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Under hypoxia, most SRGN is secreted extracellularly via the secretory autophagy pathway in CAFs. (A) Prediction of SRGN signal peptide structure using SignalP 6.0. (B) WB analysis of SRGN expression in normoxic and hypoxic CAFs with or without BFA (.2 µM, 24 h). (C) Detection of SRGN secretion levels in the supernatant of normoxic and hypoxic CAFs with or without BFA by ELISA. (D) IF showing co‐localization of SRGN and GM130 in normoxic and hypoxic CAFs with or without BFA. Scale bar = 10 µm. (E) IF observation <t>of</t> <t>LAMP1</t> protein expression in normoxic and hypoxic CAFs and changes in LysoSensor intensity. Scale bar = 50 µm. (F, G) WB analysis of LAMP1 and <t>CTSD</t> protein expression levels in normoxic and hypoxic CAFs, along with quantitative analysis. (H) IF showing co‐localization of SRGN and LC3B in normoxic and hypoxic CAFs with or without 3‐MA. Scale bar = 10 µm. (I, J) WB analysis of LAMP1, P62, CTSD, SRGN, and LC3B protein expression levels in normoxic and hypoxic CAFs treated with BFA, CQ (60 µM), and Baf A1 (20 nM) for 24 h, along with quantitative analysis of SRGN expression. (K) Detection of SRGN secretion levels in the supernatant of normoxic and hypoxic CAFs treated with CQ and Baf A1 by ELISA. ns, not significant; * p < .05; ** p < .01; *** p < .001.
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Under hypoxia, most SRGN is secreted extracellularly via the secretory autophagy pathway in CAFs. (A) Prediction of SRGN signal peptide structure using SignalP 6.0. (B) WB analysis of SRGN expression in normoxic and hypoxic CAFs with or without BFA (.2 µM, 24 h). (C) Detection of SRGN secretion levels in the supernatant of normoxic and hypoxic CAFs with or without BFA by ELISA. (D) IF showing co‐localization of SRGN and GM130 in normoxic and hypoxic CAFs with or without BFA. Scale bar = 10 µm. (E) IF observation <t>of</t> <t>LAMP1</t> protein expression in normoxic and hypoxic CAFs and changes in LysoSensor intensity. Scale bar = 50 µm. (F, G) WB analysis of LAMP1 and <t>CTSD</t> protein expression levels in normoxic and hypoxic CAFs, along with quantitative analysis. (H) IF showing co‐localization of SRGN and LC3B in normoxic and hypoxic CAFs with or without 3‐MA. Scale bar = 10 µm. (I, J) WB analysis of LAMP1, P62, CTSD, SRGN, and LC3B protein expression levels in normoxic and hypoxic CAFs treated with BFA, CQ (60 µM), and Baf A1 (20 nM) for 24 h, along with quantitative analysis of SRGN expression. (K) Detection of SRGN secretion levels in the supernatant of normoxic and hypoxic CAFs treated with CQ and Baf A1 by ELISA. ns, not significant; * p < .05; ** p < .01; *** p < .001.
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Under hypoxia, most SRGN is secreted extracellularly via the secretory autophagy pathway in CAFs. (A) Prediction of SRGN signal peptide structure using SignalP 6.0. (B) WB analysis of SRGN expression in normoxic and hypoxic CAFs with or without BFA (.2 µM, 24 h). (C) Detection of SRGN secretion levels in the supernatant of normoxic and hypoxic CAFs with or without BFA by ELISA. (D) IF showing co‐localization of SRGN and GM130 in normoxic and hypoxic CAFs with or without BFA. Scale bar = 10 µm. (E) IF observation <t>of</t> <t>LAMP1</t> protein expression in normoxic and hypoxic CAFs and changes in LysoSensor intensity. Scale bar = 50 µm. (F, G) WB analysis of LAMP1 and <t>CTSD</t> protein expression levels in normoxic and hypoxic CAFs, along with quantitative analysis. (H) IF showing co‐localization of SRGN and LC3B in normoxic and hypoxic CAFs with or without 3‐MA. Scale bar = 10 µm. (I, J) WB analysis of LAMP1, P62, CTSD, SRGN, and LC3B protein expression levels in normoxic and hypoxic CAFs treated with BFA, CQ (60 µM), and Baf A1 (20 nM) for 24 h, along with quantitative analysis of SRGN expression. (K) Detection of SRGN secretion levels in the supernatant of normoxic and hypoxic CAFs treated with CQ and Baf A1 by ELISA. ns, not significant; * p < .05; ** p < .01; *** p < .001.
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Under hypoxia, most SRGN is secreted extracellularly via the secretory autophagy pathway in CAFs. (A) Prediction of SRGN signal peptide structure using SignalP 6.0. (B) WB analysis of SRGN expression in normoxic and hypoxic CAFs with or without BFA (.2 µM, 24 h). (C) Detection of SRGN secretion levels in the supernatant of normoxic and hypoxic CAFs with or without BFA by ELISA. (D) IF showing co‐localization of SRGN and GM130 in normoxic and hypoxic CAFs with or without BFA. Scale bar = 10 µm. (E) IF observation of LAMP1 protein expression in normoxic and hypoxic CAFs and changes in LysoSensor intensity. Scale bar = 50 µm. (F, G) WB analysis of LAMP1 and CTSD protein expression levels in normoxic and hypoxic CAFs, along with quantitative analysis. (H) IF showing co‐localization of SRGN and LC3B in normoxic and hypoxic CAFs with or without 3‐MA. Scale bar = 10 µm. (I, J) WB analysis of LAMP1, P62, CTSD, SRGN, and LC3B protein expression levels in normoxic and hypoxic CAFs treated with BFA, CQ (60 µM), and Baf A1 (20 nM) for 24 h, along with quantitative analysis of SRGN expression. (K) Detection of SRGN secretion levels in the supernatant of normoxic and hypoxic CAFs treated with CQ and Baf A1 by ELISA. ns, not significant; * p < .05; ** p < .01; *** p < .001.

