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Fig. 1 The actions of βγ-CAT were inhibited by AGSLs (gangliosides and <t>sulfatides)</t> via direct interactions. a THP-1 cells were treated with gradient concentrations of neuraminidase and then incubated with βγ-CAT. The IL-1β concentration in the supernatant was then measured by ELISA. *P < 0.05 and **P < 0.01 versus control by using unpaired two-tailed Student’s t-test (n = 3). b THP-1 cells were treated with different types of glycosidase and then incubated with βγ-CAT. The IL-1β concentrations in the supernatant was measured by ELISA. NS, not signiﬁcant versus control by using unpaired two-tailed Student’s t-test (n = 3). c FITC-labeled βγ-CAT was incubated with different concentrations of gangliosides. The membrane binding of βγ-CAT to THP-1 cells was determined by ﬂow cytometry. The untreated cells were used as a negative control. d βγ-CAT was incubated with different concentrations of gangliosides and added to THP-1 cells. The oligomerization of βγ-CAT was detected by western blotting. The immunoblots are representative of three independent experiments, the original images of immunoblots are shown in Supplementary Figure 7. e FITC-labeled βγ-CAT was incubated with different concentrations of sulfatides and then mixed with THP-1 cells. The membrane binding of βγ-CAT was determined by ﬂow cytometry, the untreated cells were used as a negative control. f βγ-CAT was incubated with different concentrations of sulfatides, then mixed with THP-1 cells. The oligomerization of βγ-CAT was detected by western blotting. The immunoblots are representative of three independent experiments, the original images of immunoblots are shown in Supplementary Figure 7. g βγ-CAT was incubated with different concentrations of lipids and then added to LPS-primed THP-1 cells. The IL-1β concentrations in the supernatant were measured by ELISA. *P < 0.05, **P < 0.01 and ***P < 0.001 represent gangliosides and sulfatides versus sphingomyelin by two-way ANOVA with Bonferroni correction (n = 3). h, i The direct interaction between βγ-CAT and gangliosides (h) or sulfatides (i) was determined using a BLI assay. The BLI interaction curves are representative of three independent experiments. Bars represent the mean ± SD from three independent experiments per condition in a, b and g

Sulfatides, supplied by Croda International Plc, used in various techniques. Bioz Stars score: 95/100, based on 176 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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1) Product Images from "Endogenous pore-forming protein complex targets acidic glycosphingolipids in lipid rafts to initiate endolysosome regulation."

Article Title: Endogenous pore-forming protein complex targets acidic glycosphingolipids in lipid rafts to initiate endolysosome regulation.

Journal: Communications biology

doi: 10.1038/s42003-019-0304-y

Fig. 1 The actions of βγ-CAT were inhibited by AGSLs (gangliosides and sulfatides) via direct interactions. a THP-1 cells were treated with gradient concentrations of neuraminidase and then incubated with βγ-CAT. The IL-1β concentration in the supernatant was then measured by ELISA. *P < 0.05 and **P < 0.01 versus control by using unpaired two-tailed Student’s t-test (n = 3). b THP-1 cells were treated with different types of glycosidase and then incubated with βγ-CAT. The IL-1β concentrations in the supernatant was measured by ELISA. NS, not signiﬁcant versus control by using unpaired two-tailed Student’s t-test (n = 3). c FITC-labeled βγ-CAT was incubated with different concentrations of gangliosides. The membrane binding of βγ-CAT to THP-1 cells was determined by ﬂow cytometry. The untreated cells were used as a negative control. d βγ-CAT was incubated with different concentrations of gangliosides and added to THP-1 cells. The oligomerization of βγ-CAT was detected by western blotting. The immunoblots are representative of three independent experiments, the original images of immunoblots are shown in Supplementary Figure 7. e FITC-labeled βγ-CAT was incubated with different concentrations of sulfatides and then mixed with THP-1 cells. The membrane binding of βγ-CAT was determined by ﬂow cytometry, the untreated cells were used as a negative control. f βγ-CAT was incubated with different concentrations of sulfatides, then mixed with THP-1 cells. The oligomerization of βγ-CAT was detected by western blotting. The immunoblots are representative of three independent experiments, the original images of immunoblots are shown in Supplementary Figure 7. g βγ-CAT was incubated with different concentrations of lipids and then added to LPS-primed THP-1 cells. The IL-1β concentrations in the supernatant were measured by ELISA. *P < 0.05, **P < 0.01 and ***P < 0.001 represent gangliosides and sulfatides versus sphingomyelin by two-way ANOVA with Bonferroni correction (n = 3). h, i The direct interaction between βγ-CAT and gangliosides (h) or sulfatides (i) was determined using a BLI assay. The BLI interaction curves are representative of three independent experiments. Bars represent the mean ± SD from three independent experiments per condition in a, b and g

