Journal: Cells

Article Title: Overexpression and Activation of αvβ3 Integrin Differentially Affects TGFβ2 Signaling in Human Trabecular Meshwork Cells

doi: 10.3390/cells10081923

Figure Lengend Snippet: Differentially expressed genes in WTβ3 and/or CAβ3 cells that are associated with glaucoma. Except where noted by *, Log 2 FC values were reported in DGE analysis using EdgeR. * Genes that were filtered out due to low abundance did not originally have a FC determined (ND). Log 2 FC was calculated from the raw count data. The values in parentheses were originally calculated using EdgeR.

Article Snippet: ELISA analysis was performed using an R&D Systems Human TGF-beta 2 Quantikine ELISA Kit (R & D Systems, Minneapolis, MN), and the procedure was performed according to the manufacturer’s instructions.

Techniques: Migration, Activity Assay, Binding Assay, Ubiquitin Proteomics

Journal: Cells

Article Title: Overexpression and Activation of αvβ3 Integrin Differentially Affects TGFβ2 Signaling in Human Trabecular Meshwork Cells

doi: 10.3390/cells10081923

Figure Lengend Snippet: Differentially expressed genes in WTβ3 and/or CAβ3 cells that are associated with IOP regulation. Log 2 FC values were reported in DGE analysis using EdgeR.

Article Snippet: ELISA analysis was performed using an R&D Systems Human TGF-beta 2 Quantikine ELISA Kit (R & D Systems, Minneapolis, MN), and the procedure was performed according to the manufacturer’s instructions.

Techniques:

Journal: Cancer discovery

Article Title: Active CREB1 promotes a malignant TGFβ2 autocrine loop in glioblastoma.

doi: 10.1158/2159-8290.CD-14-0275

Figure Lengend Snippet: Figure 2. TGFβ induces TGFβ2 expression in GBM and non-GBM cell lines. A, qRT-PCR of TGFB 1 , TGFB 2 , and TGFB 3 in LN229 cells treated with TGFβ1 for 3 hours. GAPDH mRNA levels were used as an internal normalization control. ***, P < 0.005, using the Student t test; data, mean ± SD. B, qRT-PCR of TGFB 2 in LN229 cells treated with TGFβ1, TGFβ2, and TGFβ3 for 3 hours. GAPDH mRNA levels were used as an internal normalization control. *, P < 0.05, using the Student t test; data, mean ± SD. C, secreted TGFβ2 protein levels determined by ELISA in culture supernatant from LN229 cells treated with TGFβ for 72 hours. ***, P < 0.005, using the Student t test; data, mean ± SD. D, immunoblot analysis and qRT-PCR of TGF b 2 in LN229 cells treated with TGFβ1 and/or the TβRI inhibitor (TβRI inh.) LY-2109761 for 3 hours. GAPDH mRNA levels were used as an internal normalization control. *, P < 0.05, using the Student t test; data, mean ± SD. E, qRT-PCR of TGFB 2 in GBM and non-GBM cell lines treated with TGFβ for 3 hours. GAPDH mRNA levels were used as an internal normalization control. ***, P < 0.005, using the Student t test; data, mean ± SD.

Article Snippet: For the quantitative determination of TGFβ2 protein levels secreted to the media, we used the Human TGFβ2 Quantikine ELISA Kit (R&D Systems) following the manufacturer’s specifi cations.

Techniques: Expressing, Quantitative RT-PCR, Control, Enzyme-linked Immunosorbent Assay, Western Blot

Journal: Cancer discovery

Article Title: Active CREB1 promotes a malignant TGFβ2 autocrine loop in glioblastoma.

doi: 10.1158/2159-8290.CD-14-0275

Figure Lengend Snippet: Figure 3. CREB1 regulates the autocrine induction of TGFβ2 by TGFβ. A, nucleotide sequence of the proximal region of the TGFB 2 promoter. The SBEs and CREB1 site (CRE) are indicated relative to the transcription start site. ClustalW sequence alignment for 3 animal species [ Homo sapiens ( H.s .), Pan troglodytes ( P.t. ), and Mus musculus ( M.m .)] shows the conservation of the binding sites. B, qRT-PCR of TGFB 2 and CREB1 in LN229 cells expressing an shRNA targeting CREB1 treated with TGFβ for 3 hours. GAPDH mRNA levels were used as an internal normalization control. ***, P < 0.005, using the Student t test; data, mean ± SD. C, qRT-PCR of TGFB 2 and CREB1 in LN229 cells expressing an siRNA targeting CREB1 treated with TGFβ for 3 hours. GAPDH mRNA levels were used as an internal normalization control. ***, P < 0.005, using the Student t test; data, mean ± SD. D, immunoblot analysis and qRT-PCR of TGFβ2 in LN229 cells expressing ICER treated with TGFβ for 3 hours. GAPDH mRNA levels were used as an internal normalization control. ***, P < 0.005, using the Student t test; data, mean ± SD. The molecular weights are shown.

