Journal: PLoS ONE

Article Title: Identification of the ER-resident E3 ubiquitin ligase RNF145 as a novel LXR-regulated gene

doi: 10.1371/journal.pone.0172721

Figure Lengend Snippet: ( A ) Expression of Rnf145 was evaluated in the indicated mouse tissues by qPCR. Bars indicate mean ± SD (n = 3) ( B , C ) The indicated ( B ) human and ( C ) mouse cell lines and primary macrophages were cultured in lipoprotein-depletion medium for 16 hours and subsequently treated for 6 hours with 1μM GW3965 (GW). ( D ) THP1 cells were cultured in sterol depletion medium for 16 hrs and then treated with 1μM GW3965 (GW) and 100nM LG100268 (LG) for 6 hrs as indicated. Subsequently, ABCA1 and RNF145 expression was determined by qPCR and each bar and error represents the mean fold-change of ligand-treated cells over sterol-depleted cells ± SD (n≥3).

Article Snippet: Membranes were probed with the following antibodies: LDLR (Abcam, clone EP1553Y, 1:4000), tubulin (Sigma, clone DM1A, ascites fluid, 1:5000), ABCA1 (Novus Biologicals, NB400-105, 1:1000), FLAG (Sigma, clone M2, 1:1000), GFP (Santa Cruz sc-9996, 1:500), Myc (Santa Cruz 9E10, 1:3000), HA (Covance, clone 16B12, ascites fluid, 1:6000), HMGCR (rabbit polyserum was a kind gift from Dr. Peter Edwards, UCLA), SREBP2 (BD Biosciences, clone 1C6, 1:1000), SREBP1 (ThermoFisher, clone 2A4, 1:1000), actin (Merck Millipore, clone C4, 1:5000), V5 (Invitrogen, 46–0705, 1:3000), RNF145 (Abgent AP18281b, 1:8000), and ubiquitin (Enzo life Sciences, clone FK2, 1:1000).

Techniques: Expressing, Cell Culture

Journal: PLoS ONE

Article Title: Identification of the ER-resident E3 ubiquitin ligase RNF145 as a novel LXR-regulated gene

doi: 10.1371/journal.pone.0172721

Figure Lengend Snippet: ( A ) RAW264.7 macrophages were treated with 5μg/mL Actinomycin D (ActD) for the indicated time and expression of Abca1 and Rnf145 was determined by qPCR and plotted as mean ± SD relative to untreated cells (n = 3), ( B ) HepG2 and RAW264.7 cells were treated with 1μM GW3965 for 6 hours in the presence or absence of 5μg/ml actinomycinD for 4 hours, after which expression of the indicated genes was measured by qPCR. Bars indicate mean ± SD (n = 3) ( C , D ) THP1 macrophages were cultured in sterol-depletion medium for 16 hrs and then treated with ( C ) 1μM GW3965 (GW) for the indicated time, or ( D ) with the indicated concentration of GW3965 for 4 hrs. Subsequently, gene expression was evaluated qPCR and bars indicate mean ± SD (n = 3)

Article Snippet: Membranes were probed with the following antibodies: LDLR (Abcam, clone EP1553Y, 1:4000), tubulin (Sigma, clone DM1A, ascites fluid, 1:5000), ABCA1 (Novus Biologicals, NB400-105, 1:1000), FLAG (Sigma, clone M2, 1:1000), GFP (Santa Cruz sc-9996, 1:500), Myc (Santa Cruz 9E10, 1:3000), HA (Covance, clone 16B12, ascites fluid, 1:6000), HMGCR (rabbit polyserum was a kind gift from Dr. Peter Edwards, UCLA), SREBP2 (BD Biosciences, clone 1C6, 1:1000), SREBP1 (ThermoFisher, clone 2A4, 1:1000), actin (Merck Millipore, clone C4, 1:5000), V5 (Invitrogen, 46–0705, 1:3000), RNF145 (Abgent AP18281b, 1:8000), and ubiquitin (Enzo life Sciences, clone FK2, 1:1000).

Techniques: Expressing, Cell Culture, Concentration Assay, Gene Expression

Journal: PLoS ONE

Article Title: Identification of the ER-resident E3 ubiquitin ligase RNF145 as a novel LXR-regulated gene

doi: 10.1371/journal.pone.0172721

Figure Lengend Snippet: ( A ) LXR ChIP-seq experiments in human THP1 cells (GSE28319) and RAW macrophage-like cells (GSE50944) were analyzed and used to identify active LXREs within the Rnf145/Rnf145 loci, as graphically illustrated. ( B , C ) Genomic location of the identified LXREs. In bold, nucleotides that were mutated to disrupt LXR binding ( C ) A 1kb genomic region upstream of the transcriptional start site of hRNF145 was cloned into a pGL3basic. The putative LXRE was also mutated as indicated above. The empty, RNF145 WT , RNF145 MUT , and ABCA1 reporter plasmids were co-transfected with or without RXRα and LXRα expression plasmids in HEK 293T cells. 24 hours post-transfection the cells were treated with 1μM GW3965 (LXR) and 100nM LG100268 (RXR) for 24 hours and measured for luciferase signal (n≥3). ( D ) Cells were transfected with an empty or a tandem LXRE-containing pGL2 as in C . In all luciferase experiments the transfection efficiency was normalized to co-transfected Renilla luciferase. Bars report normalized chemiluminescence relative to untreated control ± SD (n = 3).