Journal: Clinical and Translational Medicine

Article Title: Hypoxia‐induced secretory autophagy in cancer‐associated fibroblasts promotes ECM remodelling through serglycin secretion in oral squamous cell carcinoma

doi: 10.1002/ctm2.70556

Figure Lengend Snippet: Under hypoxia, most SRGN is secreted extracellularly via the secretory autophagy pathway in CAFs. (A) Prediction of SRGN signal peptide structure using SignalP 6.0. (B) WB analysis of SRGN expression in normoxic and hypoxic CAFs with or without BFA (.2 µM, 24 h). (C) Detection of SRGN secretion levels in the supernatant of normoxic and hypoxic CAFs with or without BFA by ELISA. (D) IF showing co‐localization of SRGN and GM130 in normoxic and hypoxic CAFs with or without BFA. Scale bar = 10 µm. (E) IF observation of LAMP1 protein expression in normoxic and hypoxic CAFs and changes in LysoSensor intensity. Scale bar = 50 µm. (F, G) WB analysis of LAMP1 and CTSD protein expression levels in normoxic and hypoxic CAFs, along with quantitative analysis. (H) IF showing co‐localization of SRGN and LC3B in normoxic and hypoxic CAFs with or without 3‐MA. Scale bar = 10 µm. (I, J) WB analysis of LAMP1, P62, CTSD, SRGN, and LC3B protein expression levels in normoxic and hypoxic CAFs treated with BFA, CQ (60 µM), and Baf A1 (20 nM) for 24 h, along with quantitative analysis of SRGN expression. (K) Detection of SRGN secretion levels in the supernatant of normoxic and hypoxic CAFs treated with CQ and Baf A1 by ELISA. ns, not significant; * p < .05; ** p < .01; *** p < .001.

Article Snippet: The primary antibodies used are listed as follows: SRGN (1:1000, A25426, ABclonal), ATG5 (1:1000, 10181‐2‐AP, Proteintech), LC3B (1:2000, ab192890, Abcam, USA), Beclin 1 (1:1000, 11306‐1‐AP, Proteintech), β‐actin (1:4000, 20536‐1‐AP, Proteintech), LAMP1 (1:4000, 21997‐1‐AP, Proteintech), P62 (1:4000, 18420‐1‐AP, Proteintech), CTSD (1:4000, 21327‐1‐AP, Proteintech), MMP9 (1:1000, bs‐4593R, Bioss, China), MMP2 (1:1000, CY5189, Abways, China), and MMP11 (1:1000, CY5778, Abways).

Techniques: Expressing, Enzyme-linked Immunosorbent Assay