM lipids derived from IL-1β-treated and untreated neurons are referred to as IL-1β-lipids and naïve-lipids, respectively. c , d Autophagic flux inhibition by IL-1β-lipids is exacerbated by Ttyh1 deficiency and is neuronal Cerk-dependent. cKO astrocytes were treated with NCM lipids for 30 min. For the C1P (+) groups, 0.5 µM C1P was added with NCM lipids. Shown are representative immunoblot images ( c ) and quantifications of p62 and LC3 levels ( d ) from n = 3 independent experiments. Same samples were also loaded on a separate gel for probing Ttyh1 expression. Ratios were normalized to that of Ttyh1 WT-naïve-lipids control on the same blot. Data were presented as mean ± SEM. One-way ANOVA ( p62/αTub : F = 40.74, df = 23; LC3-II/LC3-I : F = 118.1, df = 23) followed by Bonferroni’s multiple comparisons post hoc test. e , f TTYH1 overexpression in human astrocytes rescues IL-1β-lipids-induced autophagic flux inhibition. NCM lipids were derived from human iNeurons. Shown are representative immunoblot images ( e ) and quantifications of p62 and LC3 levels ( f ). Ratios were normalized to that of mock-naïve-lipids control on the same blot. Data were presented as mean ± SEM. Number of biological replicates ( n ) is shown at the bottom of each bar. One-way ANOVA ( p62/αTUB : F = 13.5, df = 26; LC3-II/LC3-I : F = 35.09, df = 50) followed by Bonferroni’s multiple comparisons post hoc test. n.s. not significant, P > 0.999. Source data are provided as a Source Data file.

Journal: Nature Communications

Article Title: Endolysosomal processing of neuron-derived signaling lipids regulates autophagy and lipid droplet degradation in astrocytes

doi: 10.1038/s41467-025-60402-3

Figure Lengend Snippet: a IL-1β induces C1P production and secretion in mouse cortical neurons. Data were presented as mean ± SEM. Number of independent lipid samples ( n ) is shown in bracket at the bottom of each bar. One-way ANOVA (Intracellular: F = 33.81, df = 8; Extracellular: F = 3214, df = 11) followed by Tukey’s multiple comparisons post hoc test. b Schematic representation of extracting lipids from neuronal conditioned medium (NCM). NCM lipids derived from IL-1β-treated and untreated neurons are referred to as IL-1β-lipids and naïve-lipids, respectively. c , d Autophagic flux inhibition by IL-1β-lipids is exacerbated by Ttyh1 deficiency and is neuronal Cerk-dependent. cKO astrocytes were treated with NCM lipids for 30 min. For the C1P (+) groups, 0.5 µM C1P was added with NCM lipids. Shown are representative immunoblot images ( c ) and quantifications of p62 and LC3 levels ( d ) from n = 3 independent experiments. Same samples were also loaded on a separate gel for probing Ttyh1 expression. Ratios were normalized to that of Ttyh1 WT-naïve-lipids control on the same blot. Data were presented as mean ± SEM. One-way ANOVA ( p62/αTub : F = 40.74, df = 23; LC3-II/LC3-I : F = 118.1, df = 23) followed by Bonferroni’s multiple comparisons post hoc test. e , f TTYH1 overexpression in human astrocytes rescues IL-1β-lipids-induced autophagic flux inhibition. NCM lipids were derived from human iNeurons. Shown are representative immunoblot images ( e ) and quantifications of p62 and LC3 levels ( f ). Ratios were normalized to that of mock-naïve-lipids control on the same blot. Data were presented as mean ± SEM. Number of biological replicates ( n ) is shown at the bottom of each bar. One-way ANOVA ( p62/αTUB : F = 13.5, df = 26; LC3-II/LC3-I : F = 35.09, df = 50) followed by Bonferroni’s multiple comparisons post hoc test. n.s. not significant, P > 0.999. Source data are provided as a Source Data file.

Techniques: Derivative Assay, Inhibition, Western Blot, Expressing, Control, Over Expression

a Neuronal C1P production regulates TAG abundance in Drosophila heads. Each datapoint represents one cohort of ≥20 fly heads. Absorbance values from the colorimetric TAG assay were normalized to the mean of controls (Switch OFF). Number of independent lipid extracts ( n ) from fly heads is shown in brackets at the bottom of each bar. Unpaired two-tailed t -test ( Cerk : t = 6.881, df = 12; Cerk-IR : t = 28.87, df = 4). b , c Loss of TTYH1 exacerbates IL-1β-lipids-induced lipid droplet (LD) accumulation in astrocytes. Shown are representative confocal images ( b ) and quantifications of BODIPY signals ( c ). Values were normalized to the mean of the ctrl-shR-naïve-lipids controls. One-way ANOVA ( F = 11.79, df = 190) followed by Bonferroni’s multiple comparisons post hoc test. d Astrocytic Ttyh1 and neuronal C1P production are associated with the IL-1β-lipids-induced LD accumulation in astrocytes. Quantifications of BODIPY signals are shown. Values were normalized to the mean of Ttyh1 WT-naïve-lipids controls. One-way ANOVA ( F = 11.79, df = 190) followed by Bonferroni’s multiple comparisons post hoc test. e Schematic representation of the neuron-astrocyte coculture system. f Ttyh1 KO astrocytes cocultured with IL-1β-stimulated neurons accumulate LDs. Shown are quantifications of BODIPY signals in astrocytes after coculture. Values were normalized to the mean of Ttyh1 WT-beads controls. One-way ANOVA ( F = 4.395, df = 108) followed by Bonferroni’s multiple comparisons post hoc test. n.s. not significant, P > 0.9999. g Loss of Ttyh1 exacerbated TAG accumulation in astrocytes cocultured with IL-1β-stimulated neurons. TAG contents in astrocytes were measured after coculture. In C1P (+) groups, 0.5 µM C1P was added to the coculture medium. Absorbance values from the colorimetric TAG assay were normalized to the mean of Ttyh1 WT-naïve-ctrl-shR controls. Number of independent lipid extracts ( n ) from ≥3 independent experiments is shown in brackets at the bottom of each bar. One-way ANOVA ( F = 937.6, df = 77) followed by Bonferroni’s multiple comparisons post hoc test. *** P < 0.001. Violin plots in ( c – f ) represent median (solid line), interquartile range (dotted line), and probability density of data (smoothed shape). Number of astrocytes ( n ) from ≥3 independent experiments is shown in brackets underneath each violin plot. Bar charts in ( a , g ) represent mean ± SEM. Source data are provided as a Source Data file.