Article Snippet: For the quantitative determination of TGFβ2 protein levels secreted to the media, we used the Human TGFβ2 Quantikine ELISA Kit (R&D Systems) following the manufacturer’s specifi cations.

Techniques: Sequencing, Binding Assay, Quantitative RT-PCR, Expressing, shRNA, Control, Western Blot

Journal: Cancer discovery

Article Title: Active CREB1 promotes a malignant TGFβ2 autocrine loop in glioblastoma.

doi: 10.1158/2159-8290.CD-14-0275

Figure Lengend Snippet: Figure 5. PI3K and RSK regulate the TGFβ- mediated induction of TGFβ2 through CREB1. A, immunoblot analysis and qRT-PCR of TGFB2 in LN229 cells treated with TGFβ for 3 hours and the PI3K inhibitor (inh) LY-294002 for 24 hours. GAPDH mRNA levels were used as an internal normalization control. ***, P < 0.005, using the Student t test; data, mean ± SD. B, immunoblot analysis and qRT-PCR of TGFB2 in LN229 cells treated with increasing amounts of the RSK inhibitor BI-D1870 for 24 hours and TGFβ for 3 hours. GAPDH mRNA levels were used as an internal normalization control. ***, P < 0.005, using the Student t test; data, mean ± SD. C, secreted TGFβ2 protein levels determined by ELISA in LN229 cells treated with TGFβ for 48 hours and the PI3K inhibitor for 72 hours. *, P < 0.05, using the Student t test; data, mean ± SD. D, secreted TGFβ2 protein levels determined by ELISA in LN229 cells treated with the RSK inhibitor BI-D1870 for 72 hours and TGFβ for 48 hours. *, P < 0.05, using the Student t test; data, mean ± SD.

Article Snippet: For the quantitative determination of TGFβ2 protein levels secreted to the media, we used the Human TGFβ2 Quantikine ELISA Kit (R&D Systems) following the manufacturer’s specifi cations.

Techniques: Western Blot, Quantitative RT-PCR, Control, Enzyme-linked Immunosorbent Assay

Journal: Cancer discovery

Article Title: Active CREB1 promotes a malignant TGFβ2 autocrine loop in glioblastoma.

doi: 10.1158/2159-8290.CD-14-0275

Figure Lengend Snippet: Figure 6. TGFβ2 correlates with CREB1 expression in GBM patient tumors. A and B, graphs showing the correlation between CREB1 and TGFB 1 (B) or TGFB 2 (A) mRNA levels in patient GBM tumor samples. Data obtained from the REMBRANDT database. A Spearman test was used, and the correlation coeffi cient (ρ) and the two-tailed P value are shown. C, graph showing the correlation between p-CREB1 and TGFβ2 protein levels in tissue microarrays (TMA) from patient GBM samples. Not all spots were evaluable in all stainings. A Spearman test was used, and the correlation coeffi cient (ρ) and the two- tailed signifi cance are shown. Representative images from the TMAs are shown; scale bar, 50 μm. D, Kaplan–Meier curves showing the OS of patients with TGFB2 mRNA levels upregulated ≥3-fold and CREB1 mRNA levels upregulated ≥2-fold. Statistical signifi cance was assessed by the log-rank test. Data obtained from the REMBRANDT database.

Article Snippet: For the quantitative determination of TGFβ2 protein levels secreted to the media, we used the Human TGFβ2 Quantikine ELISA Kit (R&D Systems) following the manufacturer’s specifi cations.