Article Snippet: Membranes were probed with the following antibodies: LDLR (Abcam, clone EP1553Y, 1:4000), tubulin (Sigma, clone DM1A, ascites fluid, 1:5000), ABCA1 (Novus Biologicals, NB400-105, 1:1000), FLAG (Sigma, clone M2, 1:1000), GFP (Santa Cruz sc-9996, 1:500), Myc (Santa Cruz 9E10, 1:3000), HA (Covance, clone 16B12, ascites fluid, 1:6000), HMGCR (rabbit polyserum was a kind gift from Dr. Peter Edwards, UCLA), SREBP2 (BD Biosciences, clone 1C6, 1:1000), SREBP1 (ThermoFisher, clone 2A4, 1:1000), actin (Merck Millipore, clone C4, 1:5000), V5 (Invitrogen, 46–0705, 1:3000), RNF145 (Abgent AP18281b, 1:8000), and ubiquitin (Enzo life Sciences, clone FK2, 1:1000).

Techniques: ChIP-sequencing, Binding Assay, Clone Assay, Transfection, Expressing, Luciferase, Control

Journal:

Article Title: Retinoic Acid Receptor-Mediated Induction of ABCA1 in Macrophages

doi: 10.1128/MCB.23.21.7756-7766.2003

Figure Lengend Snippet: Retinoids induce ABCA1 in macrophages. (A) Retinoids stimulate ABCA1-mediated cholesterol efflux from mouse peritoneal macrophages. The ability of macrophages to efflux cholesterol to apoA-I responds to ATRA treatment in a dose-dependent fashion. The results are expressed as mean ± the standard error of the mean (SEM; n = 4). ✽, P < 0.05; ✽✽, P < 0.01 (compared to control). (B) ATRA and TO-901317 (LXR agonist) induce a comparable increase in cholesterol efflux to apoA-I. The results are expressed as mean ± the SEM (n = 4). (C) Retinoids increase ABCA1 protein accumulation in macrophages. ABCA1 protein levels were analyzed by Western blot in mouse peritoneal macrophages and human monocyte-derived macrophages after ATRA treatment (10 μM for human macrophages) for 24 h in DMEM containing 10% lipoprotein-deficient serum. The fold induction is shown standardized against β-actin. (D) The synthetic RAR pan-agonist, TTNPB, also increases ABCA1 protein accumulation in macrophages.

Article Snippet: Membranes were probed with anti-ABCA1 antibody (Novus Biologicals, Littleton, Colo.) and anti-β-actin antibody (Sigma) according to the manufacturer's recommendations.

Techniques: Western Blot, Derivative Assay

Journal:

Article Title: Retinoic Acid Receptor-Mediated Induction of ABCA1 in Macrophages

doi: 10.1128/MCB.23.21.7756-7766.2003

Figure Lengend Snippet: Induction of macrophages genes by ATRA. (A) Mouse peritoneal macrophages in DMEM containing 10% LPDS were treated for 24 h with various concentrations of ATRA (0.1 to 5 μM) or vehicle (DMSO). (B) Human monocyte-derived macrophages were treated for 24 h with various concentrations of ATRA (0.5 to 5 μM) or vehicle (DMSO). The expression of ABCA1, ABCG1, SREBP-1c, apoE, and LXRα mRNA were measured by quantitative real-time PCR assays (TaqMan) and standardized against β-actin mRNA levels. ✽, P < 0.05; ✽✽, P < 0.01; ✽✽✽, P < 0.001 (compared to control).

Article Snippet: Membranes were probed with anti-ABCA1 antibody (Novus Biologicals, Littleton, Colo.) and anti-β-actin antibody (Sigma) according to the manufacturer's recommendations.