Figure Legend Snippet: Fig. 1 The actions of βγ-CAT were inhibited by AGSLs (gangliosides and sulfatides) via direct interactions. a THP-1 cells were treated with gradient concentrations of neuraminidase and then incubated with βγ-CAT. The IL-1β concentration in the supernatant was then measured by ELISA. *P < 0.05 and **P < 0.01 versus control by using unpaired two-tailed Student’s t-test (n = 3). b THP-1 cells were treated with different types of glycosidase and then incubated with βγ-CAT. The IL-1β concentrations in the supernatant was measured by ELISA. NS, not signiﬁcant versus control by using unpaired two-tailed Student’s t-test (n = 3). c FITC-labeled βγ-CAT was incubated with different concentrations of gangliosides. The membrane binding of βγ-CAT to THP-1 cells was determined by ﬂow cytometry. The untreated cells were used as a negative control. d βγ-CAT was incubated with different concentrations of gangliosides and added to THP-1 cells. The oligomerization of βγ-CAT was detected by western blotting. The immunoblots are representative of three independent experiments, the original images of immunoblots are shown in Supplementary Figure 7. e FITC-labeled βγ-CAT was incubated with different concentrations of sulfatides and then mixed with THP-1 cells. The membrane binding of βγ-CAT was determined by ﬂow cytometry, the untreated cells were used as a negative control. f βγ-CAT was incubated with different concentrations of sulfatides, then mixed with THP-1 cells. The oligomerization of βγ-CAT was detected by western blotting. The immunoblots are representative of three independent experiments, the original images of immunoblots are shown in Supplementary Figure 7. g βγ-CAT was incubated with different concentrations of lipids and then added to LPS-primed THP-1 cells. The IL-1β concentrations in the supernatant were measured by ELISA. *P < 0.05, **P < 0.01 and ***P < 0.001 represent gangliosides and sulfatides versus sphingomyelin by two-way ANOVA with Bonferroni correction (n = 3). h, i The direct interaction between βγ-CAT and gangliosides (h) or sulfatides (i) was determined using a BLI assay. The BLI interaction curves are representative of three independent experiments. Bars represent the mean ± SD from three independent experiments per condition in a, b and g

Techniques Used: Incubation, Concentration Assay, Enzyme-linked Immunosorbent Assay, Control, Two Tailed Test, Labeling, Membrane, Binding Assay, Cytometry, Negative Control, Western Blot

Fig. 2 The BmALP1 and BmTFF3 subunits of βγ-CAT bound to gangliosides and sulfatides, respectively. a Schematic graph of βγ-CAT, BmALP1 subunit and BmTFF3 subunit. The BmALP1 subunit and BmTFF3 subunit of βγ-CAT have apparent molecular weights of 38 kDa and 18 kDa, respectively. b Interactions between MBP-αN and MBP-αC with gangliosides was detected by BLI assay. c Interactions between MBP-αN and MBP-αC with sulfatides was detected by BLI assay. d The binding kinetic curves between MBP-αC and gangliosides were determined by BLI assay. e βγ-CAT was incubated with different concentrations of anti-BmTFF3 polyclonal antibody or control IgG and added to LPS-primed THP-1 cells. The IL-1β concentration in the supernatant was measured by ELISA. Bars represent the mean ± SD from three independent experiments. *P < 0.05 and **P < 0.01 vs. control IgG by using unpaired two- tailed Student’s t test (n = 3). f FITC-labeled βγ-CAT was incubated with an anti-BmTFF3 polyclonal antibody or control rabbit IgG and added to THP-1 cells, the binding of βγ-CAT with THP-1 cells was evaluated by ﬂow cytometry. Untreated THP-1 cells are indicated as normal, and THP-1 cells treated with FITC-labeled βγ-CAT are indicated as the control. g βγ-CAT was incubated with an anti-BmTFF3 polyclonal antibody or control rabbit IgG and then added to THP-1 cells, the oligomerization of βγ-CAT was detected by western blotting. The immunoblots are representative of three independent experiments, the original images of immunoblots are shown in Supplementary Figure 8. h The binding of BmTFF3 with different types of sphingolipids was determined by protein-lipid overlay assay. The blots are representative of three independent experiments, the original images of blots are shown in Supplementary Figure 8. i The binding kinetic curves between BmTFF3 and sulfatides was determined by BLI assay. The BLI interaction curves in b–d and i are representative of three independent experiments