Techniques: Expressing, Two Tailed Test

Journal: Cancer discovery

Article Title: Active CREB1 promotes a malignant TGFβ2 autocrine loop in glioblastoma.

doi: 10.1158/2159-8290.CD-14-0275

Figure Lengend Snippet: Figure 7. CREB1 regulates TGFβ2 expression in PDX models. A, scheme showing the experimental procedure. B, IHC of p-CREB1 and TGFβ2 from mouse tumors 60 days after inoculation with neurospheres expressing shRNAs targeting CREB1 and control shRNAs; scale bar, 50 μm (C). Kaplan–Meier survival curves from mice in B. D, the TGFβ2 malignant autocrine loop. In GBM, TGFβ collaborates with the PI3K and RSK pathways through a CREB1– SMAD3 transcriptional complex to induce TGFβ2 expression. This leads to the generation of an autocrine loop and accumulation of TGFβ2 in the tumor, hyperactivation of TGFβ, and tumor progression.

Article Snippet: For the quantitative determination of TGFβ2 protein levels secreted to the media, we used the Human TGFβ2 Quantikine ELISA Kit (R&D Systems) following the manufacturer’s specifi cations.

Techniques: Expressing, Paraffin-embedded Immunohistochemistry, Control

Journal: PLoS ONE

Article Title: MicroRNA-30b controls endothelial cell capillary morphogenesis through regulation of transforming growth factor beta 2

doi: 10.1371/journal.pone.0185619

Figure Lengend Snippet: (A) HUVECs were transfected with either control mimic (con) or miR-30b mimic (30b) and levels of TGFβ1 and TGFβ2 mRNA were assessed by qRT-PCR. Expression levels relative to control mimic transfected cells and normalized to β-actin expression are presented as the mean ± SEM (n = 2). Overexpression of miR-30b significantly increases TGFβ2 expression. * P < 0.05, ** P < 0.01 as determined by unpaired Student’s t -test. (B) Cells were transfected with 20 nM of either control mimic (control) or miR-30b mimic (miR-30b) and protein lysates were collected after 48 hours for assessment of TGFβ2 protein levels by western blot. β-actin was used as endogenous control. (C) ELISAs for TGFβ1 and TGFβ2 were performed with 24 hour conditioned supernates from HUVECs transfected with 20 nM of either control or miR-30b mimic. Data represents the mean ± SEM (n = 2). Overexpression of miR-30b significantly increases TGFβ2 secretion into cell culture supernate. * P = 0.044 as determined by unpaired Student’s t -test. (D) HUVECs were transfected with 20 nM of either control mimic (control) or miR-30b mimic (miR-30b) and protein lysates were collected after 48 hours for assessment of Smad2 phosphorylation by western blot.

Article Snippet: Primary antibodies used were: TGFβ2 (V, SC-90), ATF-2 (C-19, SC-187), and phospho-ATF-2 (F-1, SC-8398) from Santa Cruz Biotechnology (Santa Cruz, CA), phospho-Smad2 (S465/467) from Cell Signaling Technology (3101; Danvers, MA), Smad2 from Invitrogen (511300; Carlsbad, CA), β-Actin (clone AC-74) from Sigma-Aldrich (A5316; St. Louis, MO), anti-TGFβ2 neutralizing antibody (AB-12-NA) and Normal Rabbit IgG (AB-105-C) from R&D Systems (Minneapolis, MN).

Techniques: Transfection, Control, Quantitative RT-PCR, Expressing, Over Expression, Western Blot, Cell Culture, Phospho-proteomics

Journal: PLoS ONE

Article Title: MicroRNA-30b controls endothelial cell capillary morphogenesis through regulation of transforming growth factor beta 2

