Journal: Cellular and Molecular Life Sciences: CMLS

Article Title: Cartilage intermediate layer protein inhibits ligamentum flavum hypertrophy mediated by TGF-β1/SMAD3/SERPINE2 signaling pathway

doi: 10.1007/s00018-025-06051-7

Figure Lengend Snippet: CILP attenuates LF fibrosis via the TGF-β1/SMAD3/SERPINE2 axis. ( A ) A violin plot depicted differential SERPINE2 expression between Non-LFH and LFH groups (n = 6 per group), showing significant differences. ( B ) IHC of SERPINE2 in LF samples from Non-LFH and LFH groups (n = 6 per group). Scale bar: 50 µm. ( C , D ) Western blotting revealed elevated SERPINE2 protein levels between Non-LFH and LFH groups (n = 6 per group), with relative protein expression quantified. And mRNA concentration showed consistent results. ( E , F ) Western blotting demonstrated SERPINE2 expression in LF cells treated with TGF-β1 at 0, 8, 16, and 24 h time points, with relative protein expression quantified. And mRNA concentration showed consistent results. ( G ) Western blotting assessed protein expression levels of CILP, Collagen I, p-SMAD3, and α-SMA in LF cells subjected to various SERPINE2 treatments. ( H ) qRT-PCR assessed transcriptional profiles of CILP, ACTA2 (α-SMA), and COL1A2 across experimental conditions in LF cells. ( I ) WB analysis evaluated p-SMAD3 and fibrotic protein levels 48 hours post-transfection with CILP-overexpressing plasmids under different conditions in LF cells. ( J ) WB analysis examined p-SMAD3 and fibrotic protein expression 48 hours post-transfection with CILP-silencing plasmids under various regimens. Significance levels are denoted as follows: ns, not significant;* P < 0.05;** P < 0.01;*** P < 0.01

Article Snippet: In further experiments, cells were exposed to varying concentrations of CILP protein (10, 25, 50 ng/ml, RPC382Hu01, Cloud-Clone, TX, USA) and/or SERPINE2 protein (25 μg/ml, HY- P71085 , MCE) for 24 h. The plasmids and siRNA were obtained from Hanbio Biotechnology Co., Ltd, located in Shanghai, China.

Techniques: Expressing, Western Blot, Concentration Assay, Quantitative RT-PCR, Transfection

Journal: Cellular and Molecular Life Sciences: CMLS

Article Title: Cartilage intermediate layer protein inhibits ligamentum flavum hypertrophy mediated by TGF-β1/SMAD3/SERPINE2 signaling pathway

doi: 10.1007/s00018-025-06051-7

Figure Lengend Snippet: CILP attenuates TGF-β1-mediated LFH in vivo. ( A - D ) IHC analysis of SERPINE2, TGF-β1, Collagen I, and p-SMAD3 in mouse tissues, with quantification of positive cell percentages. Scale bar: 50 µm. Significance levels are denoted as follows: ns, not significant;* P < 0.05; ** P < 0.01; *** P < 0.001

Article Snippet: In further experiments, cells were exposed to varying concentrations of CILP protein (10, 25, 50 ng/ml, RPC382Hu01, Cloud-Clone, TX, USA) and/or SERPINE2 protein (25 μg/ml, HY- P71085 , MCE) for 24 h. The plasmids and siRNA were obtained from Hanbio Biotechnology Co., Ltd, located in Shanghai, China.

Techniques: In Vivo

Journal: Reproductive Biology and Endocrinology : RB&E

Article Title: SERPINE2, an inhibitor of plasminogen activators, is highly expressed in the human endometrium during the secretory phase

