anti fpr2 antibody  (Proteintech)

Journal: Journal of Neuroimmune Pharmacology

Article Title: Formyl Peptide Receptor-2-Suppressed Autophagy Promotes the Migration and Invasion of Human Glioblastoma Cells Through PI3K/Akt Signaling

doi: 10.1007/s11481-026-10284-z

Figure Lengend Snippet: The protein expression level of FPR2 in glioma cells and glioma patients is associated with poor prognosis. ( A ) Immunoblot analysis showing the protein expression levels of FPR2 in human monocytes, human astrocytes (NHAs) and glioma cell lines, including LN-229, U87, U251, U118 and A172; human monocytes were used as positive controls. ( B ) Quantitative analysis of the blots depicted in A; * p < 0.05 compared with monocytes, # p < 0.05 compared with U87 cells. ( C ) Immunohistochemical staining suggesting that FPR2 is expressed at higher levels in glioma tissues than in nontumor brain tissues (NBT). Scale bar=100 µm. ( D ) FPR2 expression levels in glioma patients were significantly different across different grades, suggesting a statistically significant difference ( * p < 0.05) compared with Grade II patients and a significant difference ( # p < 0.05) compared with Grade III patients.( E ) Western blotting revealed FPR2 expression in six nontumor brain tissue samples and six primary glioblastoma (Grade IV) tissue samples. ( F ) The overall survival of glioma patients with FPR2 expression, as retrieved from the database https://gliovis.bioinfo.cnio.es/ , revealed that patients with lower FPR2 expression had notably longer survival ( p = 0)

Article Snippet: Afterward, the tissue slices were incubated with an anti-FPR2 antibody (1:200, #30989-1-AP, Proteintech Technology) overnight at 4 °C.

Techniques: Expressing, Western Blot, Immunohistochemical staining, Staining

Journal: Journal of Neuroimmune Pharmacology

Article Title: Formyl Peptide Receptor-2-Suppressed Autophagy Promotes the Migration and Invasion of Human Glioblastoma Cells Through PI3K/Akt Signaling

doi: 10.1007/s11481-026-10284-z

Figure Lengend Snippet: FPR2 knockdown inhibited glioma cell growth, migration and invasion.(A) RT‒qPCR results showing the mRNA expression levels of FPR2 in three groups of U87 cells infected with FPR2-KD. (B) Western blot analysis was performed to detect the protein levels of FPR2 in the three groups of U87 cells infected with FPR2-KD. (C) Quantitative analysis of the FPR2 band intensity from the Western blot shown in (B). *p< 0.05, **p< 0.01 versus the Scr-shRNA group, #p< 0.05 versus the shRNA1 group. (D) Following the infection of U87 cells with FPR2 KD, cellular proliferation was assessed using a CCK8 assay at the indicated time points. (E) After FPR2 KD was transfected into U87 cells, the cell cycle distribution was measured using flow cytometry. A reduction in FPR2 expression led to a notable increase in the number of cells in the G2/M phase and a reduction in the number of cells in the G1 phase. (F) The percentages of cells in the G1, S, and G2/M phases are shown in (E). (G) After U87 cells with stable FPR2 knockdown (KD) were stably transfected, the apoptosis rate was measured using flow cytometry. The decreased expression of FPR2 led to a substantial increase in the percentage of apoptotic cells. (H) The percentage of apoptotic cells is shown in (G). (I) Transwell assay results showing the migratory (upper panel) and invasive (lower panel) capacities of U87 cells in which FPR2 was knocked down (KD) compared with those in the scramble shRNA negative control (Scr-shRNA) group and the untransfected control group. Scale bar=100 µm. (J and K) The numbers of U87 cells that migrated and invaded following FPR2 knockdown, Scr-shRNA transfection and control treatment are presented. (L) Western blotting revealed that FPR2 inhibition initiated a caspase cascade with elevated protein levels of cleaved PARP, cleaved caspase-3/7 and cleaved caspase-8 in U87 cells. (M) The Western blot intensity of the proteins shown in (L) was quantified. All the results are presented as the means ± standard deviations from a minimum of three independent experiments;* p < 0.05 and ** p < 0.01 compared with the Scr-shRNA group.

Article Snippet: Afterward, the tissue slices were incubated with an anti-FPR2 antibody (1:200, #30989-1-AP, Proteintech Technology) overnight at 4 °C.

Techniques: Knockdown, Migration, Expressing, Infection, Western Blot, shRNA, CCK-8 Assay, Transfection, Flow Cytometry, Stable Transfection, Transwell Assay, Negative Control, Control, Inhibition

Journal: Journal of Neuroimmune Pharmacology

Article Title: Formyl Peptide Receptor-2-Suppressed Autophagy Promotes the Migration and Invasion of Human Glioblastoma Cells Through PI3K/Akt Signaling

doi: 10.1007/s11481-026-10284-z

Figure Lengend Snippet: FPR2 knockdown restricts tumor growth in vivo. ( A ) Representative images of tumor-bearing nude mice and the corresponding xenograft tumors obtained from U87/Scr-shRNA cells (left) and U87/FPR2-KD cells (right). ( B ) Growth curve analysis revealed that the tumors derived from U87/FPR2-KD cells grew at a slower rate than those derived from U87/Scr-shRNA cells did at 15 days post-subcutaneous injection, suggesting that FPR2 knockdown inhibited the proliferation of U87/FPR2-KD cells. ** p <0.01 compared with the corresponding Scr-shRNA controls; paired t test, n=8. ( C ) The weights of tumors derived from U87/FPR2 KD cells were lower than those derived from Scr-shRNA cells. ** p < 0.01, paired t test, n=8. ( D ) Western blot analysis revealed a reduction in FPR2 expression in tumors originating from U87 cells with FPR2 knockdown. ( E ) Quantification of FPR2 expression was performed via densitometric analysis with ImageJ software. ( F ) Western blot analysis revealed that cleaved caspase-3 was upregulated in tumors derived from U87/FPR2-KD cells, whereas the expression of caspase-3 was downregulated. ( G ) Cleaved caspase-3 and caspase-3 levels were quantified via densitometric analysis with ImageJ software

Article Snippet: Afterward, the tissue slices were incubated with an anti-FPR2 antibody (1:200, #30989-1-AP, Proteintech Technology) overnight at 4 °C.

