Journal: Cancer research

Article Title: HACE1 prevents lung carcinogenesis via inhibition of RAC-family GTPases

doi: 10.1158/0008-5472.CAN-19-2270

Figure Lengend Snippet: (A) Amino acid (aa) sequence alignments of murine RAC1, RAC2, and RAC3. Amino acids highlighted in red indicate differences among the family members. The amino acid positions are indicted. (B) Relative mRNA expression of Rac1, Rac2 and Rac3 normalized to β-Actin expression in primary lung tumor cells, isolated from KRasG12D;Hace1+/+Rac1+/+Rac2+/+ mice (n=5) at week 7 post lung cancer induction, followed by RT-qPCR analysis. (C) In vitro ubiquitylation assay. Recombinant GST-HACE1 was incubated with GTP- or GDP-preloaded His-tagged RAC1 or RAC2 in the presence of E1, E2 (Ubch7), ubiquitin and ATP. As a control, catalytic dead HACE1C876S was used. Blots show RAC1 and RAC2 (detected via the His-tag), HACE1 and ubiquitin after 3 h incubation. Ubiquitylated RAC1 and RAC2 are indicated (white arrows). (D) Kaplan-Meier survival curves of KRasG12D;Hace1+/+Rac1+/+Rac2+/+ (n=23), KRasG12D;Hace1–/– (n=15), KRasG12D;Rac1fl/fl (n=25), KRasG12D;Hace1–/–Rac1fl/fl (n=19), KRasG12D;Rac2–/– (n=23) and KRasG12D;Hace1–/–Rac2–/– (n=7), KRasG12D;Rac1fl/flRac2–/– (n=19) and KRasG12D;Hace1–/–Rac1fl/flRac2–/– (n=20) mice. Mice were intratracheally instilled with Adeno-Cre virus on the indicated day 0. * P<0.05, ** P<0.01, *** P<0.001, **** P<0.0001 (log-rank test). (E) Representative H&E stained-lung sections and (F) tumor-to-lung ratios at week 18 post lung cancer induction for KRasG12D;Hace1+/+Rac1+/+Rac2+/+, KRasG12D;Rac1fl/fl, KRasG12D;Hace1–/–Rac1fl/fl, KRasG12D;Rac1fl/flRac2–/– and KRasG12D;Hace1–/–Rac1fl/flRac2–/– mice. Scale bars, 1 mm for 10x images and 50μm for 40x images of lung sections. * P<0.05, ** P<0.01 (One-way ANOVA, Tukey’s post-hoc test, n≥5 mice per cohort). Data in (B) and (F) are presented as mean values ± SEM.

Article Snippet: In vitro ubiquitylation assay His-tagged recombinant human RAC1 (Cytoskeleton, RC01) and RAC2 (Cytoskeleton, RC02) were preloaded with GTP or GDP as described ( 41 ).

Techniques: Sequencing, Expressing, Isolation, Quantitative RT-PCR, In Vitro, Ubiquitin Assay, Recombinant, Incubation, Ubiquitin Proteomics, Control, Virus, Staining

Journal: Cancer research

Article Title: HACE1 prevents lung carcinogenesis via inhibition of RAC-family GTPases

doi: 10.1158/0008-5472.CAN-19-2270

Figure Lengend Snippet: (A) Kaplan-Meier curves of overall survival and (B) disease-free survival for lung adenocarcinoma patients, based on HACE1 and RAC1 mRNA expression. (C) Kaplan-Meier curves of overall survival and (D) disease-free survival for lung adenocarcinoma patients, based on HACE1, RAC1 and RAC2 mRNA expression. (E) Schematic representation of genetic alterations in HACE1, RAC1, RAC2 and RAC3 in lung adenocarcinoma patients from the TCGA (PanCancer Atlas) data set for 507 cases. Color coding indicates mutation types: red, amplification; blue, homozygous deletion; yellow, missense mutation; black, truncating mutation. Percentages (%) of cases with alteration in HACE1, RAC1, RAC2 and RAC3 are indicated. Only altered cases are shown. (F) Heatmap of gene expression profiles of HACE1, RAC1, RAC2 and RAC3 in lung adenocarcinoma patients. Each row represents the expression of either HACE1, RAC1, RAC2 or RAC3. Each line corresponds to one lung cancer patient. Z-score (RNA Seq V2 RSEM) is shown from 10 (red, highest expression) to -2 (blue, lowest expression). The mRNA expression level in a single sample is depicted according to the color scale. (G) Correlation matrix showing Spearman’s rank correlation of HACE1, RAC1, RAC2 and RAC3 mRNA expression profiles. Correlation coefficients are shown in white and the associated p-values in black (statistically significant values with P<0.05 in bold). Orange and blue colors indicate positive and negative correlations, respectively, beige indicates no correlation.