doi: 10.1186/1477-7827-9-38

Figure Lengend Snippet: Antibody specificity and presence of the SERPINE2 protein in human uterine fluid . (A) Four hundred nanograms of recombinant human SERPINE2 was resolved on 10% SDS-PAGE and followed by Western blotting using anti-mouse SERPINE2 antiserum (lane 1), an anti-human SERPINE2 antibody (R&D) (lane2), or another anti-human SERPINE2 antibody (Abnova) (lane 3). (B) One hundred micrograms of the extract of endometrial curettage was analyzed by anti-mouse SERPINE2 antiserum (lanes 1 and 2) and an anti-human SERPINE2 antibody (R&D) (lanes 3 and 4). (C) Fifty micrograms of uterine fluid proteins collected from each individual patient ( n = 7) was Western-blotted using anti-mouse SERPINE2 antiserum (1:3000) (upper panel). EP, MP, and LP indicate early-, mid-, and late-proliferative phases, and ES and MS indicate early- and mid-secretory phases, respectively. The blot was also overexposed to clearly display the staining signal (lower panel).

Article Snippet: Membranes were blocked with 10% (w/v) skim milk in phosphate-buffered saline (PBS) (blocking solution) for 2 h, and then incubated with our homemade anti-mouse SERPINE2 antiserum (1: 5000) [ , ], anti-human SERPINE2 antibody (1: 1000, catalog no. AF2980, R&D Systems, Minneapolis, MN, USA), or another anti-human SERPINE2 antibody (1: 1000, product no. H00005270-B01, Abnova) in blocking solution for 2 h at 37°C.

Techniques: Recombinant, SDS Page, Western Blot, Staining

Journal: Reproductive Biology and Endocrinology : RB&E

Article Title: SERPINE2, an inhibitor of plasminogen activators, is highly expressed in the human endometrium during the secretory phase

doi: 10.1186/1477-7827-9-38

Figure Lengend Snippet: Localization of SERPINE2 in the human uterus . Longitudinal sections of the early secretory phase uterus (n = 5) on the slide were incubated with anti-mouse SERPINE2 antiserum and then treated with biotin-conjugated goat-anti-rabbit IgG and HRP-conjugated streptavidin (brown). For contrast, specimens were further stained with hematoxylin (blue). The representative picture is shown. Magnified pictures of the luminal epithelium (A), glandular epithelium (B), and myometrium (C) are shown. Bar = 50 μm. bv, blood vessel; ge, glandular epithelium; le, luminal epithelium; m, muscle; s, stroma.

Article Snippet: Membranes were blocked with 10% (w/v) skim milk in phosphate-buffered saline (PBS) (blocking solution) for 2 h, and then incubated with our homemade anti-mouse SERPINE2 antiserum (1: 5000) [ , ], anti-human SERPINE2 antibody (1: 1000, catalog no. AF2980, R&D Systems, Minneapolis, MN, USA), or another anti-human SERPINE2 antibody (1: 1000, product no. H00005270-B01, Abnova) in blocking solution for 2 h at 37°C.

Techniques: Incubation, Staining

Journal: Reproductive Biology and Endocrinology : RB&E

Article Title: SERPINE2, an inhibitor of plasminogen activators, is highly expressed in the human endometrium during the secretory phase

doi: 10.1186/1477-7827-9-38

Figure Lengend Snippet: Glandular epithelial expression of the SERPINE2 protein in the endometrium during the menstrual cycle . Sections prepared from endometrial curettage during early-proliferative (EP), mid-proliferative (MP), late-proliferative (LP), early-secretory (ES), mid-secretory (MS), and late-secretory (LS) phases were incubated with anti-mouse SERPINE2 antiserum and then treated as described in Figure 2. Bar = 50 μm. bv, blood vessel; ge, glandular epithelium; s, stroma.

Article Snippet: Membranes were blocked with 10% (w/v) skim milk in phosphate-buffered saline (PBS) (blocking solution) for 2 h, and then incubated with our homemade anti-mouse SERPINE2 antiserum (1: 5000) [ , ], anti-human SERPINE2 antibody (1: 1000, catalog no. AF2980, R&D Systems, Minneapolis, MN, USA), or another anti-human SERPINE2 antibody (1: 1000, product no. H00005270-B01, Abnova) in blocking solution for 2 h at 37°C.