Techniques: Knockdown, In Vivo, shRNA, Derivative Assay, Injection, Western Blot, Expressing, Software

Journal: Journal of Neuroimmune Pharmacology

Article Title: Formyl Peptide Receptor-2-Suppressed Autophagy Promotes the Migration and Invasion of Human Glioblastoma Cells Through PI3K/Akt Signaling

doi: 10.1007/s11481-026-10284-z

Figure Lengend Snippet: The downregulation of FPR2 leads to G2/M cell cycle arrest in glioma cells and prevents the activation of PI3K/Akt signaling. ( A ) The knockdown of FPR2 expression suppressed the protein expression of cdc2, cyclin B1, and cdc-25C, whereas the expression of cyclin D1 did not obviously change. ( B ) Quantitative images of cdc2, cyclin B1, cdc-25C and cyclin D1 using densitometric analysis with ImageJ software. ( C ) Immunoblot analysis revealed the levels of the PI3K subunits p85 and p110a, as well as the b-catenin, GSK3, and phosphorylated and total protein levels of Akt following the stable knockdown of FPR2. ( D ) Quantification of b-cateninand GSK3 b, phosphorylation and the total levels of Akt and the PI3K subunits p85 and p110a. ( E ) The inhibition of FPR2 does not alter the expression of p-p65NF-kB/p65NF-kB but does increase the expression of cPLA2. ( F ) The levels of p-p65NF-kB/p65NF-kB and cPLA2 were quantified using densitometric analysis with ImageJ software. ( G ) The activity of nuclear NF-kB was measured by ELISA. N=8 per group. ( H ) cPLA2 enzymatic activity was measured as outlined in the Methods section. All the data are presented as the means ± standard deviations and were derived from three separate experiments; * p < 0.05, ** p < 0.01 compared with the si-NC group

Article Snippet: Afterward, the tissue slices were incubated with an anti-FPR2 antibody (1:200, #30989-1-AP, Proteintech Technology) overnight at 4 °C.

Techniques: Activation Assay, Knockdown, Expressing, Software, Western Blot, Phospho-proteomics, Inhibition, Activity Assay, Enzyme-linked Immunosorbent Assay, Derivative Assay

Journal: Journal of Neuroimmune Pharmacology

Article Title: Formyl Peptide Receptor-2-Suppressed Autophagy Promotes the Migration and Invasion of Human Glioblastoma Cells Through PI3K/Akt Signaling

doi: 10.1007/s11481-026-10284-z

Figure Lengend Snippet: The expression of FPR2 and SQSTM1 is associated with the invasiveness of glioma cells. ( A ) FPR2 positively modulates the protein expression of SQSTM. Compared with that in the shRNA or vector control groups, immunoblot analysis indicates that the protein expression level of SQSTM1 was clearly altered in FPR2-KD U87 cells, FPR2-OE LN-229 cells, and their corresponding controls; * p < 0.05, ** p < 0.01 indicate statistically significant differences in comparison with the shRNA or vector group.( C ) Correlation analysis of FPR2 and SQSTM1 in glioma patient tissues revealed a positive correlation between the mRNA levels of FPR2 and SQSTM1 (p<0.001, r=0.462) (http://gepia.cancer-pku.cn). ( D and F ) FPR2 regulates SQSTM1 expression via autophagy. Immunoblot analysis revealed that SQSTM1 expression levels in U87 cells with FPR2 knockdown and in scrambled shRNA control cells were influenced by treatment with BAF or CQ, as well as by transfection with ATG5 or BECN1 siRNA. ( F ). SQSTM1, BECN1, and ATG5 were quantified via densitometric analysis using ImageJ ( E and G ). * p < 0.05, ** p < 0.01 versus the vehicle or siNC group

Article Snippet: Afterward, the tissue slices were incubated with an anti-FPR2 antibody (1:200, #30989-1-AP, Proteintech Technology) overnight at 4 °C.

Techniques: Expressing, shRNA, Plasmid Preparation, Control, Western Blot, Comparison, Knockdown, Transfection