Article Snippet: In vitro ubiquitylation assay His-tagged recombinant human RAC1 (Cytoskeleton, RC01) and RAC2 (Cytoskeleton, RC02) were preloaded with GTP or GDP as described ( 41 ).

Techniques: Expressing, Mutagenesis, Amplification, Gene Expression, RNA Sequencing

Journal: Cancer research

Article Title: HACE1 prevents lung carcinogenesis via inhibition of RAC-family GTPases

doi: 10.1158/0008-5472.CAN-19-2270

Figure Lengend Snippet: HACE1 ubiquitylates GTP-RAC1 when bound to the NADPH oxidase complex, leading to RAC1 degradation and thereby controlling ROS production (top, left). HACE1 deficiency results in an accumulation of GTP-bound RAC1, increased NADPH oxidase activity and enhanced levels of genotoxic cellular ROS, promoting cancer progression (top, right). Additionally, deregulated RAC1 could promote tumor development by ROS-independent mechanisms. In the absence of the more abundant RAC1, the activity of GTP-RAC2 when bound to the NADPH oxidase complex is controlled by HACE1, leading to decreased cellular ROS levels (bottom, left). When HACE1 and RAC1 are both ablated, active GTP-RAC2 can compensate and promote cancer progression (bottom, right).

Article Snippet: In vitro ubiquitylation assay His-tagged recombinant human RAC1 (Cytoskeleton, RC01) and RAC2 (Cytoskeleton, RC02) were preloaded with GTP or GDP as described ( 41 ).

Techniques: Activity Assay

Journal: bioRxiv

Article Title: PI3Kδ Bridges Microbial Surveillance with Antigen Presentation to Reinforce Intestinal Immunity

doi: 10.1101/2025.05.13.653657

Figure Lengend Snippet: ( a ) GTP-loaded RAC1/2/3 in WT, δD910A, or Nod2 - /- BM-DCs assessed by Rac G-LISA after stimulation with MDP (30 µg/ml) ( left panel) or LPS (100 ng/ml) ( right panel) (n=4-7 per group). ( b ) Representative immunoblots ( left panel) and bar chart ( right panel) showing GTP-loaded RAC2 in pulldown complexes and RAC2 in TCL from MDP-stimulated WT and δD910A BM-DCs at indicated time points. GAPDH was used to verify equal loading (n=3). ( c ) Representative immunoblots ( top and bottom, left panels) and fold change ( top and bottom , right panels) of p-AKT Ser473 levels in WT and RAC2-/- BM-DCs stimulated with MDP (30 µg/ml) or LPS (100 ng/ml) at indicated times. Middle , left, and right panels show WT BM-DCs pretreated for 2 h with EHT1864 (0.5 µM) or Veh (DMSO) before MDP stimulation (n=2-3 per group). ( d ) Representative immunoblots ( left panels) showing phagosome-associated RAC2, PI3Kδ, and NOX2 components (gp91 phox , p67 phox , p47 phox ) in WT or δD910A BM-DCs that phagocytosed 3 µM beads, coated with MDP or LPS, or left uncoated at 30 min. Phagosome-associated RAC2-GTP (magenta rectangle) was pulldown with PAK-CRIB beads from BM-DC phagosome extracts of indicated genotypes, with total RAC2 and PI3Kδ in TCL is shown (black rectangle). Ratios of active RAC2 in phagosomes ( right , upper panel) or total RAC2 ( right , lower panel) are shown (n=3). ( e ) Representative immunoblots showing recombinant His-tagged p110β and p110δ binding to recombinant GTPγS-loaded His-tagged RAC2 in a cell-free system, following immunoprecipitation of complexes using Abs directed against p110α, p110β, or p110δ. GDP-loaded His-tagged RAC2 was used as a control. Immunoblots of complexes were probed using anti-His mAb. Total recombinant protein loading visualized using anti-His mAb. One representative experiment is shown (n=2). ( f ) OT-II T-cell division after co-culture with WT or δD910A BMDCs, pretreated with RAC inhibitor (EHT-1864, 0.5 µM) or Veh (DMSO) before preloading with OVA-coated beads in the presence of LPS for 5 h (n=3 per group). ( g ) Proportions of Foxp3 + and IFN-γ + OT-II T cells after restimulation with PMA and ionomycin. Results are expressed as means ± SEM. Statistical analysis by one-way or two-way ANOVA with Tukey’s post hoc test, with p values considered * p <0.05, ** p <0.01, *** p <0.001, and **** p <0.0001.