Techniques: Expressing, Incubation

Journal: Reproductive Biology and Endocrinology : RB&E

Article Title: SERPINE2, an inhibitor of plasminogen activators, is highly expressed in the human endometrium during the secretory phase

doi: 10.1186/1477-7827-9-38

Figure Lengend Snippet: Quantification of SERPINE2 protein expression levels in endometrial glands . Representative samples were analyzed by automated cell acquisition and quantification software (A). The expression signal of a respective glandular gland was quantified using HistoQuest software and is presented as a scattergram. Each spot on the scattergram stands for the intensity of one cell (B). The relative SERPINE2 protein expression levels in patients' glandular glands at various sub-phases of the menstrual cycle are shown as bar diagrams (C). Differences are significant among patients at various groups (χ = 69.32, p < 0.0001).

Article Snippet: Membranes were blocked with 10% (w/v) skim milk in phosphate-buffered saline (PBS) (blocking solution) for 2 h, and then incubated with our homemade anti-mouse SERPINE2 antiserum (1: 5000) [ , ], anti-human SERPINE2 antibody (1: 1000, catalog no. AF2980, R&D Systems, Minneapolis, MN, USA), or another anti-human SERPINE2 antibody (1: 1000, product no. H00005270-B01, Abnova) in blocking solution for 2 h at 37°C.

Techniques: Expressing, Software

Journal: Oncotarget

Article Title: Serpin E2 promotes breast cancer metastasis by remodeling the tumor matrix and polarizing tumor associated macrophages

doi: 10.18632/oncotarget.12927

Figure Lengend Snippet: ( A ) Masson trichrome staining performed on 4T1 Ctrl and shSerpine2 tumors. Representative images show increased collagen encapsulation (blue) of SerpinE2 KD tumors. Scale bar100μm. ( B - C ) Intravital imaging using (IVI-MP) of 4T1 Ctrl and shSerpine2 tumors. (B) Representative images show collagen I fibers detected by the SHG signal (cyan) at the surface of 4T1 tumors; scale bar25μm. (C) Average SHG signal intensity was determined per 100μm z-stack; data are acquired from 19-30 separate z-stacks from 3 mice per cell line. * P < 0.00036. D. IVI-MP performed on mice bearing GFP-labeled 4T1 control and shSerpinE2 tumors. Representative images show GFP-labeled tumor cells (green), phagocytic dextran positive cells (red); SHG imaging identified collagen I fibers (cyan). Scale bars25μm. (E-F) ( E ) GFP-labeled 4T1 tumor-bearing mice were treated with control liposomes or clodronate-containing liposomes until IVI-MP was performed. Representative images are shown as in (D). ( F ) Quantification of SHG (cyan) signal intensity in 100 μm Z-stacks of tumors in treated animals. Data are mean ± SEM of measurements from 40-61 Z-stacks from at least 3 different tumors for each treatment group. * P < 0.016. All data are mean ± SEM.

Article Snippet: Anti-human SerpinE2 Ab (MAB2980) was from R&D systems.

Techniques: Staining, Encapsulation, Imaging, Labeling, Control, Liposomes

Journal: Oncotarget

Article Title: Serpin E2 promotes breast cancer metastasis by remodeling the tumor matrix and polarizing tumor associated macrophages

doi: 10.18632/oncotarget.12927

Figure Lengend Snippet: Conditioned medium (CM) from 4T1 and 168FARN ( A ) or MDA-MB435 ( B ) cultures was incubated overnight with Ab11, then bound serpinE2 was pulled-down with Protein G, and analyzed by western blot with the rodent-specific antibody, 4B3 (A), or a human-specific antibody (B). (A) The right panel shows a short exposure of serpinE2 complexes from 4T1 CM, but none in 168FARN CM (long exposure on the left), as well as an IP of the preformed tPA/serpinE2 complex. ( C ) SFM loaded with purified human serpinE2 or the preformed serpinE2/tPA complex was IP'd with Ab11 as in (A) & (B) and analyzed by western blot with a human serpinE2-specific antibody. The serpinE2 complex and uncomplexed serpinE2 are indicated with arrowheads.

Article Snippet: Anti-human SerpinE2 Ab (MAB2980) was from R&D systems.