Journal: Journal of Neuroimmune Pharmacology

Article Title: Formyl Peptide Receptor-2-Suppressed Autophagy Promotes the Migration and Invasion of Human Glioblastoma Cells Through PI3K/Akt Signaling

doi: 10.1007/s11481-026-10284-z

Figure Lengend Snippet: FPR2 suppresses autophagy and induces EMT-like transformation in glioma cells. ( A ) Immunoblot analysis demonstrating the expression of Snail, vimentin, N-cadherin and E-cadherin in FPR2-KD U87 cells, FPR2-OE LN-229 cells, and their respective control cells. ( B and C ) Quantitative graphs showing the protein expression levels of Snail, vimentin, N-cadherin and E-cadherin in FPR2-KD U87 cells and FPR2-OE LN-229 cells compared with those in the shRNA or vector control groups; ** p < 0.01, * p < 0.05. ( D and F ) Immunoblot analysis revealed the expression of Snail, vimentin, N-cadherin and E-cadherin in FPR2-KD U87 cells and control cells infected with shRNA and treated with ATG5 siRNA, BECN1-siRNA (D) or 3-MA ( F ). ( E and G ) Quantitative graphs depicting the relative protein expression levels of Snail, vimentin, N-cadherin and E-cadherin in FPR2-KD U87 cells and shRNA-infected control cells treated with ATG5 siRNA, BECN1-siRNA or 3-MA ( F ); * p < 0.05, ** p < 0.01 versus the Scr-siNC, FPR2 KD-siNC or FPR2 KD vehicle groups. ( H ) Immunoblot analysis revealed the protein levels of Snail in FPR2-KD U87 cells and scramble control cells following transfection with the SQSTM1 overexpression construct. ( I ) Quantitative graphs illustrating the protein levels of Snail in FPR2-KD U87 cells and scramble control cells after transfection with the SQSTM1 overexpression construct. ( J ) Western blot analysis showing the protein expression level of Snail in LN-229 cells overexpressing FPR2 and vector control cells after SQSTM1 siRNA transfection. ( K ) Quantitative images of Snail protein expression levels in FPR2-overexpressing LN-229 cells and vector control cells after transfection with SQSTM1 siRNA; * p < 0.05, ** p < 0.01 relative to the Scr-vector, FPR2 KD-vector, vector-siNC and FPR2 OE-siNC groups

Article Snippet: Afterward, the tissue slices were incubated with an anti-FPR2 antibody (1:200, #30989-1-AP, Proteintech Technology) overnight at 4 °C.

Techniques: Transformation Assay, Western Blot, Expressing, Control, shRNA, Plasmid Preparation, Infection, Transfection, Over Expression, Construct

Journal: Journal of Neuroimmune Pharmacology

Article Title: Formyl Peptide Receptor-2-Suppressed Autophagy Promotes the Migration and Invasion of Human Glioblastoma Cells Through PI3K/Akt Signaling

doi: 10.1007/s11481-026-10284-z

Figure Lengend Snippet: The proposed model explains how the suppression of autophagy by FPR2 facilitates the migration and invasion of GBM cells. In this model, FPR2 activates the PI3K/AKT pathway, leading to the inhibition of autophagy through BECN1 and ATG5. This results in the accumulation of SQSTM1, which inhibits the degradation of Snail. Increased Snail induces EMT-like alterations, thereby facilitating GBM cell migration and invasion

Article Snippet: Afterward, the tissue slices were incubated with an anti-FPR2 antibody (1:200, #30989-1-AP, Proteintech Technology) overnight at 4 °C.

Techniques: Migration, Inhibition

Journal: Journal of Neuroimmune Pharmacology

Article Title: Formyl Peptide Receptor-2-Suppressed Autophagy Promotes the Migration and Invasion of Human Glioblastoma Cells Through PI3K/Akt Signaling

doi: 10.1007/s11481-026-10284-z

Figure Lengend Snippet: The protein expression level of FPR2 in glioma cells and glioma patients is associated with poor prognosis. ( A ) Immunoblot analysis showing the protein expression levels of FPR2 in human monocytes, human astrocytes (NHAs) and glioma cell lines, including LN-229, U87, U251, U118 and A172; human monocytes were used as positive controls. ( B ) Quantitative analysis of the blots depicted in A; * p < 0.05 compared with monocytes, # p < 0.05 compared with U87 cells. ( C ) Immunohistochemical staining suggesting that FPR2 is expressed at higher levels in glioma tissues than in nontumor brain tissues (NBT). Scale bar=100 µm. ( D ) FPR2 expression levels in glioma patients were significantly different across different grades, suggesting a statistically significant difference ( * p < 0.05) compared with Grade II patients and a significant difference ( # p < 0.05) compared with Grade III patients.( E ) Western blotting revealed FPR2 expression in six nontumor brain tissue samples and six primary glioblastoma (Grade IV) tissue samples. ( F ) The overall survival of glioma patients with FPR2 expression, as retrieved from the database https://gliovis.bioinfo.cnio.es/ , revealed that patients with lower FPR2 expression had notably longer survival ( p = 0)

Article Snippet: The sources of the antibodies used were as follows: FPR2 (#30989-1-AP) was purchased from Proteintech Technology (Wuhan, China).

Techniques: Expressing, Western Blot, Immunohistochemical staining, Staining

Journal: Journal of Neuroimmune Pharmacology

Article Title: Formyl Peptide Receptor-2-Suppressed Autophagy Promotes the Migration and Invasion of Human Glioblastoma Cells Through PI3K/Akt Signaling

