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The relationship between <t>GDF15</t> and tubulointerstitial fibrosis mediated by TGF β in HK2 cells. (A–D) Screening the differentially expressed genes related to TIF. (E, F) Western blot analysis and quantification of fibronectin, collagen I, and GDF15 in HK2 cells stimulated with 10 ng/mL of TGF‐β1 for 12, 24, and 48 h. (G) qRT‐PCR analysis of fibronectin, collagen I, and GDF15 levels in different groups as indicated. The relative expression levels of the indicated proteins were normalised to that of β‐actin ( n = 3).* p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001.

Gdf15, supplied by Bioss, used in various techniques. Bioz Stars score: 93/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 93 stars, based on 11 article reviews

gdf15 - by Bioz Stars, 2026-03

93/100 stars

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1) Product Images from "Novel Roles of GDF15 in Alleviating Renal Fibrosis: Promoting Autophagy and Lysosome Biogenesis via Inhibition of the PI3K /Akt/ mTOR Pathway"

Article Title: Novel Roles of GDF15 in Alleviating Renal Fibrosis: Promoting Autophagy and Lysosome Biogenesis via Inhibition of the PI3K /Akt/ mTOR Pathway

Journal: Journal of Cellular and Molecular Medicine

doi: 10.1111/jcmm.70951

The relationship between GDF15 and tubulointerstitial fibrosis mediated by TGF β in HK2 cells. (A–D) Screening the differentially expressed genes related to TIF. (E, F) Western blot analysis and quantification of fibronectin, collagen I, and GDF15 in HK2 cells stimulated with 10 ng/mL of TGF‐β1 for 12, 24, and 48 h. (G) qRT‐PCR analysis of fibronectin, collagen I, and GDF15 levels in different groups as indicated. The relative expression levels of the indicated proteins were normalised to that of β‐actin ( n = 3).* p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001.

Figure Legend Snippet: The relationship between GDF15 and tubulointerstitial fibrosis mediated by TGF β in HK2 cells. (A–D) Screening the differentially expressed genes related to TIF. (E, F) Western blot analysis and quantification of fibronectin, collagen I, and GDF15 in HK2 cells stimulated with 10 ng/mL of TGF‐β1 for 12, 24, and 48 h. (G) qRT‐PCR analysis of fibronectin, collagen I, and GDF15 levels in different groups as indicated. The relative expression levels of the indicated proteins were normalised to that of β‐actin ( n = 3).* p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001.

Techniques Used: Western Blot, Quantitative RT-PCR, Expressing

GDF15 expression in the fibrotic kidney of patients with CKD and UUO mice. (A) Immunohistochemical staining for Collagen I, GDF15 and representative images of Masson's trichrome staining in the kidneys of patients with CKD. (B) Correlation between Collagen I, serum creatinine, eGFR and the expression of renal GDF15 in patients with CKD. (C, E) Western blot analysis and quantification of the GDF15 and GFRAL levels in UUO mice. The relative expression levels of the indicated proteins were normalised to that of β‐actin. (D) Immunohistochemical staining for Collagen I, GDF15 and representative images of Masson's trichrome staining, Picrosirius red staining in the kidneys of UUO mice. (F) Quantitative analysis of immunohistochemistry for GDF15 in the cortex and medulla of UUO mice ( n = 6). (G) Dynamic changes in serum GDF15 concentrations at different time points following UUO intervention in mice and GDF15 levels in the supernatant of TGF‐β1‐stimulated HK2 cells ( n = 3). (H) Co‐staining of GDF15 with AGTR1: A distinct yellow signal in the merged image indicates that GDF15 is primarily localised in AGTR1‐positive tubular epithelial cells. (I) Co‐staining of GDF15 with the proximal tubule marker LTL: Absence of a yellow overlap in the merged image suggests weak GDF15 expression in proximal tubules. (J) Co‐staining of GDF15 with the collecting duct marker AQP2: No overlap signal is observed in the merged image, indicating minimal GDF15 expression in collecting ducts. (K) Co‐staining of GDF15 with WT1, a podocyte marker: The merged image shows no co‐localisation, suggesting that GDF15 is not expressed in glomerular podocytes. (L) Co‐staining of GFRAL with NCC: Strong overlap of red and green signals in the merged image indicates predominant localisation of GFRAL in the distal tubules. (M) Co‐staining of GFRAL with AQP2: No overlapping signal is observed in the merged image, demonstrating that GFRAL is not expressed in collecting ducts. Scale bars for all merged images = 50 μm ( n = 6). * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001.

Figure Legend Snippet: GDF15 expression in the fibrotic kidney of patients with CKD and UUO mice. (A) Immunohistochemical staining for Collagen I, GDF15 and representative images of Masson's trichrome staining in the kidneys of patients with CKD. (B) Correlation between Collagen I, serum creatinine, eGFR and the expression of renal GDF15 in patients with CKD. (C, E) Western blot analysis and quantification of the GDF15 and GFRAL levels in UUO mice. The relative expression levels of the indicated proteins were normalised to that of β‐actin. (D) Immunohistochemical staining for Collagen I, GDF15 and representative images of Masson's trichrome staining, Picrosirius red staining in the kidneys of UUO mice. (F) Quantitative analysis of immunohistochemistry for GDF15 in the cortex and medulla of UUO mice ( n = 6). (G) Dynamic changes in serum GDF15 concentrations at different time points following UUO intervention in mice and GDF15 levels in the supernatant of TGF‐β1‐stimulated HK2 cells ( n = 3). (H) Co‐staining of GDF15 with AGTR1: A distinct yellow signal in the merged image indicates that GDF15 is primarily localised in AGTR1‐positive tubular epithelial cells. (I) Co‐staining of GDF15 with the proximal tubule marker LTL: Absence of a yellow overlap in the merged image suggests weak GDF15 expression in proximal tubules. (J) Co‐staining of GDF15 with the collecting duct marker AQP2: No overlap signal is observed in the merged image, indicating minimal GDF15 expression in collecting ducts. (K) Co‐staining of GDF15 with WT1, a podocyte marker: The merged image shows no co‐localisation, suggesting that GDF15 is not expressed in glomerular podocytes. (L) Co‐staining of GFRAL with NCC: Strong overlap of red and green signals in the merged image indicates predominant localisation of GFRAL in the distal tubules. (M) Co‐staining of GFRAL with AQP2: No overlapping signal is observed in the merged image, demonstrating that GFRAL is not expressed in collecting ducts. Scale bars for all merged images = 50 μm ( n = 6). * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001.