Techniques: Incubation, Western Blot, Purification

Journal: Oncotarget

Article Title: Serpin E2 promotes breast cancer metastasis by remodeling the tumor matrix and polarizing tumor associated macrophages

doi: 10.18632/oncotarget.12927

Figure Lengend Snippet: The LRP1 receptor is expressed on tumor cells and on macrophages and we propose that serpinE2 targeting with Ab11 impacts on LRP1 signaling in both cell types. ( A ) In metastatic tumors, serpinE2-LRP1 binding stimulates ERK signaling and secretion of CCL2. Tumor cells display hyperactivation of receptor tyrosine kinases (RTKs); FGFRs, which are active in the 4T1 model, also stimulate ERK pathway activation. We speculate that in macrophages, the combination of high CCL2 levels and serpinE2-activated LRP1 promotes the M2 phenotype. Indeed, there are high levels of phagocytic, Texas-red positive M2 tumor associated macrophages (TAMs) in the metastatic tumors; they are known to be responsible for degrading the matrix during tumor development. ( B ) Ab11 or sepinE2 KD (not drawn in model) lowers ERK pathway activity and the secretion of CCL2, and stimulates TIMP1 secretion. Tyrosine kinase inhibitors (TKIs) block RTK signaling. The matrix-degrading M2 TAMs are decreased in Ab11-treated tumors. Moreover, depleting macrophages with clodronate liposomes results in deposition of a dense collagen matrix, similar to that observed in Ab11-treated tumors. Thus, we propose that the drop in CCL2, which contributes to a decrease in M2 TAMs, as well as blocking serpinE2, which skews the TAMs towards the M1 phenotype, causes the emergence of a dense collagen matrix that inhibits intravasation and metastatic dissemination.

Article Snippet: Anti-human SerpinE2 Ab (MAB2980) was from R&D systems.

Techniques: Binding Assay, Activation Assay, Activity Assay, Blocking Assay, Liposomes

Journal: Oncotarget

Article Title: Regulation of tumor growth by circulating full-length chromogranin A

doi: 10.18632/oncotarget.12237

Figure Lengend Snippet: A. Induction of protease nexin-1 mRNA in endothelial cells . HUVECs were treated with various doses of recombinant CgA for 20 h. The presence of PN-1 transcripts in cells was analyzed by real time PCR. PN-1 mRNA expression is reported as fold change compared to untreated cells. The cumulative results of 3 experiments are shown: in each experiment each sample was analyzed 5-6 times by real-time PCR (each in triplicate). Box-plots with median, interquartiles and 5-95 percentile values are shown (dotted line, mean value of controls). ***, P < 0.001, by t test (2-tailed). B. Effect of PN1 gene silencing on the activity of CgA in the endothelial spheroid sprouting assay . HUVEC cells spheroids were transfected with PN-1 siRNA mixture (siPN1) or with control siRNA (siCtrl) as described in Methods. After transfection, spheroids were treated with or without and 0.2 nM recombinant CgA 1-439 for 16 hours. The number of sprouts was from each spheroid was then counted. Cumulative results of two independent experiments (8-16 spheroids/experiment). The number of spheroids used is indicated in each panel ( n ). *, P < 0.05; **, P < 0.01 by t test. C. - D. Effect of anti-PN-1 antibodies on the activity of CgA in the endothelial spheroid sprouting assay . Cumulative results of two independent experiments (8 spheroids/experiment, total n = 16). Spheroids were incubated with or without recombinant CgA (0.2 nM) in the absence or the presence of anti-PN-1 polyclonal immunoglobulins (goat IgGs anti-human Serpin E2/PN1), or control immunoglobulins (normal goat IgGs) as indicated. Bars: mean ± SE. ****, P < 0.0001, ***, P < 0.001, by t test (2-tailed). Representative microphotographs of spheroids are shown in ( C ) (arrows: endothelial cell sprouts). E. Effect of anti-PN-1 antibodies on the anti-tumor activity of CgA . WEHI-164- or TS/A-tumor-bearing mice were treated with recombinant CgA (i.p.) in combination with anti-PN-1, or with control immunoglobulins (normal goat IgGs) at the indicated doses. Antibodies were given 2.5 h before CgA. Arrows indicate the day of treatment. Tumor volume (mean ± SE). The area under the curve for each mouse was calculated using the GraphPad Prism Software. Statistical analysis was performed by Mann-Whitney test on the calculated areas (6 animals per group; **, P < 0.01; *, P < 0.05).