doi: 10.1371/journal.pone.0185619

Figure Lengend Snippet: (A) JDP2 mRNA expression was assessed in HUVECs transfected with miR-30b mimic (20 nM) as compared to control by qRT-PCR. Data represents the mean ± SEM (n = 3) normalized to β-actin as endogenous control. * P = 0.016 as determined by unpaired Student’s t -test. (B) HUVEC were transfected with 50 nM of either control siRNA or ATF2 siRNA 1 or 2 and RNA was isolated at 48 hours post transfection. Levels of ATF2 and TGFβ2 mRNA were assessed by qRT-PCR with β-actin as endogenous control. Data presented is mean ± SEM (n = 2). Statistically significant decreases in ATF2 and TGFβ2 expression were seen in ATF2 siRNA treated cells as compared to control siRNA treated cells. * P < 0.05, ** P < 0.01, *** P < 0.001 as determined by unpaired Student’s t -tests for each ATF2 siRNA compared to control siRNA. (C) Cells transfected with 5 nM of either control siRNA or ATF2 siRNA 1 were seeded onto growth factor reduced BME and the formation of capillary-like cord structures and number of loops was assessed after 24 hours. (D) A statistically significant increase in cord formation was observed in cells depleted of ATF2 through siRNA. Data represents the mean ± SEM (n = 2). * P = 0.041 as determined by unpaired Student’s t -test. (E) HUVECs were co-transfected with miRNA mimic (20 nM) and ATF2 siRNA 1 or 2 (50 nM) in the combinations displayed and cell lysates were collected at 48 hours post transfection and assessed for TGFβ2 mRNA expression. Data presented is mean ± SEM (n = 2). * P < 0.05, ** P < 0.01, *** P < 0.001 as determined by ANOVA with post hoc analysis. (F) Cells were transfected as in (E) using miRNA mimic (20 nM) and ATF2 siRNA 1 (5 nM) and serum starved overnight in MCDB 131 with 0.5% FBS prior to protein expression analysis by western blot. Data is representative of expression levels observed in two independently performed experiments.

Article Snippet: Primary antibodies used were: TGFβ2 (V, SC-90), ATF-2 (C-19, SC-187), and phospho-ATF-2 (F-1, SC-8398) from Santa Cruz Biotechnology (Santa Cruz, CA), phospho-Smad2 (S465/467) from Cell Signaling Technology (3101; Danvers, MA), Smad2 from Invitrogen (511300; Carlsbad, CA), β-Actin (clone AC-74) from Sigma-Aldrich (A5316; St. Louis, MO), anti-TGFβ2 neutralizing antibody (AB-12-NA) and Normal Rabbit IgG (AB-105-C) from R&D Systems (Minneapolis, MN).

Techniques: Expressing, Transfection, Control, Quantitative RT-PCR, Isolation, Western Blot

Journal: PLoS ONE

Article Title: MicroRNA-30b controls endothelial cell capillary morphogenesis through regulation of transforming growth factor beta 2

doi: 10.1371/journal.pone.0185619

Figure Lengend Snippet: (A) HUVECs were serum starved overnight in MCDB 131 with 0.5% FBS and stimulated with VEGF (50 ng/ml) in the presence or absence of Avastin (1 μg/ml) for 24 hours. Data represents the mean ± SEM (n = 2) for expression of TGFβ1 and TGFβ2 assessed by qRT-PCR relative to β-actin endogenous control. * P < 0.05, ** P < 0.01, *** P < 0.001 as determined by ANOVA. (B) HUVECs were treated with 5 ng/ml of TGFβ2 for 3 days prior to seeding onto growth factor reduced BME for assessment of capillary-like cord formation after 24 hours. (C) A significant decrease in cord formation is observed in the TGFβ2 treated group. Data represents the mean ± SEM (n = 2). ** P = 0.0072 as determined by unpaired Student’s t -test. (D) HUVECs transfected with 1 nM control or miR-30b mimic were treated 4 hours post transfection with 0.8 μg/ml anti-TGFβ2 neutralizing antibody or rabbit IgG. Media was refreshed after 24 hours, again with rabbit IgG or anti-TGFβ2 antibody and cells were seeded onto growth factor reduced BME 24 hours later (ie. 48 hours post transfection) in media containing rabbit IgG or anti-TGFβ2 antibody. (E) Data represents the mean ± SEM (n = 3) of the number of capillary-like cord structures or number of loops formed after 24 hours on BME. * P < 0.05, ns denotes not significant as determined by ANOVA with post hoc analysis.

Article Snippet: Primary antibodies used were: TGFβ2 (V, SC-90), ATF-2 (C-19, SC-187), and phospho-ATF-2 (F-1, SC-8398) from Santa Cruz Biotechnology (Santa Cruz, CA), phospho-Smad2 (S465/467) from Cell Signaling Technology (3101; Danvers, MA), Smad2 from Invitrogen (511300; Carlsbad, CA), β-Actin (clone AC-74) from Sigma-Aldrich (A5316; St. Louis, MO), anti-TGFβ2 neutralizing antibody (AB-12-NA) and Normal Rabbit IgG (AB-105-C) from R&D Systems (Minneapolis, MN).