Techniques Used: Expressing, Immunohistochemical staining, Staining, Western Blot, Immunohistochemistry, Marker

Downregulation of GDF15 enhances TGF β‐stimulated TIF in vitro and UUO‐induced TIF in vivo. (A) Representative images of Masson's trichrome staining, Picrosirius red staining and immunohistochemical staining for Collagen I, Fibronectin, and macrophage infiltration in the kidney homogenates from sham and UUO mice injected with shNC or sh556. (B) Quantitative analysis of immunohistochemistry for Collagen I, Fibronectin and macrophage in different groups as indicated. (C, E) Western blot analysis and quantification of the Collagen I, Fibronectin and GDF15 in vitro ( n = 3). The relative expression levels of the indicated proteins were normalised to that of β‐actin. (G) qRT‐PCR analysis of fibronectin, collagen I, and GDF15 levels in vitro ( n = 3). (D, F) Western blot analysis and quantification of the Collagen I, Fibronectin and GDF15 in vivo. The relative expression levels of the indicated proteins were normalised to that of β‐actin ( n = 6). (H) qRT‐PCR analysis of fibronectin, collagen I, and GDF15 levels in vivo ( n = 6). * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001.

Figure Legend Snippet: Downregulation of GDF15 enhances TGF β‐stimulated TIF in vitro and UUO‐induced TIF in vivo. (A) Representative images of Masson's trichrome staining, Picrosirius red staining and immunohistochemical staining for Collagen I, Fibronectin, and macrophage infiltration in the kidney homogenates from sham and UUO mice injected with shNC or sh556. (B) Quantitative analysis of immunohistochemistry for Collagen I, Fibronectin and macrophage in different groups as indicated. (C, E) Western blot analysis and quantification of the Collagen I, Fibronectin and GDF15 in vitro ( n = 3). The relative expression levels of the indicated proteins were normalised to that of β‐actin. (G) qRT‐PCR analysis of fibronectin, collagen I, and GDF15 levels in vitro ( n = 3). (D, F) Western blot analysis and quantification of the Collagen I, Fibronectin and GDF15 in vivo. The relative expression levels of the indicated proteins were normalised to that of β‐actin ( n = 6). (H) qRT‐PCR analysis of fibronectin, collagen I, and GDF15 levels in vivo ( n = 6). * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001.

Techniques Used: In Vitro, In Vivo, Staining, Immunohistochemical staining, Injection, Immunohistochemistry, Western Blot, Expressing, Quantitative RT-PCR

Overexpression of GDF15 ameliorated TGF‐β‐stimulated TIF in vitro and UUO‐induced TIF in vivo. (A) Representative images of Masson's trichrome staining, Picrosirius red staining and immunohistochemical staining for Collagen I, Fibronectin, and macrophage infiltration in the kidney homogenates from sham and UUO mice injected with empty vector or pGV362‐GDF15. (B) Quantitative analysis of immunohistochemistry for Collagen I, Fibronectin and GDF15 in different groups as indicated. (C, E) Western blot analysis and quantification of the Collagen I, Fibronectin and GDF15 in vitro ( n = 3). The relative expression levels of the indicated proteins were normalised to that of β‐actin. (G) qRT‐PCR analysis of fibronectin, collagen I, and GDF15 levels in vitro ( n = 3). (D, F) Western blot analysis and quantification of the Collagen I, Fibronectin and GDF15 in vivo. The relative expression levels of the indicated proteins were normalised to that of β‐actin ( n = 6). (H) qRT‐PCR analysis of fibronectin, collagen I, and GDF15 levels in vivo ( n = 6). * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001.

Figure Legend Snippet: Overexpression of GDF15 ameliorated TGF‐β‐stimulated TIF in vitro and UUO‐induced TIF in vivo. (A) Representative images of Masson's trichrome staining, Picrosirius red staining and immunohistochemical staining for Collagen I, Fibronectin, and macrophage infiltration in the kidney homogenates from sham and UUO mice injected with empty vector or pGV362‐GDF15. (B) Quantitative analysis of immunohistochemistry for Collagen I, Fibronectin and GDF15 in different groups as indicated. (C, E) Western blot analysis and quantification of the Collagen I, Fibronectin and GDF15 in vitro ( n = 3). The relative expression levels of the indicated proteins were normalised to that of β‐actin. (G) qRT‐PCR analysis of fibronectin, collagen I, and GDF15 levels in vitro ( n = 3). (D, F) Western blot analysis and quantification of the Collagen I, Fibronectin and GDF15 in vivo. The relative expression levels of the indicated proteins were normalised to that of β‐actin ( n = 6). (H) qRT‐PCR analysis of fibronectin, collagen I, and GDF15 levels in vivo ( n = 6). * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001.

Techniques Used: Over Expression, In Vitro, In Vivo, Staining, Immunohistochemical staining, Injection, Plasmid Preparation, Immunohistochemistry, Western Blot, Expressing, Quantitative RT-PCR

GDF15 ameliorates renal fibrosis through enhancing autophagy. (A) Bioinformatics predicts the mechanism of GDF15: PCA; Differentially clustered volcano plot; Top 15 of GO enrichment. (B) Western blot analysis of the LC3B, Beclin1 and p62 in TGF‐β‐stimulated TIF with transfection of shNC or sh865 ( n = 3). (C, F) Western blot analysis and quantification of the LC3B, Beclin1 in UUO‐induced TIF with injecting shNC or sh556 ( n = 6). (D) Western blot analysis of the LC3B, Beclin1 and p62 in TGF‐β‐stimulated TIF with transfection of empty vector or pGV362‐GDF15 ( n = 3). (E, G) Western blot analysis and quantification of the LC3B, Beclin1 in UUO‐induced TIF with injecting empty vector or pGV362‐GDF15 ( n = 6). (H) Western blot analysis the Collagen I and Fibronectin in TGF‐β‐stimulated TIF with transfection of empty vector, pGV362‐GDF15 and chloroquine treatment ( n = 3). (I) qRT‐PCR analysis of fibronectin and collagen I levels in different groups as indicated. * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001.

Figure Legend Snippet: GDF15 ameliorates renal fibrosis through enhancing autophagy. (A) Bioinformatics predicts the mechanism of GDF15: PCA; Differentially clustered volcano plot; Top 15 of GO enrichment. (B) Western blot analysis of the LC3B, Beclin1 and p62 in TGF‐β‐stimulated TIF with transfection of shNC or sh865 ( n = 3). (C, F) Western blot analysis and quantification of the LC3B, Beclin1 in UUO‐induced TIF with injecting shNC or sh556 ( n = 6). (D) Western blot analysis of the LC3B, Beclin1 and p62 in TGF‐β‐stimulated TIF with transfection of empty vector or pGV362‐GDF15 ( n = 3). (E, G) Western blot analysis and quantification of the LC3B, Beclin1 in UUO‐induced TIF with injecting empty vector or pGV362‐GDF15 ( n = 6). (H) Western blot analysis the Collagen I and Fibronectin in TGF‐β‐stimulated TIF with transfection of empty vector, pGV362‐GDF15 and chloroquine treatment ( n = 3). (I) qRT‐PCR analysis of fibronectin and collagen I levels in different groups as indicated. * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001.