Article Snippet: Goat IgGs anti-mouse serpin E2/PN1, goat IgGs anti-human serpin E2/PN1 and normal goat immunoglobulins were from R&D System.

Techniques: Recombinant, Real-time Polymerase Chain Reaction, Expressing, Activity Assay, Transfection, Incubation, Software, MANN-WHITNEY

Journal: Frontiers in Oncology

Article Title: SerpinE2 promotes M2 polarization in macrophage to accelerate colorectal cancer progression

doi: 10.3389/fonc.2025.1585935

Figure Lengend Snippet: SERPINE2 expression is significantly upregulated in COAD. (A) Box plot of SERPINE family genes mRNA expression.in COAD(p < 0.05). (B) Box plot of SERPINE1 and SERPINE2 protein expression in COAD(p < 0.05). (C) Box plot of SERPINE2 mRNA expression among groups of different tumor grades in COAD (p < 0.05).

Article Snippet: Specific primary antibodies against SERPINE2 (Proteintech) was used.

Techniques: Expressing

Journal: Frontiers in Oncology

Article Title: SerpinE2 promotes M2 polarization in macrophage to accelerate colorectal cancer progression

doi: 10.3389/fonc.2025.1585935

Figure Lengend Snippet: SERPINE2 expression correlates with tumor immunoregulation, division and proliferation. (A) Volcano map of SERPINE2 co-expressed genes in COAD. (B, C) GO and KEGG enrichment analysis of SERPINE2 co-expressed genes obtained from the cBioPortal, the terms p and q < 0.05 were considered to be significantly enriched. Only 20 leading gene sets are displayed in the plot.

Article Snippet: Specific primary antibodies against SERPINE2 (Proteintech) was used.

Techniques: Expressing

Journal: Frontiers in Oncology

Article Title: SerpinE2 promotes M2 polarization in macrophage to accelerate colorectal cancer progression

doi: 10.3389/fonc.2025.1585935

Figure Lengend Snippet: SERPINE2 is positively correlated with M2 macrophage infiltration in COAD. (A) Scatter plot showing the correlation of 6 different immune cell types and SERPINE2 expression (p < 0.05). The black line in each plot is a fitted linear model indicating the proportion of tropism of the immune cell along with SERPINE2 expression, and the Pearson coefficient was used for the correlation test. (B) Scatter plot showing the correlation of CD68+ Marcophage and SERPINE2 expression (p < 0.05). C.Scatter plot showing the correlation of M1/M2 macrophage and SERPINE2 expression (p < 0.05). The blue line in each plot is a fitted linear model indicating the proportion of tropism of the immune cell along with SERPINE2 expression, and the Pearson coefficient was used for the correlation test. (p < 0.05).

Article Snippet: Specific primary antibodies against SERPINE2 (Proteintech) was used.

Techniques: Expressing

Journal: Frontiers in Oncology

Article Title: SerpinE2 promotes M2 polarization in macrophage to accelerate colorectal cancer progression

doi: 10.3389/fonc.2025.1585935

Figure Lengend Snippet: SERPINE2 is associated with infiltration of CD68 macrophage in COAD patients. (A) The expression of SEPRINE2 in patient tissues was detected by IHC. Adjacent tissue not expressing SERPINE2; tumor tissue strongly expressing SERPINE2. (B) Scatterplot showing the correlation between SERPINE2 and CD68 expression (p < 0.05). The blue line in each plot is a fitted linear model indicating the relationship between SERPINE2 and CD68 expression. (C) The expression of SERPINE2 and CD68 in patient tissues were detected by IHC. High levels of SERPINE2 expression are associated with increased expression of CD68. (* p<0.05, **p<0.01, *** p<0.001).