Article Snippet: 5 × 10 5 NIH-3T3 cells were transfected with 2 ug of Flag Rac2 in pcDNA3 (Plasmid #12192, Addgene) together with 2 µg Myc-tagged p110δ-WT or Myc-tagged p110δ-CAAX plasmids or empty vector pMX using jetPRIME ® (Polyplus).

Techniques: Western Blot, Recombinant, Binding Assay, Immunoprecipitation, Control, Co-Culture Assay

Journal: RSC advances

Article Title: Bio-fabrication of pigment-capped silver nanoparticles encountering antibiotic-resistant strains and their cytotoxic effect towards human epidermoid larynx carcinoma (HEp-2) cells.

doi: 10.1039/c9ra01072f

Figure Lengend Snippet: Fig. 11 Apoptotic mechanism of HEp-2 cells treated with pcAgNPs. DNA fragmentation of HEp-2 cells exposed to pcAgNPs (a). RT-PCR analysis of p53 expression, leading to apoptotic cell death (b and c); pcAgNP activation of p53, leading to increased catalase expression. HEp-2 cells treated with 15 mg mL1 pcAgNPs for 24 h, showing p53, p21 and catalase expressions assessed using Western blotting analysis. b-actin served as a loading control. Numbers were calculated by quantitative densitometric analysis and indicate the ratio of specific proteins versus b-actin. (d) Data are representative of at least three independent experiments.

Article Snippet: In the western blotting analysis, the following primary antibodies were used: rabbit polyclonal anti-p21 (1 : 100) (cat. no. TA322940, OriGene, USA), mouse monoclonal anti-p53 (1 : 500) (cat. no. TA327920, OriGene, USA), andmouse monoclonal anticatalase (1 : 100) (cat. no. TA502496, OriGene, USA).

Techniques: Reverse Transcription Polymerase Chain Reaction, Expressing, Activation Assay, Western Blot, Control

Journal: PLoS ONE

Article Title: Rac2 Controls Tumor Growth, Metastasis and M1-M2 Macrophage Differentiation In Vivo

doi: 10.1371/journal.pone.0095893

Figure Lengend Snippet: (A & B) WT and Rac2-/- mice (n = 8-10) were subcutaneously implanted with 1×10 5 LLC, B16F10 and 2×10 6 NB9464D cells on the dorsal flank. Tumor growth was monitored regularly, until tumors were harvested on day 21. Mean tumor volume (A) and mass (B) for each group (n = 8) is plotted. Graphs present mean ± SEM of 8 mice in each group. Statistical significance is assessed by two sample t -test where *denotes P <0.05, ** denotes P <0.01 and *** denotes P <0.001. Experiment was repeated 7–8 times with similar results. (C) Left panel shows representative immunofluorescent staining of tumor vasculature by CD31 (green) and counterstain by DAPI (blue) on frozen tumor sections of LLC and B16 tumors implanted subcutaneously in WT and Rac2-/- mice. Right panel shows reduced microvascular density (MVD) in tumors isolated from Rac2-/- animals as compared to WT animals. MVD was determined by counting the number of microvessels per high-power field (HPF) in the section with an antibody reactive to CD31. Microvessels were counted blindly in 5–10 randomly chosen fields and data is representative of three independent experiments with 4–5 mice. * P <0.05 vs. WT. (D) H & E stained images (magnification 4X and 20X) showing invasive interface between the skin and muscularis layer of subcutaneous implanted LLC tumor into WT and Rac2-/- animals. The invasive interface is shown by arrows. Same results were obtained with 7–8 mice in each group and experiment is repeated 7–8 times.

Article Snippet: Rac2 antibody is from Novus Biologicals.