Techniques Used: Western Blot, Transfection, Plasmid Preparation, Quantitative RT-PCR

GDF15 ameliorates renal fibrosis through improving lysosomal neogenesis. (A) GSEA enrichment. (B) Downregulation of kidney GDF15 in the UUO model, electron microscopy detected the number of lysosomes (i, ii), the scale bars in the upper‐row images represent 2 μm, and those in the lower‐row images represent 500 nm and immunohistochemical staining analysis of the LAMP (iii). (C) qRT‐PCR analysis of Lamp1 and Lamp2 in different groups as indicated. (D) Overexpression of kidney GDF15 in the UUO model, electron microscopy detected the number of lysosomes (i, ii), the scale bars in the upper‐row images represent 2 μm, and those in the lower‐row images represent 500 nm and immunohistochemical staining analysis of the LAMP (iii). (E) qRT‐PCR analysis of Lamp1 and Lamp2 in different groups as indicated ( n = 3). * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001.

Figure Legend Snippet: GDF15 ameliorates renal fibrosis through improving lysosomal neogenesis. (A) GSEA enrichment. (B) Downregulation of kidney GDF15 in the UUO model, electron microscopy detected the number of lysosomes (i, ii), the scale bars in the upper‐row images represent 2 μm, and those in the lower‐row images represent 500 nm and immunohistochemical staining analysis of the LAMP (iii). (C) qRT‐PCR analysis of Lamp1 and Lamp2 in different groups as indicated. (D) Overexpression of kidney GDF15 in the UUO model, electron microscopy detected the number of lysosomes (i, ii), the scale bars in the upper‐row images represent 2 μm, and those in the lower‐row images represent 500 nm and immunohistochemical staining analysis of the LAMP (iii). (E) qRT‐PCR analysis of Lamp1 and Lamp2 in different groups as indicated ( n = 3). * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001.

Techniques Used: Electron Microscopy, Immunohistochemical staining, Staining, Quantitative RT-PCR, Over Expression

GDF15 promoted autophagy and lysosome biogenesis by inhibiting the PI3K/Akt/mTOR pathway. (A) Downregulation of kidney GDF15 in the UUO model, Western blot analysis and quantification of TFEB. The relative expression levels of the indicated proteins were normalised to that of β‐actin. (B) qRT‐PCR analysis of TFEB and PASP in different groups as indicated. (C) Overexpression of kidney GDF15 in the UUO model, Western blot analysis and quantification of TFEB. The relative expression levels of the indicated proteins were normalised to that of β‐actin. (D) qRT‐PCR analysis of TFEB and PASP in different groups as indicated. (E) Western blot analysis of p‐mTOR, mTOR, p‐Akt, Akt, p‐PI3K, and PI3K levels in TGF β‐stimulated TIF with transfection of empty vector or pGV362‐GDF15. (F, G) Effects of GDF15 silencing and PI3K inhibition on the PI3K signalling pathway and the expression of fibrosis‐ and autophagy‐related proteins. HK‐2 cells were transfected with shGDF15 (sh865) or control vector (shNC) for 48 h, followed by treatment with the PI3K inhibitor LY294002 (final concentration 20 μM) for 24 h. Western blot and quantification was performed to detect the expression levels of p‐PI3K, PI3K, fibronectin, collagen I, TFEB, and the internal control β‐actin. All data were normalised to β‐actin ( n = 3). * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001.

Figure Legend Snippet: GDF15 promoted autophagy and lysosome biogenesis by inhibiting the PI3K/Akt/mTOR pathway. (A) Downregulation of kidney GDF15 in the UUO model, Western blot analysis and quantification of TFEB. The relative expression levels of the indicated proteins were normalised to that of β‐actin. (B) qRT‐PCR analysis of TFEB and PASP in different groups as indicated. (C) Overexpression of kidney GDF15 in the UUO model, Western blot analysis and quantification of TFEB. The relative expression levels of the indicated proteins were normalised to that of β‐actin. (D) qRT‐PCR analysis of TFEB and PASP in different groups as indicated. (E) Western blot analysis of p‐mTOR, mTOR, p‐Akt, Akt, p‐PI3K, and PI3K levels in TGF β‐stimulated TIF with transfection of empty vector or pGV362‐GDF15. (F, G) Effects of GDF15 silencing and PI3K inhibition on the PI3K signalling pathway and the expression of fibrosis‐ and autophagy‐related proteins. HK‐2 cells were transfected with shGDF15 (sh865) or control vector (shNC) for 48 h, followed by treatment with the PI3K inhibitor LY294002 (final concentration 20 μM) for 24 h. Western blot and quantification was performed to detect the expression levels of p‐PI3K, PI3K, fibronectin, collagen I, TFEB, and the internal control β‐actin. All data were normalised to β‐actin ( n = 3). * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001.

Techniques Used: Western Blot, Expressing, Quantitative RT-PCR, Over Expression, Transfection, Plasmid Preparation, Inhibition, Control, Concentration Assay

GDF15 mediates autophagy activation and anti‐fibrotic effects through GFRAL. (A) Western blot analysis and quantification of GFRAL protein expression in HK2 cells following siRNA‐mediated knockdown. siNC served as the negative control, and siGFRAL#1, #2, and #3 represent different interference sequences. (B) Western blot analysis and quantification of fibronectin, collagen I, and GDF15 protein expression in various treatment groups (Vector, GDF15, GDF15 + siNC, GDF15 + siGFRAL) under TGF‐β stimulation. β‐actin was used as the loading control. (C) Western blot analysis and quantification of LC3B, P62, and Beclin1 protein levels in each group. (D) Western blot analysis and quantification of TFEB protein expression in each group. (E) Transmission electron microscopy was used to observe the structural changes of lysosomes in HK2 cells from each group. The scale bars in the upper‐row images represent 1 μm, and those in the lower‐row images represent 500 nm. (F) qRT‐PCR analysis of Lamp1 and Lamp2 in different groups as indicated. (G) Western blot analysis and quantification of PI3K/AKT/mTOR signalling pathway proteins, including p‐mTOR, mTOR, p‐AKT, AKT, p‐PI3K, and PI3K. β‐actin was used as the loading control ( n = 3).* p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001.