Figure Legend Snippet: Fig. 2 The BmALP1 and BmTFF3 subunits of βγ-CAT bound to gangliosides and sulfatides, respectively. a Schematic graph of βγ-CAT, BmALP1 subunit and BmTFF3 subunit. The BmALP1 subunit and BmTFF3 subunit of βγ-CAT have apparent molecular weights of 38 kDa and 18 kDa, respectively. b Interactions between MBP-αN and MBP-αC with gangliosides was detected by BLI assay. c Interactions between MBP-αN and MBP-αC with sulfatides was detected by BLI assay. d The binding kinetic curves between MBP-αC and gangliosides were determined by BLI assay. e βγ-CAT was incubated with different concentrations of anti-BmTFF3 polyclonal antibody or control IgG and added to LPS-primed THP-1 cells. The IL-1β concentration in the supernatant was measured by ELISA. Bars represent the mean ± SD from three independent experiments. *P < 0.05 and **P < 0.01 vs. control IgG by using unpaired two- tailed Student’s t test (n = 3). f FITC-labeled βγ-CAT was incubated with an anti-BmTFF3 polyclonal antibody or control rabbit IgG and added to THP-1 cells, the binding of βγ-CAT with THP-1 cells was evaluated by ﬂow cytometry. Untreated THP-1 cells are indicated as normal, and THP-1 cells treated with FITC-labeled βγ-CAT are indicated as the control. g βγ-CAT was incubated with an anti-BmTFF3 polyclonal antibody or control rabbit IgG and then added to THP-1 cells, the oligomerization of βγ-CAT was detected by western blotting. The immunoblots are representative of three independent experiments, the original images of immunoblots are shown in Supplementary Figure 8. h The binding of BmTFF3 with different types of sphingolipids was determined by protein-lipid overlay assay. The blots are representative of three independent experiments, the original images of blots are shown in Supplementary Figure 8. i The binding kinetic curves between BmTFF3 and sulfatides was determined by BLI assay. The BLI interaction curves in b–d and i are representative of three independent experiments

Techniques Used: Binding Assay, Incubation, Control, Concentration Assay, Enzyme-linked Immunosorbent Assay, Two Tailed Test, Labeling, Cytometry, Western Blot, Protein-lipid Overlay Assay (PLOA)

Fig. 4 AGSLs of the cell membrane were essential for the actions of βγ-CAT. a THP-1 cells were treated with PPMP and then incubated with FITC-labeled βγ-CAT. The binding between βγ-CAT and THP-1 cells was detected by ﬂow cytometry. b The oligomerization of βγ-CAT was determined by western blotting. The immunoblots are representative of three independent experiments, the original images of immunoblots are shown in Supplementary Figure 12. c The IL-1β release induced by βγ-CAT was measured by ELISA. *P < 0.05 vs. control by using unpaired two-tailed Student’s t test (n = 3). d–f THP-1 cells in which ganglioside expression was knocked down or gangliosides re-addition, then incubated with βγ-CAT. The binding between βγ-CAT and THP-1 cells was detected by ﬂow cytometry (d), the oligomerization of βγ-CAT was detected by western blotting (e), and the IL-1β concentration was measured by ELISA (f). *P < 0.05 vs. the respective control by using unpaired two-tailed Student’s t test (n = 3). The immunoblots (e) are representative of three independent experiments, the original images of immunoblots are shown in Supplementary Figure 13. g–i THP-1 cells in which sulfatide expression was knocked down or sulfatides re-addition, then incubated with βγ-CAT. The binding between βγ-CAT and THP-1 cells was detected by ﬂow cytometry (g), the oligomerization of βγ-CAT was detected by western blotting (h), and the IL-1β concentration was measured by ELISA (i). *P < 0.05 vs. the respective control by using unpaired two-tailed Student’s t test (n = 3). The immunoblots (h) are representative of three independent experiments, the original images of immunoblots are shown in Supplementary Figure 13. In ﬂow cytometry (a, d, g), the untreated THP-1 cells are indicated as normal, and THP-1 cells treated with FITC-labeled βγ-CAT are indicated as control. Bars represent the mean ± SD from three independent experiments per condition in c, f, i