Techniques: Staining, Isolation

Journal: PLoS ONE

Article Title: Rac2 Controls Tumor Growth, Metastasis and M1-M2 Macrophage Differentiation In Vivo

doi: 10.1371/journal.pone.0095893

Figure Lengend Snippet: (A) Experimental metastasis of B16 melanoma cells in WT and Rac2-/- mice (n = 5). B16 F10 melanoma cells (5×10 5 cells) were injected through the tail vein, and after 15 days, the lungs were removed and the photographs were taken shown as upper panel in the figure. Lower panel shows mean number of tumor nodules visible on the surface of the lungs in WT and Rac2-/- mice. Surface tumor nodules in lungs were counted under dissecting microscope. Values are mean ± SEM ( n = 5 or 6; P <0.001; pair wise two-sided Student's t test). A marked suppression in the number of metastatic nodules was observed in Rac2-/- mice.(B) H&E-stained lung tissues demonstrating large macroscopic nodules (black arrows) were greatly increased in number and size in the WT vs. Rac2-/- mice, 15 d after B16 tumor cell injection. (C) Upper panel shows tumor mass of pancreatic tumors implanted orthotopically in WT and Rac2-/- mice. Panc02 (1×10 6 ) cells were injected in the pancreas of WT and Rac2-/- mice (n = 10). Tumors were removed 30 days after tumor implantation. Values are mean ± SEM ( n = 10; P<0.05; pair wise two-sided Student's t test). Bottom panel shows representative images of pancreatic tumors isolated from pancreas of WT and Rac2-/- mice. (D) Left panel shows macroscopic view of Panc02 metastatic mesenteric lymph nodes from WT and Rac2-/- mice. Right panel shows number of metastatic mesenteric lymph nodes/mesentery. Values are mean ± SEM ( n = 5 or 6; P<0.001; pair wise two-sided Student's t test). The data are representative of three independent experiments performed.

Article Snippet: Rac2 antibody is from Novus Biologicals.

Techniques: Injection, Microscopy, Staining, Tumor Implantation, Isolation

Journal: PLoS ONE

Article Title: Rac2 Controls Tumor Growth, Metastasis and M1-M2 Macrophage Differentiation In Vivo

doi: 10.1371/journal.pone.0095893

Figure Lengend Snippet: (A) Left panel shows BMDMs from WT, and Rac2-/- mice were tested in haptotaxis assay for capacity to migrate on different matrix proteins or fragments of fibronectin, vitronectin (via α v β 3 /α v β 5 ); H296, via α 4 β 1 ; CH271, via α 5 β 1 and collagen via α 2 β 1 /α 2 β 2 . Comparison of WT to Rac2-/- BMDMs shows significant difference on H296 peptide ( P <0.001), CH271 peptide ( P <0.05), VN protein ( P <0.01). Data represent mean ± SEM, representative of 4 independent experiments performed (n = 3). Right Upper panel shows Rac2 pull down assay indicating the extent of Rac2 activation in WT BMDMs under conditions of adhesion to: NS, no stimulation; Vitronectin (α v β 3 /α v β 5 ); H296, fibronectin fragment for α 4 β 1 ; CH271, fibronectin fragment for α 5 β 1 ; and Collagen (α 2 β 1 /α 2 β 2 ). Conversion of GDP-Rac2/Rac1 to GTP-Rac2/Rac1 was determined by using GST fusion protein representing the GTP-Rac-binding CRIB domain of the PAK-1 kinase. Cell lysate used in this comparison contained equal amounts of protein per lane. Total Rac1 and Rac2 protein was loaded for control. Right Lower panel shows Rac2 pull down assay indicating the extent of Rac2 activation in WT and α4Y991A knock in BMDMs under conditions of adhesion to H296, fibronectin fragment for α 4 β 1. Experiments were repeated 2-3 times with similar results. (B) LLC cells were inoculated subcutaneously in WT and α4Y991A mice (n = 6–8) and tumor growth was recorded as described in . Values represent mean ± SEM ( n = 6–8 mice per group; P<0.001) (C) Quantitative PCR analysis of mRNA for M1, M2 specific genes in the macrophages sorted from LLC tumors grown in WT and α4Y991A mice (n = 3–4). LLC tumors implanted in WT and α4Y991A mice were used for FACS sorting of macrophages on the basis of F4/80 and CD11b staining as described in . RNA was isolated from these macrophages and was used for real-time PCR analysis of the indicated genes described in . Values are mean ± SEM ( n = 3–4). Statistical significance is assessed by two sample t -test where *denotes P <0.05, ** denotes P <0.01 and *** denotes P <0.001.). (D) Left panel shows representative photograph of pulmonary metastatic foci produced 15 days after intravenous injection of B16F10 cells in WT and α4Y991A mice (n = 6–8). Right panel shows mean number of tumor nodules visible on the surface of the lungs in WT and α4Y991A mice. Values are mean ± SEM (n = 6; P<0.001; pair wise two-sided Student's t test). (E), Quantitative PCR analysis of mRNA for IL 1, uPA, TNFα, MMP9, Mgl1, MMR, YM1 and TGF-β in BMDMs isolated from WT and α4Y991A knock in mice and cultured in MCSF in vitro . Data are representative of three independent experiments, shown are mean ± SEM, *P<0.05, **P<0.01 and ***P<0.001 vs. WT, t test.