Figure Legend Snippet: GDF15 mediates autophagy activation and anti‐fibrotic effects through GFRAL. (A) Western blot analysis and quantification of GFRAL protein expression in HK2 cells following siRNA‐mediated knockdown. siNC served as the negative control, and siGFRAL#1, #2, and #3 represent different interference sequences. (B) Western blot analysis and quantification of fibronectin, collagen I, and GDF15 protein expression in various treatment groups (Vector, GDF15, GDF15 + siNC, GDF15 + siGFRAL) under TGF‐β stimulation. β‐actin was used as the loading control. (C) Western blot analysis and quantification of LC3B, P62, and Beclin1 protein levels in each group. (D) Western blot analysis and quantification of TFEB protein expression in each group. (E) Transmission electron microscopy was used to observe the structural changes of lysosomes in HK2 cells from each group. The scale bars in the upper‐row images represent 1 μm, and those in the lower‐row images represent 500 nm. (F) qRT‐PCR analysis of Lamp1 and Lamp2 in different groups as indicated. (G) Western blot analysis and quantification of PI3K/AKT/mTOR signalling pathway proteins, including p‐mTOR, mTOR, p‐AKT, AKT, p‐PI3K, and PI3K. β‐actin was used as the loading control ( n = 3).* p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001.

Techniques Used: Activation Assay, Western Blot, Expressing, Knockdown, Negative Control, Plasmid Preparation, Control, Transmission Assay, Electron Microscopy, Quantitative RT-PCR

Image Search Results

TNF-α modulates the WISP1 expression in stroma cells of the human bladder. (A) The RT-qPCR determined the expression of WISP1 in the human bladder cells. (B) Two WISP1 isoforms (WISP1v1 and WISP1v2) were found in the human bladder fibroblast (HBdSF) and bladder smooth muscle (HBdSMC) cells by RT-PCR with the pair of primers as shown. The expressions of WISP1, IL-6, CXCL5, CXCL12, and GDF15 of the HBdSF (C) and HBdSMC (D) cells after 10 ng/ml TNF-α treatment assessed by RT-qPCR. WISP1 (E) and IL-6 (F) secretions after TNF-α (0 – 20 ng/mL) treatments in HBdSF cells. Secretion of WISP1 (G) and IL-6 (F) in HBdSMC_shCOL and HBdSMC_shWISP1 cells treated with/without 10 ng/ml of TNF-α. Data are presented as the mean percentage (± SE; n = 4) in relation to the vehicle-treated HBdSMC_shCOL cells. (I) WISP1 secretion after 20 μM CAPE and/or TNF-α in HBdSF cells determined by ELISA assays. Data are presented as the mean percentage (±SE; n = 4) in relation to the vehicle-treated HBdSF cells. (J) The luciferase activity of the WISP1 reporter vector when HBdSMC cells were treated with TNF-α (10 ng/mL) and/or 20 μM CAPE for 24 h. * p < 0.05; ** p < 0.01; ND: no detectable.

Journal: Translational Oncology

Article Title: WISP1 is the stromal-secreting oncoprotein via paracrine downregulation of NDRG1, KAI1, and Maspin in human bladder cancer cells

doi: 10.1016/j.tranon.2026.102680

Figure Lengend Snippet: TNF-α modulates the WISP1 expression in stroma cells of the human bladder. (A) The RT-qPCR determined the expression of WISP1 in the human bladder cells. (B) Two WISP1 isoforms (WISP1v1 and WISP1v2) were found in the human bladder fibroblast (HBdSF) and bladder smooth muscle (HBdSMC) cells by RT-PCR with the pair of primers as shown. The expressions of WISP1, IL-6, CXCL5, CXCL12, and GDF15 of the HBdSF (C) and HBdSMC (D) cells after 10 ng/ml TNF-α treatment assessed by RT-qPCR. WISP1 (E) and IL-6 (F) secretions after TNF-α (0 – 20 ng/mL) treatments in HBdSF cells. Secretion of WISP1 (G) and IL-6 (F) in HBdSMC_shCOL and HBdSMC_shWISP1 cells treated with/without 10 ng/ml of TNF-α. Data are presented as the mean percentage (± SE; n = 4) in relation to the vehicle-treated HBdSMC_shCOL cells. (I) WISP1 secretion after 20 μM CAPE and/or TNF-α in HBdSF cells determined by ELISA assays. Data are presented as the mean percentage (±SE; n = 4) in relation to the vehicle-treated HBdSF cells. (J) The luciferase activity of the WISP1 reporter vector when HBdSMC cells were treated with TNF-α (10 ng/mL) and/or 20 μM CAPE for 24 h. * p < 0.05; ** p < 0.01; ND: no detectable.

Article Snippet: TaqManTM gene expression master mix and polymerase chain reaction (PCR) FAM dye-labeled TaqMan MGB probes for human WISP1 (Hs04234730_m1 for total isoforms and Hs00180245 for WISP1v1), α-SMA (Hs00426835_g1), IL-6 (Hs00985639_m1), GDF15 (Hs00171132_m1), CXCL5 (Hs01099660_g1), SDF-1/CXCL12 (Hs03676656_m1), NDRG1 (Hs00608387_m1), KAI1 (Hs00356310_m1), Maspin (Hs00985283_m1), E-cadherin (Hs01023894_m1), N-cadherin (Hs00169953_m1), Snail (Hs00195591_m1), Slug (Hs00161904_m1), Vimentin (Hs00185584_m1), and β-actin (Hs01060665_g1) were purchased from Thermo Fisher Scientific Inc. (Vilnius, Lithuania).

Techniques: Expressing, Quantitative RT-PCR, Reverse Transcription Polymerase Chain Reaction, Enzyme-linked Immunosorbent Assay, Luciferase, Activity Assay, Plasmid Preparation

WISP1 modulates expressions of α-SMA, IL-6, GDF15, and CXCL5 in bladder stroma cells. The mRNA levels of two WISP1 isoforms (WISP1v1 and WISP1v2) after WISP1 knock-downed in the HBdSF (A) and HBdSMC (B) cells were determined by RT-PCR. The protein levels with quantification analysis of WISP1, GDF15, and α-SMA of HBdSMC (C) and HBdSF (D) cells after mock-knockdown or WISP1-knockdown were assessed by immunoblot assays. The mRNA levels of the WISP1, α-SMA, IL-6, GDF15, and CXCL5 after knockdown of WISP1 in the HBdSMC (E) and HBdSF (F) cells, as indicated, were determined by RT-qPCR. Data are presented as target genes/β-actin of mock-knockdown cells relative to WISP1-knockdown cells. ** p < 0.01.

Journal: Translational Oncology

Article Title: WISP1 is the stromal-secreting oncoprotein via paracrine downregulation of NDRG1, KAI1, and Maspin in human bladder cancer cells

doi: 10.1016/j.tranon.2026.102680

Figure Lengend Snippet: WISP1 modulates expressions of α-SMA, IL-6, GDF15, and CXCL5 in bladder stroma cells. The mRNA levels of two WISP1 isoforms (WISP1v1 and WISP1v2) after WISP1 knock-downed in the HBdSF (A) and HBdSMC (B) cells were determined by RT-PCR. The protein levels with quantification analysis of WISP1, GDF15, and α-SMA of HBdSMC (C) and HBdSF (D) cells after mock-knockdown or WISP1-knockdown were assessed by immunoblot assays. The mRNA levels of the WISP1, α-SMA, IL-6, GDF15, and CXCL5 after knockdown of WISP1 in the HBdSMC (E) and HBdSF (F) cells, as indicated, were determined by RT-qPCR. Data are presented as target genes/β-actin of mock-knockdown cells relative to WISP1-knockdown cells. ** p < 0.01.