Article Snippet: Specific primary antibodies against SERPINE2 (Proteintech) was used.

Techniques: Expressing

Journal: Frontiers in Oncology

Article Title: SerpinE2 promotes M2 polarization in macrophage to accelerate colorectal cancer progression

doi: 10.3389/fonc.2025.1585935

Figure Lengend Snippet: The external secretion of SERPINE2 from colorectal cancer cells promotes macrophage polarization to accelerate the development of colorectal cancer. (A) Schema diagram showing that THP-1 cells were treated with PMA, followed by the treatment of SERPINE2 recombinant protein as indicated treatments to obtain activated macrophages. Then tumor cells cocultured with these macrophages. were used to subsequent experiments. (B, C) RT-qPCR and Westen blot displayed SERPINE2 mRNA and Protein expression were upregulated in colorectal cancer cells. (D) The secretion of SERPINE2 in colorectal cancer cells was detected by ELISA. (E) The effect of SERPINE2 recombinant protein on macrophage polarization. (F) RT-qPCR displayed conditioned medium (CM) derived from colorectal cancer cells promotes the upregulation of macrophage M2 markers, compared to normal Intestinal cells. (G) ELISA analysis demonstrated that SERPINE2 secretion was significantly reduced after SERPINE2 knockdown. (H) RT-qPCR displayed conditioned medium with SERPINE2 knockdown down-regulated macrophage M2 markers. (I, J) The conditioned medium from macrophages treated with SERPINE2 recombinant protein promoted cancer cell proliferation (measured by CCK-8 assay) and migration (assessed by Transwell assay. (*p<0.05, **p<0.01, ***p<0.001).

Article Snippet: Specific primary antibodies against SERPINE2 (Proteintech) was used.

Techniques: Recombinant, Quantitative RT-PCR, Expressing, Enzyme-linked Immunosorbent Assay, Derivative Assay, Knockdown, CCK-8 Assay, Migration, Transwell Assay

Journal: Frontiers in Oncology

Article Title: SerpinE2 promotes M2 polarization in macrophage to accelerate colorectal cancer progression

doi: 10.3389/fonc.2025.1585935

Figure Lengend Snippet: SERPINE2 expression is significantly upregulated in COAD. (A) Box plot of SERPINE family genes mRNA expression.in COAD(p < 0.05). (B) Box plot of SERPINE1 and SERPINE2 protein expression in COAD(p < 0.05). (C) Box plot of SERPINE2 mRNA expression among groups of different tumor grades in COAD (p < 0.05).

Article Snippet: Besides, in order to explore the effect of SERPINE2 on macrophage polarization, M0 macrophages were treated with recombinant SERPINE2 (0.4 ng/mL, TargetMol) during 24 hours and then harvested for subsequent experiment.

Techniques: Expressing

Journal: Frontiers in Oncology

Article Title: SerpinE2 promotes M2 polarization in macrophage to accelerate colorectal cancer progression

doi: 10.3389/fonc.2025.1585935

Figure Lengend Snippet: SERPINE2 expression correlates with tumor immunoregulation, division and proliferation. (A) Volcano map of SERPINE2 co-expressed genes in COAD. (B, C) GO and KEGG enrichment analysis of SERPINE2 co-expressed genes obtained from the cBioPortal, the terms p and q < 0.05 were considered to be significantly enriched. Only 20 leading gene sets are displayed in the plot.

Article Snippet: Besides, in order to explore the effect of SERPINE2 on macrophage polarization, M0 macrophages were treated with recombinant SERPINE2 (0.4 ng/mL, TargetMol) during 24 hours and then harvested for subsequent experiment.