Article Snippet: Rac2 antibody is from Novus Biologicals.

Techniques: Comparison, Pull Down Assay, Activation Assay, Binding Assay, Control, Knock-In, Real-time Polymerase Chain Reaction, Staining, Isolation, Produced, Injection, Cell Culture, In Vitro

Journal: PLoS ONE

Article Title: Rac2 Controls Tumor Growth, Metastasis and M1-M2 Macrophage Differentiation In Vivo

doi: 10.1371/journal.pone.0095893

Figure Lengend Snippet: (A) Identification of F4/80 + macrophages by immunofluorescence microscopy in the frozen sections of LLC and B16 tumors stained with antibodies against F4/80 and imaged by fluorescence microscopy. The average no. of macrophages per HPF for 3 different experiments were 42±8, (WT) 38±6 (Rac2-/-) for LLC tumors and 50±5, (WT) 45±10, (Rac2-/-) for B16 tumors. Macrophages were counted blindly by 3 individuals in 5-10 randomly chosen fields and data is representative of three independent experiments with 4 mice. (B) Figure represents FACS data showing the quantification of CD11b and F480 + macrophages infiltrated in LLC tumors implanted in WT and Rac2-/- mice. Experiment was repeated 4-5 times with 3-4 mice in each group and similar results were obtained. (C) Quantitative PCR analysis of mRNA for M1, M2 specific genes in the macrophages sorted from LLC tumors grown in WT and Rac2-/- mice (n = 3–4) as described in . Values are mean ± SEM. Statistical significance is assessed by two sample t -test where *denotes P <0.05, ** denotes P <0.01 and *** denotes P <0.001. (D) Arginase activity was measured in macrophages sorted from LLC tumors injected in WT and Rac2-/- mice as described in . (E) Nitrite production in macrophages sorted from LLC tumors injected in WT and Rac2-/- and stimulated with 10 ng/ml LPS for 24 h. Supernatants were collected, and nitrite concentration was measured as described in . Results are mean ± SEM (n = 3–4 mice) for 3 independent experiments performed in triplicate (P<0.05 for arginase activity and P <0.001 for nitrite assay; student's t test).

Article Snippet: Rac2 antibody is from Novus Biologicals.

Techniques: Immunofluorescence, Microscopy, Staining, Fluorescence, Real-time Polymerase Chain Reaction, Activity Assay, Injection, Concentration Assay, Nitration

Journal: PLoS ONE

Article Title: Rac2 Controls Tumor Growth, Metastasis and M1-M2 Macrophage Differentiation In Vivo

doi: 10.1371/journal.pone.0095893

Figure Lengend Snippet: (A) Quantitative PCR analysis of mRNA for IL 1, uPA, TNFα, MMP9, Mgl1, MMR, YM1 and TGF-β in BMDMs isolated from WT and Rac2-/- mice and cultured in MCSF in vitro . Values are mean ± SEM (n = 3-4 mice). Statistical significance is assessed by two sample t -test where *denotes P <0.05, ** denotes P <0.01 and *** denotes P <0.001. (B) & (C), Heat map generated from microarray analysis of BMDMs isolated from WT and Rac2-/- mice (n = 5 in each group) as described in Materials and Methods. Colors illustrate fold changes, Red: up-regulation; green: down- regulation; black: no change. The bar code on the bottom represents the color scale of the log 2 values. The differential expression of genes related to cell cycle, angiogenesis and invasion are shown in B and M1-M2 polarization are shown in (C). (D) & (E), Heatmap representation of metabolites across BMDMs from WT (n = 5) and Rac2-/- (n = 5) mice. Shades of yellow represent elevation of a metabolite and shades of blue represent decrease of a metabolite relative to the median metabolite levels (see color scale). Colors illustrate fold changes, Yellow: up-regulation; blue: down-regulation; black: no change. Data shows higher expression of metabolites related to carbohydrate (D) and lipid metabolism (E) in Rac2-/- BMDMs.