Techniques: Reverse Transcription Polymerase Chain Reaction, Knockdown, Western Blot, Quantitative RT-PCR

Journal: Journal of Cellular and Molecular Medicine

Article Title: Novel Roles of GDF15 in Alleviating Renal Fibrosis: Promoting Autophagy and Lysosome Biogenesis via Inhibition of the PI3K /Akt/ mTOR Pathway

doi: 10.1111/jcmm.70951

Figure Lengend Snippet: The relationship between GDF15 and tubulointerstitial fibrosis mediated by TGF β in HK2 cells. (A–D) Screening the differentially expressed genes related to TIF. (E, F) Western blot analysis and quantification of fibronectin, collagen I, and GDF15 in HK2 cells stimulated with 10 ng/mL of TGF‐β1 for 12, 24, and 48 h. (G) qRT‐PCR analysis of fibronectin, collagen I, and GDF15 levels in different groups as indicated. The relative expression levels of the indicated proteins were normalised to that of β‐actin ( n = 3).* p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001.

Article Snippet: After blocking non‐specific binding with 5% BSA for 1 h, we incubated the membranes overnight at 4°C with primary antibodies against the following: collagen IA (1:1000; BA0325; Boster), Beclin1 (1:1000; T55092 ; Abmart), P62 (1:1000; T55546 ; Abmart), LC3B (1:1000; T55992 ; Abmart), total PI3K (1:1000; T40064 ; Abmart), phospho‐PI3K (1:1000; T40065 ; Abmart), total mTOR (1:1000; T55306 ; Abmart), phospho‐mTOR (1:1000; T56571 ; Abmart), TFEB (1:1000; TA7015; Abmart), total Akt (1:1000; 60203–2‐Ig; Proteintech), phospho‐Akt (1:1000; 66444–1‐Ig; Proteintech), fibronectin (1:1000; ab2413; Abcam), GDF15 (1:500; BS3818‐R; Bioss), and anti‐GFRAL (1:1000; ab214929; Abcam).

Techniques: Western Blot, Quantitative RT-PCR, Expressing

Journal: Journal of Cellular and Molecular Medicine

Article Title: Novel Roles of GDF15 in Alleviating Renal Fibrosis: Promoting Autophagy and Lysosome Biogenesis via Inhibition of the PI3K /Akt/ mTOR Pathway

doi: 10.1111/jcmm.70951

Figure Lengend Snippet: GDF15 expression in the fibrotic kidney of patients with CKD and UUO mice. (A) Immunohistochemical staining for Collagen I, GDF15 and representative images of Masson's trichrome staining in the kidneys of patients with CKD. (B) Correlation between Collagen I, serum creatinine, eGFR and the expression of renal GDF15 in patients with CKD. (C, E) Western blot analysis and quantification of the GDF15 and GFRAL levels in UUO mice. The relative expression levels of the indicated proteins were normalised to that of β‐actin. (D) Immunohistochemical staining for Collagen I, GDF15 and representative images of Masson's trichrome staining, Picrosirius red staining in the kidneys of UUO mice. (F) Quantitative analysis of immunohistochemistry for GDF15 in the cortex and medulla of UUO mice ( n = 6). (G) Dynamic changes in serum GDF15 concentrations at different time points following UUO intervention in mice and GDF15 levels in the supernatant of TGF‐β1‐stimulated HK2 cells ( n = 3). (H) Co‐staining of GDF15 with AGTR1: A distinct yellow signal in the merged image indicates that GDF15 is primarily localised in AGTR1‐positive tubular epithelial cells. (I) Co‐staining of GDF15 with the proximal tubule marker LTL: Absence of a yellow overlap in the merged image suggests weak GDF15 expression in proximal tubules. (J) Co‐staining of GDF15 with the collecting duct marker AQP2: No overlap signal is observed in the merged image, indicating minimal GDF15 expression in collecting ducts. (K) Co‐staining of GDF15 with WT1, a podocyte marker: The merged image shows no co‐localisation, suggesting that GDF15 is not expressed in glomerular podocytes. (L) Co‐staining of GFRAL with NCC: Strong overlap of red and green signals in the merged image indicates predominant localisation of GFRAL in the distal tubules. (M) Co‐staining of GFRAL with AQP2: No overlapping signal is observed in the merged image, demonstrating that GFRAL is not expressed in collecting ducts. Scale bars for all merged images = 50 μm ( n = 6). * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001.

Techniques: Expressing, Immunohistochemical staining, Staining, Western Blot, Immunohistochemistry, Marker

Journal: Journal of Cellular and Molecular Medicine

Article Title: Novel Roles of GDF15 in Alleviating Renal Fibrosis: Promoting Autophagy and Lysosome Biogenesis via Inhibition of the PI3K /Akt/ mTOR Pathway

doi: 10.1111/jcmm.70951

Figure Lengend Snippet: Downregulation of GDF15 enhances TGF β‐stimulated TIF in vitro and UUO‐induced TIF in vivo. (A) Representative images of Masson's trichrome staining, Picrosirius red staining and immunohistochemical staining for Collagen I, Fibronectin, and macrophage infiltration in the kidney homogenates from sham and UUO mice injected with shNC or sh556. (B) Quantitative analysis of immunohistochemistry for Collagen I, Fibronectin and macrophage in different groups as indicated. (C, E) Western blot analysis and quantification of the Collagen I, Fibronectin and GDF15 in vitro ( n = 3). The relative expression levels of the indicated proteins were normalised to that of β‐actin. (G) qRT‐PCR analysis of fibronectin, collagen I, and GDF15 levels in vitro ( n = 3). (D, F) Western blot analysis and quantification of the Collagen I, Fibronectin and GDF15 in vivo. The relative expression levels of the indicated proteins were normalised to that of β‐actin ( n = 6). (H) qRT‐PCR analysis of fibronectin, collagen I, and GDF15 levels in vivo ( n = 6). * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001.