Techniques: Expressing

Journal: Frontiers in Oncology

Article Title: SerpinE2 promotes M2 polarization in macrophage to accelerate colorectal cancer progression

doi: 10.3389/fonc.2025.1585935

Figure Lengend Snippet: SERPINE2 is positively correlated with M2 macrophage infiltration in COAD. (A) Scatter plot showing the correlation of 6 different immune cell types and SERPINE2 expression (p < 0.05). The black line in each plot is a fitted linear model indicating the proportion of tropism of the immune cell along with SERPINE2 expression, and the Pearson coefficient was used for the correlation test. (B) Scatter plot showing the correlation of CD68+ Marcophage and SERPINE2 expression (p < 0.05). C.Scatter plot showing the correlation of M1/M2 macrophage and SERPINE2 expression (p < 0.05). The blue line in each plot is a fitted linear model indicating the proportion of tropism of the immune cell along with SERPINE2 expression, and the Pearson coefficient was used for the correlation test. (p < 0.05).

Article Snippet: Besides, in order to explore the effect of SERPINE2 on macrophage polarization, M0 macrophages were treated with recombinant SERPINE2 (0.4 ng/mL, TargetMol) during 24 hours and then harvested for subsequent experiment.

Techniques: Expressing

Journal: Frontiers in Oncology

Article Title: SerpinE2 promotes M2 polarization in macrophage to accelerate colorectal cancer progression

doi: 10.3389/fonc.2025.1585935

Figure Lengend Snippet: SERPINE2 is associated with infiltration of CD68 macrophage in COAD patients. (A) The expression of SEPRINE2 in patient tissues was detected by IHC. Adjacent tissue not expressing SERPINE2; tumor tissue strongly expressing SERPINE2. (B) Scatterplot showing the correlation between SERPINE2 and CD68 expression (p < 0.05). The blue line in each plot is a fitted linear model indicating the relationship between SERPINE2 and CD68 expression. (C) The expression of SERPINE2 and CD68 in patient tissues were detected by IHC. High levels of SERPINE2 expression are associated with increased expression of CD68. (* p<0.05, **p<0.01, *** p<0.001).

Article Snippet: Besides, in order to explore the effect of SERPINE2 on macrophage polarization, M0 macrophages were treated with recombinant SERPINE2 (0.4 ng/mL, TargetMol) during 24 hours and then harvested for subsequent experiment.

Techniques: Expressing

Journal: Frontiers in Oncology

Article Title: SerpinE2 promotes M2 polarization in macrophage to accelerate colorectal cancer progression

doi: 10.3389/fonc.2025.1585935

Figure Lengend Snippet: The external secretion of SERPINE2 from colorectal cancer cells promotes macrophage polarization to accelerate the development of colorectal cancer. (A) Schema diagram showing that THP-1 cells were treated with PMA, followed by the treatment of SERPINE2 recombinant protein as indicated treatments to obtain activated macrophages. Then tumor cells cocultured with these macrophages. were used to subsequent experiments. (B, C) RT-qPCR and Westen blot displayed SERPINE2 mRNA and Protein expression were upregulated in colorectal cancer cells. (D) The secretion of SERPINE2 in colorectal cancer cells was detected by ELISA. (E) The effect of SERPINE2 recombinant protein on macrophage polarization. (F) RT-qPCR displayed conditioned medium (CM) derived from colorectal cancer cells promotes the upregulation of macrophage M2 markers, compared to normal Intestinal cells. (G) ELISA analysis demonstrated that SERPINE2 secretion was significantly reduced after SERPINE2 knockdown. (H) RT-qPCR displayed conditioned medium with SERPINE2 knockdown down-regulated macrophage M2 markers. (I, J) The conditioned medium from macrophages treated with SERPINE2 recombinant protein promoted cancer cell proliferation (measured by CCK-8 assay) and migration (assessed by Transwell assay. (*p<0.05, **p<0.01, ***p<0.001).

Article Snippet: Besides, in order to explore the effect of SERPINE2 on macrophage polarization, M0 macrophages were treated with recombinant SERPINE2 (0.4 ng/mL, TargetMol) during 24 hours and then harvested for subsequent experiment.

Techniques: Recombinant, Quantitative RT-PCR, Expressing, Enzyme-linked Immunosorbent Assay, Derivative Assay, Knockdown, CCK-8 Assay, Migration, Transwell Assay