Techniques: Expressing, Quantitative RT-PCR, Control, Transfection

Journal: bioRxiv

Article Title: Macrophage Migration Inhibitory Factor (MIF)-CD74 Signaling Pathway Mediates Trabecular Meshwork Dysfunction in Glaucoma

doi: 10.64898/2026.03.18.712673

Figure Lengend Snippet: Wild-type C57BL/6 mice (n=12/group) were injected intravitreally with either LV-TGF-β2 or LV-null vectors. ( A ) Weekly IOP measurements demonstrate significant and sustained IOP elevation in LV-TGF-β2-injected mice compared with LV-null controls. ( B ) Immunofluorescence staining of anterior segment cross-sections for α-SMA and MIF shows co-localization of MIF with the TM marker α-SMA, indicating increased MIF expression in the TM of LV-TGF-β2 injected mice. ( C-E ) qPCR ( C ) and western blot ( D, E ) analyses of anterior segment tissues show upregulation of MIF and CD74 accompanied by suppression of Blimp-1 in LV-TGF-β2-injected mice. Increased expression of profibrotic markers, including α-SMA, Fn-1, and MYOC, was also evident in LV-TGF-β2-injected mice. Western blot bands were quantified by densitometric analysis using ImageJ and normalized to the housekeeping control β-actin, and protein levels are presented as relative expression (AU) ( E ). Data represent mean ± SD. **p<0.005, ***p<0.0005, and ****p<0.0001. Two-way ANOVA with Tukey’s multiple-comparison test (A), unpaired t-test (C, E).

Article Snippet: Recombinant human TGF-β2 (302-B2-010/CF) protein was purchased from R&D Systems (Minneapolis, MN).

Techniques: Injection, Immunofluorescence, Staining, Marker, Expressing, Western Blot, Control, Comparison

Journal: bioRxiv

Article Title: Macrophage Migration Inhibitory Factor (MIF)-CD74 Signaling Pathway Mediates Trabecular Meshwork Dysfunction in Glaucoma

doi: 10.64898/2026.03.18.712673

Figure Lengend Snippet: Primary HTMCs (n=3) were challenged with TGF-β2 (10ng/mL), rMIF (100ng/mL), or pro-inflammatory cytokine pool (CP; TNF-α, IL-1β, IL-6, and IL-17 100ng/mL) for 24h. (A) qPCR analysis shows significant upregulation of MIF and CD74 transcripts accompanied by reduced Blimp-1 expression in response to glaucomatous stressors. ( B ) Immunofluorescence staining demonstrates increased MIF expression following TGF-β2 or CP treatment. (C) Western blot analysis confirms induction of MIF and CD74 with concurrent suppression of Blimp-1 at the protein level. Data represent mean ± SD. **p<0.005, ***p<0.0005, and ***p<0.0001, One-way ANOVA with Dunnett’s multiple-comparison test.

Article Snippet: Recombinant human TGF-β2 (302-B2-010/CF) protein was purchased from R&D Systems (Minneapolis, MN).

Techniques: Expressing, Immunofluorescence, Staining, Western Blot, Comparison

Journal: bioRxiv

Article Title: Macrophage Migration Inhibitory Factor (MIF)-CD74 Signaling Pathway Mediates Trabecular Meshwork Dysfunction in Glaucoma

doi: 10.64898/2026.03.18.712673

Figure Lengend Snippet: Primary HTMCs (n=3) were challenged with rMIF (100 ng/mL) in the presence or absence of MIF inhibitor 4-IPP (100µM) or the metabolites Agm or Thia (100 ng/mL) for 24h. Cells treated with TGF-β2 (10ng/mL) served as a positive control. (A-B) Western blot analysis confirms activation of the RhoA/ROCK/pMLC signaling pathway in response to MIF treatment, which is significantly attenuated by MIF inhibition with 4-IPP, Agm, or Thia ( A ). Western blot bands were quantified by densitometric analysis using ImageJ and normalized to the housekeeping control β-actin, and protein levels are presented as relative expression (AU) ( B ). (C) Immunofluorescence analysis shows that MIF induces pMLC staining, comparable to that observed with TGF-β2 stimulation, which is significantly attenuated by MIF inhibition with 4-IPP, Agm, or Thia. Data represent mean ± SD. *p<0.05, **p<0.005, ***p<0.0005, and ****p<0.0001, One-way ANOVA with Dunnett’s multiple-comparison test.

Article Snippet: Recombinant human TGF-β2 (302-B2-010/CF) protein was purchased from R&D Systems (Minneapolis, MN).