Techniques: In Vitro, In Vivo, Staining, Immunohistochemical staining, Injection, Immunohistochemistry, Western Blot, Expressing, Quantitative RT-PCR

Journal: Journal of Cellular and Molecular Medicine

Article Title: Novel Roles of GDF15 in Alleviating Renal Fibrosis: Promoting Autophagy and Lysosome Biogenesis via Inhibition of the PI3K /Akt/ mTOR Pathway

doi: 10.1111/jcmm.70951

Figure Lengend Snippet: Overexpression of GDF15 ameliorated TGF‐β‐stimulated TIF in vitro and UUO‐induced TIF in vivo. (A) Representative images of Masson's trichrome staining, Picrosirius red staining and immunohistochemical staining for Collagen I, Fibronectin, and macrophage infiltration in the kidney homogenates from sham and UUO mice injected with empty vector or pGV362‐GDF15. (B) Quantitative analysis of immunohistochemistry for Collagen I, Fibronectin and GDF15 in different groups as indicated. (C, E) Western blot analysis and quantification of the Collagen I, Fibronectin and GDF15 in vitro ( n = 3). The relative expression levels of the indicated proteins were normalised to that of β‐actin. (G) qRT‐PCR analysis of fibronectin, collagen I, and GDF15 levels in vitro ( n = 3). (D, F) Western blot analysis and quantification of the Collagen I, Fibronectin and GDF15 in vivo. The relative expression levels of the indicated proteins were normalised to that of β‐actin ( n = 6). (H) qRT‐PCR analysis of fibronectin, collagen I, and GDF15 levels in vivo ( n = 6). * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001.

Techniques: Over Expression, In Vitro, In Vivo, Staining, Immunohistochemical staining, Injection, Plasmid Preparation, Immunohistochemistry, Western Blot, Expressing, Quantitative RT-PCR

Journal: Journal of Cellular and Molecular Medicine

Article Title: Novel Roles of GDF15 in Alleviating Renal Fibrosis: Promoting Autophagy and Lysosome Biogenesis via Inhibition of the PI3K /Akt/ mTOR Pathway

doi: 10.1111/jcmm.70951

Figure Lengend Snippet: GDF15 ameliorates renal fibrosis through enhancing autophagy. (A) Bioinformatics predicts the mechanism of GDF15: PCA; Differentially clustered volcano plot; Top 15 of GO enrichment. (B) Western blot analysis of the LC3B, Beclin1 and p62 in TGF‐β‐stimulated TIF with transfection of shNC or sh865 ( n = 3). (C, F) Western blot analysis and quantification of the LC3B, Beclin1 in UUO‐induced TIF with injecting shNC or sh556 ( n = 6). (D) Western blot analysis of the LC3B, Beclin1 and p62 in TGF‐β‐stimulated TIF with transfection of empty vector or pGV362‐GDF15 ( n = 3). (E, G) Western blot analysis and quantification of the LC3B, Beclin1 in UUO‐induced TIF with injecting empty vector or pGV362‐GDF15 ( n = 6). (H) Western blot analysis the Collagen I and Fibronectin in TGF‐β‐stimulated TIF with transfection of empty vector, pGV362‐GDF15 and chloroquine treatment ( n = 3). (I) qRT‐PCR analysis of fibronectin and collagen I levels in different groups as indicated. * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001.

Techniques: Western Blot, Transfection, Plasmid Preparation, Quantitative RT-PCR

Journal: Journal of Cellular and Molecular Medicine

Article Title: Novel Roles of GDF15 in Alleviating Renal Fibrosis: Promoting Autophagy and Lysosome Biogenesis via Inhibition of the PI3K /Akt/ mTOR Pathway

doi: 10.1111/jcmm.70951

Figure Lengend Snippet: GDF15 ameliorates renal fibrosis through improving lysosomal neogenesis. (A) GSEA enrichment. (B) Downregulation of kidney GDF15 in the UUO model, electron microscopy detected the number of lysosomes (i, ii), the scale bars in the upper‐row images represent 2 μm, and those in the lower‐row images represent 500 nm and immunohistochemical staining analysis of the LAMP (iii). (C) qRT‐PCR analysis of Lamp1 and Lamp2 in different groups as indicated. (D) Overexpression of kidney GDF15 in the UUO model, electron microscopy detected the number of lysosomes (i, ii), the scale bars in the upper‐row images represent 2 μm, and those in the lower‐row images represent 500 nm and immunohistochemical staining analysis of the LAMP (iii). (E) qRT‐PCR analysis of Lamp1 and Lamp2 in different groups as indicated ( n = 3). * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001.

Techniques: Electron Microscopy, Immunohistochemical staining, Staining, Quantitative RT-PCR, Over Expression

Journal: Journal of Cellular and Molecular Medicine

Article Title: Novel Roles of GDF15 in Alleviating Renal Fibrosis: Promoting Autophagy and Lysosome Biogenesis via Inhibition of the PI3K /Akt/ mTOR Pathway

doi: 10.1111/jcmm.70951

Figure Lengend Snippet: GDF15 promoted autophagy and lysosome biogenesis by inhibiting the PI3K/Akt/mTOR pathway. (A) Downregulation of kidney GDF15 in the UUO model, Western blot analysis and quantification of TFEB. The relative expression levels of the indicated proteins were normalised to that of β‐actin. (B) qRT‐PCR analysis of TFEB and PASP in different groups as indicated. (C) Overexpression of kidney GDF15 in the UUO model, Western blot analysis and quantification of TFEB. The relative expression levels of the indicated proteins were normalised to that of β‐actin. (D) qRT‐PCR analysis of TFEB and PASP in different groups as indicated. (E) Western blot analysis of p‐mTOR, mTOR, p‐Akt, Akt, p‐PI3K, and PI3K levels in TGF β‐stimulated TIF with transfection of empty vector or pGV362‐GDF15. (F, G) Effects of GDF15 silencing and PI3K inhibition on the PI3K signalling pathway and the expression of fibrosis‐ and autophagy‐related proteins. HK‐2 cells were transfected with shGDF15 (sh865) or control vector (shNC) for 48 h, followed by treatment with the PI3K inhibitor LY294002 (final concentration 20 μM) for 24 h. Western blot and quantification was performed to detect the expression levels of p‐PI3K, PI3K, fibronectin, collagen I, TFEB, and the internal control β‐actin. All data were normalised to β‐actin ( n = 3). * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001.

Techniques: Western Blot, Expressing, Quantitative RT-PCR, Over Expression, Transfection, Plasmid Preparation, Inhibition, Control, Concentration Assay

Journal: Journal of Cellular and Molecular Medicine

Article Title: Novel Roles of GDF15 in Alleviating Renal Fibrosis: Promoting Autophagy and Lysosome Biogenesis via Inhibition of the PI3K /Akt/ mTOR Pathway

doi: 10.1111/jcmm.70951

Figure Lengend Snippet: GDF15 mediates autophagy activation and anti‐fibrotic effects through GFRAL. (A) Western blot analysis and quantification of GFRAL protein expression in HK2 cells following siRNA‐mediated knockdown. siNC served as the negative control, and siGFRAL#1, #2, and #3 represent different interference sequences. (B) Western blot analysis and quantification of fibronectin, collagen I, and GDF15 protein expression in various treatment groups (Vector, GDF15, GDF15 + siNC, GDF15 + siGFRAL) under TGF‐β stimulation. β‐actin was used as the loading control. (C) Western blot analysis and quantification of LC3B, P62, and Beclin1 protein levels in each group. (D) Western blot analysis and quantification of TFEB protein expression in each group. (E) Transmission electron microscopy was used to observe the structural changes of lysosomes in HK2 cells from each group. The scale bars in the upper‐row images represent 1 μm, and those in the lower‐row images represent 500 nm. (F) qRT‐PCR analysis of Lamp1 and Lamp2 in different groups as indicated. (G) Western blot analysis and quantification of PI3K/AKT/mTOR signalling pathway proteins, including p‐mTOR, mTOR, p‐AKT, AKT, p‐PI3K, and PI3K. β‐actin was used as the loading control ( n = 3).* p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001.