doi: 10.1007/s11481-026-10284-z

Figure Lengend Snippet: FPR2 knockdown inhibited glioma cell growth, migration and invasion.(A) RT‒qPCR results showing the mRNA expression levels of FPR2 in three groups of U87 cells infected with FPR2-KD. (B) Western blot analysis was performed to detect the protein levels of FPR2 in the three groups of U87 cells infected with FPR2-KD. (C) Quantitative analysis of the FPR2 band intensity from the Western blot shown in (B). *p< 0.05, **p< 0.01 versus the Scr-shRNA group, #p< 0.05 versus the shRNA1 group. (D) Following the infection of U87 cells with FPR2 KD, cellular proliferation was assessed using a CCK8 assay at the indicated time points. (E) After FPR2 KD was transfected into U87 cells, the cell cycle distribution was measured using flow cytometry. A reduction in FPR2 expression led to a notable increase in the number of cells in the G2/M phase and a reduction in the number of cells in the G1 phase. (F) The percentages of cells in the G1, S, and G2/M phases are shown in (E). (G) After U87 cells with stable FPR2 knockdown (KD) were stably transfected, the apoptosis rate was measured using flow cytometry. The decreased expression of FPR2 led to a substantial increase in the percentage of apoptotic cells. (H) The percentage of apoptotic cells is shown in (G). (I) Transwell assay results showing the migratory (upper panel) and invasive (lower panel) capacities of U87 cells in which FPR2 was knocked down (KD) compared with those in the scramble shRNA negative control (Scr-shRNA) group and the untransfected control group. Scale bar=100 µm. (J and K) The numbers of U87 cells that migrated and invaded following FPR2 knockdown, Scr-shRNA transfection and control treatment are presented. (L) Western blotting revealed that FPR2 inhibition initiated a caspase cascade with elevated protein levels of cleaved PARP, cleaved caspase-3/7 and cleaved caspase-8 in U87 cells. (M) The Western blot intensity of the proteins shown in (L) was quantified. All the results are presented as the means ± standard deviations from a minimum of three independent experiments;* p < 0.05 and ** p < 0.01 compared with the Scr-shRNA group.

Article Snippet: The sources of the antibodies used were as follows: FPR2 (#30989-1-AP) was purchased from Proteintech Technology (Wuhan, China).

Techniques: Knockdown, Migration, Expressing, Infection, Western Blot, shRNA, CCK-8 Assay, Transfection, Flow Cytometry, Stable Transfection, Transwell Assay, Negative Control, Control, Inhibition

Journal: Journal of Neuroimmune Pharmacology

Article Title: Formyl Peptide Receptor-2-Suppressed Autophagy Promotes the Migration and Invasion of Human Glioblastoma Cells Through PI3K/Akt Signaling

doi: 10.1007/s11481-026-10284-z

Figure Lengend Snippet: FPR2 knockdown restricts tumor growth in vivo. ( A ) Representative images of tumor-bearing nude mice and the corresponding xenograft tumors obtained from U87/Scr-shRNA cells (left) and U87/FPR2-KD cells (right). ( B ) Growth curve analysis revealed that the tumors derived from U87/FPR2-KD cells grew at a slower rate than those derived from U87/Scr-shRNA cells did at 15 days post-subcutaneous injection, suggesting that FPR2 knockdown inhibited the proliferation of U87/FPR2-KD cells. ** p <0.01 compared with the corresponding Scr-shRNA controls; paired t test, n=8. ( C ) The weights of tumors derived from U87/FPR2 KD cells were lower than those derived from Scr-shRNA cells. ** p < 0.01, paired t test, n=8. ( D ) Western blot analysis revealed a reduction in FPR2 expression in tumors originating from U87 cells with FPR2 knockdown. ( E ) Quantification of FPR2 expression was performed via densitometric analysis with ImageJ software. ( F ) Western blot analysis revealed that cleaved caspase-3 was upregulated in tumors derived from U87/FPR2-KD cells, whereas the expression of caspase-3 was downregulated. ( G ) Cleaved caspase-3 and caspase-3 levels were quantified via densitometric analysis with ImageJ software

Article Snippet: The sources of the antibodies used were as follows: FPR2 (#30989-1-AP) was purchased from Proteintech Technology (Wuhan, China).

Techniques: Knockdown, In Vivo, shRNA, Derivative Assay, Injection, Western Blot, Expressing, Software

Journal: Journal of Neuroimmune Pharmacology

Article Title: Formyl Peptide Receptor-2-Suppressed Autophagy Promotes the Migration and Invasion of Human Glioblastoma Cells Through PI3K/Akt Signaling

doi: 10.1007/s11481-026-10284-z

Figure Lengend Snippet: The downregulation of FPR2 leads to G2/M cell cycle arrest in glioma cells and prevents the activation of PI3K/Akt signaling. ( A ) The knockdown of FPR2 expression suppressed the protein expression of cdc2, cyclin B1, and cdc-25C, whereas the expression of cyclin D1 did not obviously change. ( B ) Quantitative images of cdc2, cyclin B1, cdc-25C and cyclin D1 using densitometric analysis with ImageJ software. ( C ) Immunoblot analysis revealed the levels of the PI3K subunits p85 and p110a, as well as the b-catenin, GSK3, and phosphorylated and total protein levels of Akt following the stable knockdown of FPR2. ( D ) Quantification of b-cateninand GSK3 b, phosphorylation and the total levels of Akt and the PI3K subunits p85 and p110a. ( E ) The inhibition of FPR2 does not alter the expression of p-p65NF-kB/p65NF-kB but does increase the expression of cPLA2. ( F ) The levels of p-p65NF-kB/p65NF-kB and cPLA2 were quantified using densitometric analysis with ImageJ software. ( G ) The activity of nuclear NF-kB was measured by ELISA. N=8 per group. ( H ) cPLA2 enzymatic activity was measured as outlined in the Methods section. All the data are presented as the means ± standard deviations and were derived from three separate experiments; * p < 0.05, ** p < 0.01 compared with the si-NC group

Article Snippet: The sources of the antibodies used were as follows: FPR2 (#30989-1-AP) was purchased from Proteintech Technology (Wuhan, China).