Techniques: Positive Control, Western Blot, Activation Assay, Inhibition, Control, Expressing, Immunofluorescence, Staining, Comparison

Journal: bioRxiv

Article Title: Macrophage Migration Inhibitory Factor (MIF)-CD74 Signaling Pathway Mediates Trabecular Meshwork Dysfunction in Glaucoma

doi: 10.64898/2026.03.18.712673

Figure Lengend Snippet: OHT was induced in WT C57BL/6 mice (n=12) by intravitreal injection of LV-TGF-β2. LV-null-injected mcie served as controls. Following OHT induction, extracellular vesicle-loaded agmatine (EV-Agm; 0.1 µg/eye) was applied topically once daily. (A) Weekly IOP measurements over 9 weeks show that EV-Agm treatment significantly reduces IOP compared with untreated LV-TGF-β2-injected mice. (B) qPCR analysis of anterior segment tissue demonstrates that EV-Agm significantly reduces expression of Mif, Cd74, pro-inflammatory cytokines ( Il-1 β , Il-6 ), and cytoskeletal/ECM markers (α -Sma, Myoc, Fn-1 ), while restoring Blimp-1 expression compared with untreated LV-TGF-β2-injected mice. *p<0.05, **p<0.005, ###,***p<0.0005, and ####,****p<0.0001. Two-way ANOVA with Tukey’s multiple comparison (A), one-way ANOVA with Tukey’s multiple comparison (B). In panel A, * denotes LV-null vs. LV-TGF-β2, and # denotes LV-TGF-β2 vs. LV-TGF-β2+EV-Agm comparisons.

Article Snippet: Recombinant human TGF-β2 (302-B2-010/CF) protein was purchased from R&D Systems (Minneapolis, MN).

Techniques: Injection, Expressing, Comparison

Journal: Scientific Reports

Article Title: Cholangiocarcinoma derived exosomes attenuate the anti-tumor functions of NK cells

doi: 10.1038/s41598-026-36706-9

Figure Lengend Snippet: Effect of RBE-Exos on the adhesion of NK-92 cells. ( A ) Growth status of NK-92 cells. NK cells treated with RBE-Exos lost the normal cluster growing. ( B ) CD11a protein levels. ( C ) CD18 protein levels. ( D ) CD54 protein levels. Western blot showed that the protein levels of CD11a, CD18 and, CD54 were obviously decreased in NK-92 cells treated with RBE-Exos. ( E ) Relative transcriptional levels of CD11a , CD18 , CD54 and, CD2 in NK-92 cells. qRT-PCR displayed that RBE-Exos downregulated the transcriptional levels of CD11a , CD18 , CD54 , but not CD2 . Data were presented as mean ± SEM for three independent experiments. * P < 0.05, ** P < 0.01, and *** P < 0.001.

Article Snippet: The primary antibodies were as follows: rabbit anti-human CD63, BCL-2, BCL-XL, CD11a, β-actin (Abcam, USA), mouse anti-human HSP70 (Santa-Cruz, USA), rabbit anti-human CD18 (Proteintech, China), mouse anti-human CD54 (Proteintech, China).

Techniques: Western Blot, Quantitative RT-PCR

Journal: Scientific Reports

Article Title: Cholangiocarcinoma derived exosomes attenuate the anti-tumor functions of NK cells

doi: 10.1038/s41598-026-36706-9

Figure Lengend Snippet: Cytotoxicity and expression of adhesion molecules in primary NK cells. ( A ) Cytotoxicity of primary NK cells from CCA patients and healthy people against target cells. LDH detection displayed the cytotoxicity of NK cells from CCA patients was significantly lower than that of NK cells healthy people. Data are presented as the mean ± SEM from n = 3 independent experiments. ( B ) Protein levels of CD18 in primary NK cells from CCA patients and healthy people. Data are presented as the mean ± SEM from n = 3 independent experiments. ( C ) Protein levels of CD54 in primary NK cells from CCA patients and healthy people. Data are presented as the mean ± SEM from n = 3 independent experiments. ** P < 0.01.

Article Snippet: The primary antibodies were as follows: rabbit anti-human CD63, BCL-2, BCL-XL, CD11a, β-actin (Abcam, USA), mouse anti-human HSP70 (Santa-Cruz, USA), rabbit anti-human CD18 (Proteintech, China), mouse anti-human CD54 (Proteintech, China).

Techniques: Expressing