Techniques: Activation Assay, Western Blot, Expressing, Knockdown, Negative Control, Plasmid Preparation, Control, Transmission Assay, Electron Microscopy, Quantitative RT-PCR

Multifaceted validation of GDF15 changes in serum from SICM patients and their clinical associations. (A) GDF15 levels were quantified using the Luminex platform. (B) A volcano plot illustrated the gene expression distribution of GDF15 among differentially expressed genes (DEGs) in whole blood. (C) A heatmap displayed the expression profiles of GDF15 and inflammatory cytokines. (D) Serum GDF15 levels in patients. (E) Pearson correlation analysis demonstrated the association between GDF15 and SOFA score, as well as EF. (F) ROC curves were plotted to assess the diagnostic accuracy of GDF15 and SOFA score in identifying SICM. (G) Multivariate logistic regression analysis was performed to identify independent risk factors for the development of SICM in septic patients. ∗p < 0.05 indicates significant differences; ns: no significant differences.

Journal: Redox Biology

Article Title: GDF15 nanotherapy ameliorates NLRP3-associated redox imbalance and cardiac injury in sepsis

doi: 10.1016/j.redox.2025.103897

Figure Lengend Snippet: Multifaceted validation of GDF15 changes in serum from SICM patients and their clinical associations. (A) GDF15 levels were quantified using the Luminex platform. (B) A volcano plot illustrated the gene expression distribution of GDF15 among differentially expressed genes (DEGs) in whole blood. (C) A heatmap displayed the expression profiles of GDF15 and inflammatory cytokines. (D) Serum GDF15 levels in patients. (E) Pearson correlation analysis demonstrated the association between GDF15 and SOFA score, as well as EF. (F) ROC curves were plotted to assess the diagnostic accuracy of GDF15 and SOFA score in identifying SICM. (G) Multivariate logistic regression analysis was performed to identify independent risk factors for the development of SICM in septic patients. ∗p < 0.05 indicates significant differences; ns: no significant differences.

Article Snippet: Enzyme-linked immunosorbent assays (ELISA) were conducted using commercial kits to quantify serum levels of human GDF15 (Proteintech, Cat# KE00108), mouse GDF15 (Proteintech, Cat# KE10082), and mouse IL-6 (MULTI SCIENCES, Cat# EK206).

Techniques: Biomarker Discovery, Luminex, Gene Expression, Expressing, Diagnostic Assay

Upregulation of GDF15 in the SICM model. (A) A schematic workflow for the establishment of the SICM model in C57BL/6J mice via intraperitoneal injection of LPS or saline. (B) Cardiac contractile function parameters, including EF and FS. (C) Serum levels of GDF15 and IL-6. (D) Histopathological analysis of heart tissue, H&E staining (left) and immunohistochemical staining for Ly6G and CD68 (right). Black arrows indicate inflammatory cell infiltration; scale bar: 50 μm. (E) Western blot analysis of GDF15 protein expression in heart tissue. n = 4. (F) qPCR analysis of Gdf15 , Bnp , Il-1β , Il-6 , Icam-1 and Vcam- 1 mRNA levels in heart tissue. (G) Identification of GDF15-positive cells in single-cell RNA-sequencing dataset ( GSE190856 ). (H) qPCR analysis of Gdf15 and Il-1β , Il-6, Nos2, Ptgs2 mRNA expression in BMDM after LPS stimulation. ∗p < 0.05 indicates significant differences; n = 6 per group.

Journal: Redox Biology

Article Title: GDF15 nanotherapy ameliorates NLRP3-associated redox imbalance and cardiac injury in sepsis

doi: 10.1016/j.redox.2025.103897

Figure Lengend Snippet: Upregulation of GDF15 in the SICM model. (A) A schematic workflow for the establishment of the SICM model in C57BL/6J mice via intraperitoneal injection of LPS or saline. (B) Cardiac contractile function parameters, including EF and FS. (C) Serum levels of GDF15 and IL-6. (D) Histopathological analysis of heart tissue, H&E staining (left) and immunohistochemical staining for Ly6G and CD68 (right). Black arrows indicate inflammatory cell infiltration; scale bar: 50 μm. (E) Western blot analysis of GDF15 protein expression in heart tissue. n = 4. (F) qPCR analysis of Gdf15 , Bnp , Il-1β , Il-6 , Icam-1 and Vcam- 1 mRNA levels in heart tissue. (G) Identification of GDF15-positive cells in single-cell RNA-sequencing dataset ( GSE190856 ). (H) qPCR analysis of Gdf15 and Il-1β , Il-6, Nos2, Ptgs2 mRNA expression in BMDM after LPS stimulation. ∗p < 0.05 indicates significant differences; n = 6 per group.

Techniques: Injection, Saline, Staining, Immunohistochemical staining, Western Blot, Expressing, RNA Sequencing

GDF15 deficiency exacerbates LPS-induced SICM in mice. (A) Schematic workflow for the establishment of the SICM model in Gdf15 −/− mice. Gdf15 −/− mice were intraperitoneally injected with LPS or saline to induce SICM, with tissue samples collected 24 h post-injection for further analysis. (B) Echocardiographic assessment of EF and FS. (C) H&E staining of heart tissue, black arrows indicate inflammatory cell infiltration. scale bar: 50 μm. (D) CD68 immunofluorescence staining of heart tissue. Blue staining highlights nuclei, red staining identifies CD68 + macrophages; scale bar: 20 μm. (E) qPCR analysis of mRNA expression levels of Bnp , Il-1β, Il-6, and Mcp-1 in heart tissue. n = 6 per group.

Journal: Redox Biology

Article Title: GDF15 nanotherapy ameliorates NLRP3-associated redox imbalance and cardiac injury in sepsis

doi: 10.1016/j.redox.2025.103897

Figure Lengend Snippet: GDF15 deficiency exacerbates LPS-induced SICM in mice. (A) Schematic workflow for the establishment of the SICM model in Gdf15 −/− mice. Gdf15 −/− mice were intraperitoneally injected with LPS or saline to induce SICM, with tissue samples collected 24 h post-injection for further analysis. (B) Echocardiographic assessment of EF and FS. (C) H&E staining of heart tissue, black arrows indicate inflammatory cell infiltration. scale bar: 50 μm. (D) CD68 immunofluorescence staining of heart tissue. Blue staining highlights nuclei, red staining identifies CD68 + macrophages; scale bar: 20 μm. (E) qPCR analysis of mRNA expression levels of Bnp , Il-1β, Il-6, and Mcp-1 in heart tissue. n = 6 per group.