Journal: Nature Communications

Article Title: Endolysosomal processing of neuron-derived signaling lipids regulates autophagy and lipid droplet degradation in astrocytes

doi: 10.1038/s41467-025-60402-3

Figure Lengend Snippet: a Neuronal C1P production regulates TAG abundance in Drosophila heads. Each datapoint represents one cohort of ≥20 fly heads. Absorbance values from the colorimetric TAG assay were normalized to the mean of controls (Switch OFF). Number of independent lipid extracts ( n ) from fly heads is shown in brackets at the bottom of each bar. Unpaired two-tailed t -test ( Cerk : t = 6.881, df = 12; Cerk-IR : t = 28.87, df = 4). b , c Loss of TTYH1 exacerbates IL-1β-lipids-induced lipid droplet (LD) accumulation in astrocytes. Shown are representative confocal images ( b ) and quantifications of BODIPY signals ( c ). Values were normalized to the mean of the ctrl-shR-naïve-lipids controls. One-way ANOVA ( F = 11.79, df = 190) followed by Bonferroni’s multiple comparisons post hoc test. d Astrocytic Ttyh1 and neuronal C1P production are associated with the IL-1β-lipids-induced LD accumulation in astrocytes. Quantifications of BODIPY signals are shown. Values were normalized to the mean of Ttyh1 WT-naïve-lipids controls. One-way ANOVA ( F = 11.79, df = 190) followed by Bonferroni’s multiple comparisons post hoc test. e Schematic representation of the neuron-astrocyte coculture system. f Ttyh1 KO astrocytes cocultured with IL-1β-stimulated neurons accumulate LDs. Shown are quantifications of BODIPY signals in astrocytes after coculture. Values were normalized to the mean of Ttyh1 WT-beads controls. One-way ANOVA ( F = 4.395, df = 108) followed by Bonferroni’s multiple comparisons post hoc test. n.s. not significant, P > 0.9999. g Loss of Ttyh1 exacerbated TAG accumulation in astrocytes cocultured with IL-1β-stimulated neurons. TAG contents in astrocytes were measured after coculture. In C1P (+) groups, 0.5 µM C1P was added to the coculture medium. Absorbance values from the colorimetric TAG assay were normalized to the mean of Ttyh1 WT-naïve-ctrl-shR controls. Number of independent lipid extracts ( n ) from ≥3 independent experiments is shown in brackets at the bottom of each bar. One-way ANOVA ( F = 937.6, df = 77) followed by Bonferroni’s multiple comparisons post hoc test. *** P < 0.001. Violin plots in ( c – f ) represent median (solid line), interquartile range (dotted line), and probability density of data (smoothed shape). Number of astrocytes ( n ) from ≥3 independent experiments is shown in brackets underneath each violin plot. Bar charts in ( a , g ) represent mean ± SEM. Source data are provided as a Source Data file.

Techniques: Two Tailed Test

Inflammatory cytokine stimulates C1P biosynthesis in neurons. C1P and other lipid metabolites secreted by neurons are taken up by the astrocyte endolysosomes, where they are processed by resident enzymes. TTYH1 facilitates the extraction of C1P from endolysosomal membrane, which is necessary for maintaining autophagic flux and lipid droplet degradation. Excessive C1P internalized by astrocytes slows down autophagic flux and reduces lipid droplet degradation. These catabolic activities are further impaired upon TTYH1 deficiency, resulting in autophagic flux blockage and lipid droplet accumulation.

Journal: Nature Communications

Article Title: Endolysosomal processing of neuron-derived signaling lipids regulates autophagy and lipid droplet degradation in astrocytes

doi: 10.1038/s41467-025-60402-3

Figure Lengend Snippet: Inflammatory cytokine stimulates C1P biosynthesis in neurons. C1P and other lipid metabolites secreted by neurons are taken up by the astrocyte endolysosomes, where they are processed by resident enzymes. TTYH1 facilitates the extraction of C1P from endolysosomal membrane, which is necessary for maintaining autophagic flux and lipid droplet degradation. Excessive C1P internalized by astrocytes slows down autophagic flux and reduces lipid droplet degradation. These catabolic activities are further impaired upon TTYH1 deficiency, resulting in autophagic flux blockage and lipid droplet accumulation.

Techniques: Extraction, Membrane

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c1p d18 (Croda International Plc)

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