Techniques: Activation Assay, Knockdown, Expressing, Software, Western Blot, Phospho-proteomics, Inhibition, Activity Assay, Enzyme-linked Immunosorbent Assay, Derivative Assay

Journal: Journal of Neuroimmune Pharmacology

Article Title: Formyl Peptide Receptor-2-Suppressed Autophagy Promotes the Migration and Invasion of Human Glioblastoma Cells Through PI3K/Akt Signaling

doi: 10.1007/s11481-026-10284-z

Figure Lengend Snippet: The expression of FPR2 and SQSTM1 is associated with the invasiveness of glioma cells. ( A ) FPR2 positively modulates the protein expression of SQSTM. Compared with that in the shRNA or vector control groups, immunoblot analysis indicates that the protein expression level of SQSTM1 was clearly altered in FPR2-KD U87 cells, FPR2-OE LN-229 cells, and their corresponding controls; * p < 0.05, ** p < 0.01 indicate statistically significant differences in comparison with the shRNA or vector group.( C ) Correlation analysis of FPR2 and SQSTM1 in glioma patient tissues revealed a positive correlation between the mRNA levels of FPR2 and SQSTM1 (p<0.001, r=0.462) (http://gepia.cancer-pku.cn). ( D and F ) FPR2 regulates SQSTM1 expression via autophagy. Immunoblot analysis revealed that SQSTM1 expression levels in U87 cells with FPR2 knockdown and in scrambled shRNA control cells were influenced by treatment with BAF or CQ, as well as by transfection with ATG5 or BECN1 siRNA. ( F ). SQSTM1, BECN1, and ATG5 were quantified via densitometric analysis using ImageJ ( E and G ). * p < 0.05, ** p < 0.01 versus the vehicle or siNC group

Article Snippet: The sources of the antibodies used were as follows: FPR2 (#30989-1-AP) was purchased from Proteintech Technology (Wuhan, China).

Techniques: Expressing, shRNA, Plasmid Preparation, Control, Western Blot, Comparison, Knockdown, Transfection

Journal: Journal of Neuroimmune Pharmacology

Article Title: Formyl Peptide Receptor-2-Suppressed Autophagy Promotes the Migration and Invasion of Human Glioblastoma Cells Through PI3K/Akt Signaling

doi: 10.1007/s11481-026-10284-z

Figure Lengend Snippet: FPR2 suppresses autophagy and induces EMT-like transformation in glioma cells. ( A ) Immunoblot analysis demonstrating the expression of Snail, vimentin, N-cadherin and E-cadherin in FPR2-KD U87 cells, FPR2-OE LN-229 cells, and their respective control cells. ( B and C ) Quantitative graphs showing the protein expression levels of Snail, vimentin, N-cadherin and E-cadherin in FPR2-KD U87 cells and FPR2-OE LN-229 cells compared with those in the shRNA or vector control groups; ** p < 0.01, * p < 0.05. ( D and F ) Immunoblot analysis revealed the expression of Snail, vimentin, N-cadherin and E-cadherin in FPR2-KD U87 cells and control cells infected with shRNA and treated with ATG5 siRNA, BECN1-siRNA (D) or 3-MA ( F ). ( E and G ) Quantitative graphs depicting the relative protein expression levels of Snail, vimentin, N-cadherin and E-cadherin in FPR2-KD U87 cells and shRNA-infected control cells treated with ATG5 siRNA, BECN1-siRNA or 3-MA ( F ); * p < 0.05, ** p < 0.01 versus the Scr-siNC, FPR2 KD-siNC or FPR2 KD vehicle groups. ( H ) Immunoblot analysis revealed the protein levels of Snail in FPR2-KD U87 cells and scramble control cells following transfection with the SQSTM1 overexpression construct. ( I ) Quantitative graphs illustrating the protein levels of Snail in FPR2-KD U87 cells and scramble control cells after transfection with the SQSTM1 overexpression construct. ( J ) Western blot analysis showing the protein expression level of Snail in LN-229 cells overexpressing FPR2 and vector control cells after SQSTM1 siRNA transfection. ( K ) Quantitative images of Snail protein expression levels in FPR2-overexpressing LN-229 cells and vector control cells after transfection with SQSTM1 siRNA; * p < 0.05, ** p < 0.01 relative to the Scr-vector, FPR2 KD-vector, vector-siNC and FPR2 OE-siNC groups

Article Snippet: The sources of the antibodies used were as follows: FPR2 (#30989-1-AP) was purchased from Proteintech Technology (Wuhan, China).

Techniques: Transformation Assay, Western Blot, Expressing, Control, shRNA, Plasmid Preparation, Infection, Transfection, Over Expression, Construct

Journal: Journal of Neuroimmune Pharmacology

Article Title: Formyl Peptide Receptor-2-Suppressed Autophagy Promotes the Migration and Invasion of Human Glioblastoma Cells Through PI3K/Akt Signaling

doi: 10.1007/s11481-026-10284-z

Figure Lengend Snippet: The proposed model explains how the suppression of autophagy by FPR2 facilitates the migration and invasion of GBM cells. In this model, FPR2 activates the PI3K/AKT pathway, leading to the inhibition of autophagy through BECN1 and ATG5. This results in the accumulation of SQSTM1, which inhibits the degradation of Snail. Increased Snail induces EMT-like alterations, thereby facilitating GBM cell migration and invasion

Article Snippet: The sources of the antibodies used were as follows: FPR2 (#30989-1-AP) was purchased from Proteintech Technology (Wuhan, China).