Article Snippet: Rac2 antibody is from Novus Biologicals.

Techniques: Real-time Polymerase Chain Reaction, Isolation, Cell Culture, In Vitro, Generated, Microarray, Quantitative Proteomics, Expressing

Journal: PLoS ONE

Article Title: Rac2 Controls Tumor Growth, Metastasis and M1-M2 Macrophage Differentiation In Vivo

doi: 10.1371/journal.pone.0095893

Figure Lengend Snippet: (A) Upper panel shows that MCSF signaling differentially activates Rac2 while GMCSF signaling does not result in significant Rac2 activation. BMDMs or GBMDMs cultured in MCSF or GMCSF for 7 days were serum starved for 4 hrs and stimulated with 50 ng/ml of MCSF or GMCSF for 15 min followed by Rac2 GTP pull down assays as described in . Lower panel shows the differential activation of Rac2 when Mθs are costimulated through the MCSFR and α 4 β 1 integrin. WT BMDMs cultured in MCSF for 7 days were serum starved for 4 hrs, trypsinized and were allowed to engage with α 4 β 1 ligand (H296) or α 2 β 1 ligand (collagen), followed by MCSF stimulation (50 ng/ml) for 15 min and Rac2 GTP pull down assay as described before. (B & C) Tumor volume (B) and mass (C) of LLC tumors grown in Rac2-/- mice treated with or without 1 million WT BMDMs or Rac2-/- BMDMs or WT GBMDMs. After 5 days of LLC tumor inoculation, Rac2-/- mice were treated either with 1 million WT BMDMs or GBMDMs or Rac2-/- BMDMs or every third day, until tumors were removed on day 21. Values are mean ± SEM ( n = 6-8). Statistical significance is assessed by two sample t -test where *denotes P <0.05, ** denotes P <0.01 and *** denotes P <0.001. Experiment was repeated three times with similar results. (D) Reversal of B16 metastasis by injection of WT BMDMs and not by WT GBMDMs in Rac2-/- mice. Figure shows representative photograph of pulmonary metastatic foci produced 15 days after intravenous injection of B16F10 cells in Rac2-/- mice and treated with 1 million WT BMDMs or WT GBMDMs. One dose of 1 million BMDMs or GBMDMs were given to Rac2-/- mice two days before inoculating 5×10 5 B16F10 cells intravenously followed by treatment with 1 million BMDM or GBMDM every third day, lungs were harvested on day 15. Data are representative of three independent experiments with 6–8 mice in each group. (E) Reversal of metastatic defect in Rac2-/- mice by local injections of 1 million WT BMDMs in the right lobe of lungs and 1 million WT GBMDMs or Rac2-/- BMDMs in the left lobe of Rac2-/- mice, followed by tail vein injections of B16 luciferase cells (5×10 5 ) after 2 days. The luciferase signal was monitored every third day on IVIS by injecting luciferin, until lungs were harvested on day 15 (n = 5). Data are representative of two independent experiments with 5–6 mice in each group.

Article Snippet: Rac2 antibody is from Novus Biologicals.

Techniques: Activation Assay, Cell Culture, Pull Down Assay, Injection, Produced, Luciferase

Journal: PLoS ONE

Article Title: Rac2 Controls Tumor Growth, Metastasis and M1-M2 Macrophage Differentiation In Vivo

doi: 10.1371/journal.pone.0095893

Figure Lengend Snippet: (A) Graphic representation of novel integrin-Rac2 signaling axis in macrophages required for tumor growth, invasion, metastasis and the polarization of macrophages into M2 phenotype. (B) Interactome map developed from multiple-omic data which predicts how Rac2 regulates macrophage M2 differentiation. Nodes indicate genes either preselected for hierarchical analysis (colored borderer) or prioritized directly by the network propagation algorithm. Edges indicate protein-protein interactions. Node color indicates the protein or gene expression change in the Rac2-/- vs. WT condition.

Article Snippet: Rac2 antibody is from Novus Biologicals.

Techniques: Protein-Protein interactions, Gene Expression