Figure Legend Snippet: Fig. 4 AGSLs of the cell membrane were essential for the actions of βγ-CAT. a THP-1 cells were treated with PPMP and then incubated with FITC-labeled βγ-CAT. The binding between βγ-CAT and THP-1 cells was detected by ﬂow cytometry. b The oligomerization of βγ-CAT was determined by western blotting. The immunoblots are representative of three independent experiments, the original images of immunoblots are shown in Supplementary Figure 12. c The IL-1β release induced by βγ-CAT was measured by ELISA. *P < 0.05 vs. control by using unpaired two-tailed Student’s t test (n = 3). d–f THP-1 cells in which ganglioside expression was knocked down or gangliosides re-addition, then incubated with βγ-CAT. The binding between βγ-CAT and THP-1 cells was detected by ﬂow cytometry (d), the oligomerization of βγ-CAT was detected by western blotting (e), and the IL-1β concentration was measured by ELISA (f). *P < 0.05 vs. the respective control by using unpaired two-tailed Student’s t test (n = 3). The immunoblots (e) are representative of three independent experiments, the original images of immunoblots are shown in Supplementary Figure 13. g–i THP-1 cells in which sulfatide expression was knocked down or sulfatides re-addition, then incubated with βγ-CAT. The binding between βγ-CAT and THP-1 cells was detected by ﬂow cytometry (g), the oligomerization of βγ-CAT was detected by western blotting (h), and the IL-1β concentration was measured by ELISA (i). *P < 0.05 vs. the respective control by using unpaired two-tailed Student’s t test (n = 3). The immunoblots (h) are representative of three independent experiments, the original images of immunoblots are shown in Supplementary Figure 13. In ﬂow cytometry (a, d, g), the untreated THP-1 cells are indicated as normal, and THP-1 cells treated with FITC-labeled βγ-CAT are indicated as control. Bars represent the mean ± SD from three independent experiments per condition in c, f, i

Techniques Used: Membrane, Incubation, Labeling, Binding Assay, Cytometry, Western Blot, Enzyme-linked Immunosorbent Assay, Control, Two Tailed Test, Expressing, Concentration Assay

Fig. 6 The proposed action model and pathway of βγ-CAT. As a vertebrate-secreted ALP and TFF protein complex, βγ-CAT exerts its functions via an assembly process. The actions of assembled βγ-CAT can be divided into four steps. Step 1. Membrane binding. Once the assembled βγ-CAT encounters target cells, βγ-CAT is subsequently anchored to lipid raft microdomains on the plasma membrane. Therefore, the BmALP1 subunit of βγ-CAT binds to the extracellular glycan headgroup of gangliosides, and the BmTFF3 subunit of βγ-CAT binds to the extracellular glycan headgroup of sulfatides. Step 2. After βγ-CAT binding to the membrane, the BmTFF3 subunit detaches from the membrane, and the BmALP1 subunit of βγ-CAT is endocytosed and enters the cell. Step 3. The endocytic βγ-CAT then oligomerizes and forms pores in the membranes of endolysosomes. Step 4. The formed pores induce a ﬂux of substances, such as ions, ultimately regulating the properties of endolysosomes. As we observed previously, changes in the properties of endolysosomes can trigger various effects, such as the expulsion of pathogen-containing vesicles16 and increased lysosome destabilization, leading to inﬂammasome- dependent IL-1β release15 and tissue repair10

Figure Legend Snippet: Fig. 6 The proposed action model and pathway of βγ-CAT. As a vertebrate-secreted ALP and TFF protein complex, βγ-CAT exerts its functions via an assembly process. The actions of assembled βγ-CAT can be divided into four steps. Step 1. Membrane binding. Once the assembled βγ-CAT encounters target cells, βγ-CAT is subsequently anchored to lipid raft microdomains on the plasma membrane. Therefore, the BmALP1 subunit of βγ-CAT binds to the extracellular glycan headgroup of gangliosides, and the BmTFF3 subunit of βγ-CAT binds to the extracellular glycan headgroup of sulfatides. Step 2. After βγ-CAT binding to the membrane, the BmTFF3 subunit detaches from the membrane, and the BmALP1 subunit of βγ-CAT is endocytosed and enters the cell. Step 3. The endocytic βγ-CAT then oligomerizes and forms pores in the membranes of endolysosomes. Step 4. The formed pores induce a ﬂux of substances, such as ions, ultimately regulating the properties of endolysosomes. As we observed previously, changes in the properties of endolysosomes can trigger various effects, such as the expulsion of pathogen-containing vesicles16 and increased lysosome destabilization, leading to inﬂammasome- dependent IL-1β release15 and tissue repair10

Techniques Used: Membrane, Binding Assay, Clinical Proteomics, Glycoproteomics

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