Techniques: Migration, Inhibition

Journal: International Dental Journal

Article Title: Elevated LL-37/FPR2 Axis and its Regulatory Role for Gingival Fibroblasts in Periodontitis

doi: 10.1016/j.identj.2025.103943

Figure Lengend Snippet: LL-37 activates FPR2 to enhance inflammatory response in GFs. (A-B) Healthy GFs were treated with LPS (1 μg/ml) for 4 h and then treated with LL-37 (2, 4 and 8 μM) for 24 h, and the mRNA expression levels of IL-1β, IL-8 and CCL2 were evaluated by RT-qPCR (n = 6). (C) FPR2 was silenced in healthy GFs by siRNA, and the mRNA (n = 5) and protein expression levels were evaluated by RT-qPCR and Western blot. (D-E) Intracellular calcium mobilization in response to 2 µM LL-37 in control (NC) and FPR2-knockdown (siFPR2) human GFs (n = 3). The arrow indicates the time of LL-37 application. Traces represent mean fluorescence intensity (ΔF/F₀). (F) NC and siFPR2 healthy GFs were treated with LPS (1 μg/ml) for 4 h and then treated with LL-37 (2 μM) for 24 h, and the mRNA expression levels of IL-1β, IL-8 and CCL2 were evaluated by RT-qPCR (n = 6). (G-H) Intracellular calcium mobilization in response to 4 µM LL-37 in NC and siFPR2 human GFs (n = 3). The arrow indicates the time of LL-37 application. Traces represent mean fluorescence intensity (ΔF/F₀). (I) NC and siFPR2 healthy GFs were treated with LPS (1 μg/ml) for 4 h and then treated with LL-37 (4 μM) for 24 h, and the mRNA expression levels of IL-1β, IL-8 and CCL2 were evaluated by RT-qPCR (n = 6). (J-K) FPR2 was silenced in inflamed GFs by siRNA, and the mRNA expressions of IL-1β, IL-8 and CCL2 were evaluated by RT-qPCR (n = 6). ns, no significance. * P < . 05, ** P < . 01 (1-way ANOVA with Dunn's multiple comparisons test).

Article Snippet: After blocking with 5% BSA, sections were incubated with the following primary antibodies: LL-37 (ab69484, Abcam) and FPR2 (NLS1878, Novus Biologicals), followed by secondary antibodies, and counterstained with hematoxylin.

Techniques: Expressing, Quantitative RT-PCR, Western Blot, Control, Knockdown, Fluorescence

Journal: International Dental Journal

Article Title: Elevated LL-37/FPR2 Axis and its Regulatory Role for Gingival Fibroblasts in Periodontitis

doi: 10.1016/j.identj.2025.103943

Figure Lengend Snippet: LL-37 and FPR2 are upregulated in gingival tissues of periodontitis patients. (A) Transcriptions of LL-37 and FPR2 in the healthy and the periodontitis groups from GSE16134 . (B) RT-qPCR analysis of mRNA expression levels of LL-37 (n = 30). (C) ELISA analysis of the concentrations of LL-37 in GCF (n = 30). (D) RT-qPCR analysis of mRNA expression levels of FPR2 (n = 30). (E) Western blot and quantification of protein expression levels of FPR2 (n = 6). (F) Hematoxylin-eosin staining, IHC staining of LL-37 and FPR2 and positivity rate across cells in gingival connective tissues (n = 6). (G) The correlation of LL-37 expression and concentration with FPR2 mRNA expression in periodontitis groups. H, the healthy group; P, the periodontitis group; ** P < . 01, *** P < . 001 (Mann Whitney test and Spearman's correlation analysis).

Article Snippet: After blocking with 5% BSA, sections were incubated with the following primary antibodies: LL-37 (ab69484, Abcam) and FPR2 (NLS1878, Novus Biologicals), followed by secondary antibodies, and counterstained with hematoxylin.

Techniques: Quantitative RT-PCR, Expressing, Enzyme-linked Immunosorbent Assay, Western Blot, Staining, Immunohistochemistry, Concentration Assay, MANN-WHITNEY

Journal: International Dental Journal

Article Title: Elevated LL-37/FPR2 Axis and its Regulatory Role for Gingival Fibroblasts in Periodontitis

doi: 10.1016/j.identj.2025.103943

Figure Lengend Snippet: FPR2 is upregulated in GFs from periodontitis patients. (A) Representative mIHC staining of FPR2 and Vimentin in gingival tissues of the healthy and periodontitis groups, and quantification of positive rate of FPR2 in fibroblasts (n = 6). Scale bar = 200 µm or 20 µm. (B) Primary GFs were isolated from gingival tissues of the healthy and periodontitis groups. Created with BioRender.com. (C) Representative mIHC staining of FPR2, Cytokeratin and Vimentin in primary GFs, and quantification of positive rate of FPR2 in primary GFs. Scale bar = 100 µm. (D) RT-qPCR analysis of mRNA expression of FPR2 in primary GFs (n = 15). (E) Western blot and quantification of protein levels of FPR2 in primary GFs (n = 6). ** P < . 01 (Mann Whitney test).

Article Snippet: After blocking with 5% BSA, sections were incubated with the following primary antibodies: LL-37 (ab69484, Abcam) and FPR2 (NLS1878, Novus Biologicals), followed by secondary antibodies, and counterstained with hematoxylin.

Techniques: Staining, Isolation, Quantitative RT-PCR, Expressing, Western Blot, MANN-WHITNEY

Journal: International Dental Journal

Article Title: Elevated LL-37/FPR2 Axis and its Regulatory Role for Gingival Fibroblasts in Periodontitis

doi: 10.1016/j.identj.2025.103943

Figure Lengend Snippet: LL-37 and FPR2 indicate the local periodontal status. (A) The ROC curve analysis of LL-37 mRNA expression in gingival tissues of the healthy and periodontitis groups (n = 30). (B) The ROC curve analysis of FPR2 mRNA expression in gingival tissues of the healthy and periodontitis groups (n = 30). (C) The ROC curve analysis of combination of LL-37 and FPR2 mRNA expression in gingival tissues of the healthy and periodontitis groups (n = 30).