Techniques: Injection, Saline, Staining, Immunofluorescence, Expressing

MGP exerts anti-inflammatory effects via the MYPT1/AKT/YBX-1 signaling pathway. (A) IP-MS of BMDM to identify the interaction with GDF15. MYPT1 is marked in red. (B) Z-DOCK predicted the interaction domain between GDF15 and MYPT1. Pink represents GDF15, green represents MYPT1, and the boxed region indicates the binding domain. (C) Co-IP combined with Western blot analysis of GDF-15 and MYPT1 binding in macrophages after LPS treatment. (n = 3). (D) Immunofluorescence detection of co-localization between GDF15 (green) and MYPT1 (red), with blue staining for nuclei. Scale bar: 20 μm. (E) Protein expression levels of p -YBX-1, YBX-1, and p -AKT, AKT in BMDM after LPS and/or MGP treatment, with gray-scale intensity analysis of relative expression differences. (F) Representative immunofluorescence images of YBX-1 staining in BMDM after LPS and/or MGP treatment. Blue staining highlights nuclei, and red staining identifies YBX-1. Scale bar: 20 μm ∗p < 0.05, significantly different from control group. #p < 0.05, significantly different from LPS group. n = 6 per group.

Journal: Redox Biology

Article Title: GDF15 nanotherapy ameliorates NLRP3-associated redox imbalance and cardiac injury in sepsis

doi: 10.1016/j.redox.2025.103897

Figure Lengend Snippet: MGP exerts anti-inflammatory effects via the MYPT1/AKT/YBX-1 signaling pathway. (A) IP-MS of BMDM to identify the interaction with GDF15. MYPT1 is marked in red. (B) Z-DOCK predicted the interaction domain between GDF15 and MYPT1. Pink represents GDF15, green represents MYPT1, and the boxed region indicates the binding domain. (C) Co-IP combined with Western blot analysis of GDF-15 and MYPT1 binding in macrophages after LPS treatment. (n = 3). (D) Immunofluorescence detection of co-localization between GDF15 (green) and MYPT1 (red), with blue staining for nuclei. Scale bar: 20 μm. (E) Protein expression levels of p -YBX-1, YBX-1, and p -AKT, AKT in BMDM after LPS and/or MGP treatment, with gray-scale intensity analysis of relative expression differences. (F) Representative immunofluorescence images of YBX-1 staining in BMDM after LPS and/or MGP treatment. Blue staining highlights nuclei, and red staining identifies YBX-1. Scale bar: 20 μm ∗p < 0.05, significantly different from control group. #p < 0.05, significantly different from LPS group. n = 6 per group.

Techniques: Protein-Protein interactions, Binding Assay, Co-Immunoprecipitation Assay, Western Blot, Immunofluorescence, Staining, Expressing, Control

YBX-1 mediates GDF15-mediated transcriptional regulation of the NLRP3 pathway. (A) qPCR analysis of mRNA expression levels of Nlrp3, Asc , and Il-1β in LPS-stimulated BMDM after Si- Ybx-1 . (B) Western blot analysis of protein expression levels of NLRP3 and IL-1β in LPS-stimulated BMDM after YBX-1 knockdown. (C) qPCR analysis of mRNA expression levels of Nlrp3 and Il-1β in LPS and MGP-treated BMDM after YBX-1 knockdown. (D) Schematic diagram of the luciferase reporter plasmid for the Nlrp3 promoter. (E) Luciferase activity of pcDNA3.1-YBX-1 or empty vector-transfected cells. (F) Luciferase activity after LPS and MGP treatment. n = 6 per group.

Journal: Redox Biology

Article Title: GDF15 nanotherapy ameliorates NLRP3-associated redox imbalance and cardiac injury in sepsis

doi: 10.1016/j.redox.2025.103897

Figure Lengend Snippet: YBX-1 mediates GDF15-mediated transcriptional regulation of the NLRP3 pathway. (A) qPCR analysis of mRNA expression levels of Nlrp3, Asc , and Il-1β in LPS-stimulated BMDM after Si- Ybx-1 . (B) Western blot analysis of protein expression levels of NLRP3 and IL-1β in LPS-stimulated BMDM after YBX-1 knockdown. (C) qPCR analysis of mRNA expression levels of Nlrp3 and Il-1β in LPS and MGP-treated BMDM after YBX-1 knockdown. (D) Schematic diagram of the luciferase reporter plasmid for the Nlrp3 promoter. (E) Luciferase activity of pcDNA3.1-YBX-1 or empty vector-transfected cells. (F) Luciferase activity after LPS and MGP treatment. n = 6 per group.

Techniques: Expressing, Western Blot, Knockdown, Luciferase, Plasmid Preparation, Activity Assay, Transfection

Mechanism of action of macrophage-biomimetic nanocarriers delivering GDF15 to target the YBX-1-NLRP3 axis in SICM. Macrophage-biomimetic nanocarriers loaded with rhGDF15 are targeted to inflammatory sites in the heart, enhancing local drug accumulation, while GDF15 binds to MYPT1 to inhibit YBX-1 phosphorylation and block its nuclear translocation, leading to reduced nuclear YBX-1 expression and decreased transcriptional activity of the Nlrp3 promoter, which suppresses NLRP3 inflammasome assembly and pro-inflammatory cytokine release such as IL-1β, ultimately alleviating macrophage inflammatory responses, myocardial cell injury, and improving cardiac function in SICM.

Journal: Redox Biology

Article Title: GDF15 nanotherapy ameliorates NLRP3-associated redox imbalance and cardiac injury in sepsis

doi: 10.1016/j.redox.2025.103897

Figure Lengend Snippet: Mechanism of action of macrophage-biomimetic nanocarriers delivering GDF15 to target the YBX-1-NLRP3 axis in SICM. Macrophage-biomimetic nanocarriers loaded with rhGDF15 are targeted to inflammatory sites in the heart, enhancing local drug accumulation, while GDF15 binds to MYPT1 to inhibit YBX-1 phosphorylation and block its nuclear translocation, leading to reduced nuclear YBX-1 expression and decreased transcriptional activity of the Nlrp3 promoter, which suppresses NLRP3 inflammasome assembly and pro-inflammatory cytokine release such as IL-1β, ultimately alleviating macrophage inflammatory responses, myocardial cell injury, and improving cardiac function in SICM.

Techniques: Phospho-proteomics, Blocking Assay, Translocation Assay, Expressing, Activity Assay

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