Article Snippet: After blocking with 5% BSA, sections were incubated with the following primary antibodies: LL-37 (ab69484, Abcam) and FPR2 (NLS1878, Novus Biologicals), followed by secondary antibodies, and counterstained with hematoxylin.

Techniques: Expressing

Journal: International Dental Journal

Article Title: Elevated LL-37/FPR2 Axis and its Regulatory Role for Gingival Fibroblasts in Periodontitis

doi: 10.1016/j.identj.2025.103943

Figure Lengend Snippet: LL-37 and FPR2 show positive correlation with periodontitis clinical parameters. (A) The correlation of LL-37 mRNA expression in gingival tissues with PD and CAL of periodontitis patients (n = 30). (B) The correlation of FPR2 mRNA expression with PD and CAL of periodontitis patients (n = 30). (C) Periodontitis patients were stratified into 2 groups [ LL-37 low (n = 15) and LL-37 high (n = 15)] based on LL-37 (cut-off: 0.012296) levels. (D) The PD and CAL levels in the LL-37 low and LL-37 high groups. (E) The FPR2 mRNA expression levels in the LL-37 low and LL-37 high groups. (F) The correlation of LL-37 and FPR2 mRNA expression with PD and CAL in the LL-37 low groups. (G) The correlation of LL-37 and FPR2 mRNA expression with PD and CAL in the LL-37 high groups. (H) Periodontitis patients were stratified into 4 groups [ LL-37 low FPR2 low (n = 10), LL-37 low FPR2 high (n = 5), LL-37 high FPR2 low (n = 7) and LL-37 high FPR2 high (n = 8)] based on LL-37 (cut-off: 0.012296) and FPR2 (cut-off: 0.4788) levels. (I) Schematic illustrating that high concentration of LL-37 amplifying pro-inflammation in periodontitis. * P < . 05, *** P < . 001 (Spearman’s correlation analysis, Mann Whitney test and 1-way ANOVA with Dunn’s multiple comparisons test).

Article Snippet: After blocking with 5% BSA, sections were incubated with the following primary antibodies: LL-37 (ab69484, Abcam) and FPR2 (NLS1878, Novus Biologicals), followed by secondary antibodies, and counterstained with hematoxylin.

Techniques: Expressing, Concentration Assay, MANN-WHITNEY

Journal: International Dental Journal

Article Title: Elevated LL-37/FPR2 Axis and its Regulatory Role for Gingival Fibroblasts in Periodontitis

doi: 10.1016/j.identj.2025.103943

Figure Lengend Snippet: LL-37 activates FPR2 to enhance inflammatory response in GFs. (A-B) Healthy GFs were treated with LPS (1 μg/ml) for 4 h and then treated with LL-37 (2, 4 and 8 μM) for 24 h, and the mRNA expression levels of IL-1β, IL-8 and CCL2 were evaluated by RT-qPCR (n = 6). (C) FPR2 was silenced in healthy GFs by siRNA, and the mRNA (n = 5) and protein expression levels were evaluated by RT-qPCR and Western blot. (D-E) Intracellular calcium mobilization in response to 2 µM LL-37 in control (NC) and FPR2-knockdown (siFPR2) human GFs (n = 3). The arrow indicates the time of LL-37 application. Traces represent mean fluorescence intensity (ΔF/F₀). (F) NC and siFPR2 healthy GFs were treated with LPS (1 μg/ml) for 4 h and then treated with LL-37 (2 μM) for 24 h, and the mRNA expression levels of IL-1β, IL-8 and CCL2 were evaluated by RT-qPCR (n = 6). (G-H) Intracellular calcium mobilization in response to 4 µM LL-37 in NC and siFPR2 human GFs (n = 3). The arrow indicates the time of LL-37 application. Traces represent mean fluorescence intensity (ΔF/F₀). (I) NC and siFPR2 healthy GFs were treated with LPS (1 μg/ml) for 4 h and then treated with LL-37 (4 μM) for 24 h, and the mRNA expression levels of IL-1β, IL-8 and CCL2 were evaluated by RT-qPCR (n = 6). (J-K) FPR2 was silenced in inflamed GFs by siRNA, and the mRNA expressions of IL-1β, IL-8 and CCL2 were evaluated by RT-qPCR (n = 6). ns, no significance. * P < . 05, ** P < . 01 (1-way ANOVA with Dunn's multiple comparisons test).

Article Snippet: The membranes were blocked with 5% bovine serum albumin (BSA) and incubated overnight with primary antibodies against FPR2 (sc-57141, Santa Cruz, Delaware, CA, USA) and β-actin (4970, Cell Signaling Technology, Danvers, MA, USA).

Techniques: Expressing, Quantitative RT-PCR, Western Blot, Control, Knockdown, Fluorescence

Journal: International Dental Journal

Article Title: Elevated LL-37/FPR2 Axis and its Regulatory Role for Gingival Fibroblasts in Periodontitis

doi: 10.1016/j.identj.2025.103943

Figure Lengend Snippet: LL-37 and FPR2 are upregulated in gingival tissues of periodontitis patients. (A) Transcriptions of LL-37 and FPR2 in the healthy and the periodontitis groups from GSE16134 . (B) RT-qPCR analysis of mRNA expression levels of LL-37 (n = 30). (C) ELISA analysis of the concentrations of LL-37 in GCF (n = 30). (D) RT-qPCR analysis of mRNA expression levels of FPR2 (n = 30). (E) Western blot and quantification of protein expression levels of FPR2 (n = 6). (F) Hematoxylin-eosin staining, IHC staining of LL-37 and FPR2 and positivity rate across cells in gingival connective tissues (n = 6). (G) The correlation of LL-37 expression and concentration with FPR2 mRNA expression in periodontitis groups. H, the healthy group; P, the periodontitis group; ** P < . 01, *** P < . 001 (Mann Whitney test and Spearman's correlation analysis).

Article Snippet: The membranes were blocked with 5% bovine serum albumin (BSA) and incubated overnight with primary antibodies against FPR2 (sc-57141, Santa Cruz, Delaware, CA, USA) and β-actin (4970, Cell Signaling Technology, Danvers, MA, USA).

Techniques: Quantitative RT-PCR, Expressing, Enzyme-linked Immunosorbent Assay, Western Blot, Staining, Immunohistochemistry, Concentration Assay, MANN-WHITNEY

Journal: International Dental Journal

Article Title: Elevated LL-37/FPR2 Axis and its Regulatory Role for Gingival Fibroblasts in Periodontitis

doi: 10.1016/j.identj.2025.103943

Figure Lengend Snippet: FPR2 is upregulated in GFs from periodontitis patients. (A) Representative mIHC staining of FPR2 and Vimentin in gingival tissues of the healthy and periodontitis groups, and quantification of positive rate of FPR2 in fibroblasts (n = 6). Scale bar = 200 µm or 20 µm. (B) Primary GFs were isolated from gingival tissues of the healthy and periodontitis groups. Created with BioRender.com. (C) Representative mIHC staining of FPR2, Cytokeratin and Vimentin in primary GFs, and quantification of positive rate of FPR2 in primary GFs. Scale bar = 100 µm. (D) RT-qPCR analysis of mRNA expression of FPR2 in primary GFs (n = 15). (E) Western blot and quantification of protein levels of FPR2 in primary GFs (n = 6). ** P < . 01 (Mann Whitney test).

Article Snippet: The membranes were blocked with 5% bovine serum albumin (BSA) and incubated overnight with primary antibodies against FPR2 (sc-57141, Santa Cruz, Delaware, CA, USA) and β-actin (4970, Cell Signaling Technology, Danvers, MA, USA).

Techniques: Staining, Isolation, Quantitative RT-PCR, Expressing, Western Blot, MANN-WHITNEY

Journal: International Dental Journal

Article Title: Elevated LL-37/FPR2 Axis and its Regulatory Role for Gingival Fibroblasts in Periodontitis

doi: 10.1016/j.identj.2025.103943

Figure Lengend Snippet: LL-37 and FPR2 indicate the local periodontal status. (A) The ROC curve analysis of LL-37 mRNA expression in gingival tissues of the healthy and periodontitis groups (n = 30). (B) The ROC curve analysis of FPR2 mRNA expression in gingival tissues of the healthy and periodontitis groups (n = 30). (C) The ROC curve analysis of combination of LL-37 and FPR2 mRNA expression in gingival tissues of the healthy and periodontitis groups (n = 30).

Article Snippet: The membranes were blocked with 5% bovine serum albumin (BSA) and incubated overnight with primary antibodies against FPR2 (sc-57141, Santa Cruz, Delaware, CA, USA) and β-actin (4970, Cell Signaling Technology, Danvers, MA, USA).

Techniques: Expressing

Journal: International Dental Journal

Article Title: Elevated LL-37/FPR2 Axis and its Regulatory Role for Gingival Fibroblasts in Periodontitis

doi: 10.1016/j.identj.2025.103943

Figure Lengend Snippet: LL-37 and FPR2 show positive correlation with periodontitis clinical parameters. (A) The correlation of LL-37 mRNA expression in gingival tissues with PD and CAL of periodontitis patients (n = 30). (B) The correlation of FPR2 mRNA expression with PD and CAL of periodontitis patients (n = 30). (C) Periodontitis patients were stratified into 2 groups [ LL-37 low (n = 15) and LL-37 high (n = 15)] based on LL-37 (cut-off: 0.012296) levels. (D) The PD and CAL levels in the LL-37 low and LL-37 high groups. (E) The FPR2 mRNA expression levels in the LL-37 low and LL-37 high groups. (F) The correlation of LL-37 and FPR2 mRNA expression with PD and CAL in the LL-37 low groups. (G) The correlation of LL-37 and FPR2 mRNA expression with PD and CAL in the LL-37 high groups. (H) Periodontitis patients were stratified into 4 groups [ LL-37 low FPR2 low (n = 10), LL-37 low FPR2 high (n = 5), LL-37 high FPR2 low (n = 7) and LL-37 high FPR2 high (n = 8)] based on LL-37 (cut-off: 0.012296) and FPR2 (cut-off: 0.4788) levels. (I) Schematic illustrating that high concentration of LL-37 amplifying pro-inflammation in periodontitis. * P < . 05, *** P < . 001 (Spearman’s correlation analysis, Mann Whitney test and 1-way ANOVA with Dunn’s multiple comparisons test).

Article Snippet: The membranes were blocked with 5% bovine serum albumin (BSA) and incubated overnight with primary antibodies against FPR2 (sc-57141, Santa Cruz, Delaware, CA, USA) and β-actin (4970, Cell Signaling Technology, Danvers, MA, USA).

Techniques: Expressing, Concentration Assay, MANN-WHITNEY