Techniques: Derivative Assay, Expressing, Real-time Polymerase Chain Reaction

Journal:

Article Title: Retinoic Acid Receptor-Mediated Induction of ABCA1 in Macrophages

doi: 10.1128/MCB.23.21.7756-7766.2003

Figure Lengend Snippet: Retinoids do not induce lipogenic SREBP-1c target genes in vivo. (A) RAR regulation of ABCA1 and SREBP-1c expression in mouse peritoneal macrophages. Macrophages were exposed to TTNPB (1 μM) or DMSO (control) for 24 h in 10% LPDS. ABCA1 and SREBP-1c mRNA levels were determined by quantitative real-time reverse transcription-PCR and standardized against β-actin mRNA levels. The results are expressed as mean ± the SEM (n = 4 and 6). ✽, P < 0.05; ✽✽, P < 0.01 (compared to control). (B) Regulation of gene expression by TTNPB in the mouse liver. Mice were injected intraperitoneally with TTNPB (1 or 10 mg/kg) or vehicle (DMSO-polyethylene glycol 300). After 24 h, the mice were anesthetized, the livers were perfused, and the square lobes were removed for isolation of RNA. The expression of SREBP-1c, FAS, ABCA1, and Cyp26 mRNA (positive control for the effect of TTNPB) were measured by quantitative real-time PCR assays (TaqMan) and standardized against β-actin mRNA levels. The results are expressed as mean ± the SEM (n = 5).

Article Snippet: Membranes were probed with anti-ABCA1 antibody (Novus Biologicals, Littleton, Colo.) and anti-β-actin antibody (Sigma) according to the manufacturer's recommendations.

Techniques: In Vivo, Expressing, Reverse Transcription, Injection, Isolation, Positive Control, Real-time Polymerase Chain Reaction

Journal:

Article Title: Retinoic Acid Receptor-Mediated Induction of ABCA1 in Macrophages

doi: 10.1128/MCB.23.21.7756-7766.2003

Figure Lengend Snippet: Human ABCA1 promoter is activated by RXR/RAR. (A) In HEK293 cells, hABCA1 promoter is activated by RARγ. HEK293 cells were transfected with hABCA1 promoter (pb −928 to pb +101) and/or pCMX-hRXRα, pCMX-hRARα, pCMX-hRARβ, and pCMX-hRARγ1 and then exposed to DMSO (control) or 0.1 μM TTNPB in DMEM-lipoprotein-deficient serum-10% penicillin-streptomycin for 36 h before analysis. The luciferase activity was determined as described previously (6). The values are means ± the SEM of three to six independent experiments. ✽, P < 0.05 (Mann-Whitney test). (B) Activation of human ABCA1 promoter by RARγ does not need cotransfection of RXRα. (C) RAR activates hABCA1 promoter through its LXRE DR4 element. HEK 293 cells were transfected with hABCA1 wild-type promoter, a deleted version (bp −100 to bp +101),or the full-length promoter containing mutations in the DR4 element previously described as an LXRE (6). Cells were cotransfected with pCMX-RXRα and pCMX RARγ1 and exposed to 0.1 μM TTNPB for 36 h before luciferase analysis. The values are mean ± the SD of three independent experiments performed in duplicates. (D) RXRα/RARγ1 heterodimer binds hABCA1 DR4 element in EMSAs. In vitro-translated RXRα and RARγ were incubated with 32P-labeled hABCA1 DR4 element. The arrow indicates the resulting complex. Lane 1, wheat germ extract; lane 2, RXRα/RARγ complex on the DR4; lane 3, competition with unlabeled hABCA1 DR4; lanes 4 and 5, asterisks represent a shift of the complex in the presence of RARγ (lane 4) or RXRα (lane 5) polyclonal antibody; lane 6, control anti-RORα antibody; lane 7, competition with mutated unlabeled hABCA1 DR4 (described in Fig. ​Fig.4C,4C, independent experiment). (E) Structure of the mSREBP-1c promoter and position of the two DR4s (LXRE a and b). (F) RXRα/RARγ heterodimer does not interact with the DR4 sequences of the mouse SREBP-1c promoter. (Left panel) RXRα, RARγ, and LXRβ were separately produced by using an in vitro transcription-translation wheat germ extract systems and used in EMSAs with a 32P-labeled mouse SREBP-1c DR4b element as a probe. Lane 1, RXRα/LXRβ binding; lane 2, absence of binding of RXRα/RARγ. (Right panel) EMSA analysis as described in panel D but with a 32P-labeled human ABCA1 DR4 element as a probe. Lane 1, binding of RXRα/RARγ on DR4; lane 2, competition with unlabeled probe; lane 3, competition assay using unlabeled mouse SREBP-1c DR4b element as competitor.

Article Snippet: Membranes were probed with anti-ABCA1 antibody (Novus Biologicals, Littleton, Colo.) and anti-β-actin antibody (Sigma) according to the manufacturer's recommendations.

Techniques: Transfection, Luciferase, Activity Assay, MANN-WHITNEY, Activation Assay, Cotransfection, In Vitro, Incubation, Labeling, Produced, Binding Assay, Competitive Binding Assay

Journal:

Article Title: Retinoic Acid Receptor-Mediated Induction of ABCA1 in Macrophages

doi: 10.1128/MCB.23.21.7756-7766.2003

Figure Lengend Snippet: (A) RARγ tissue distribution in C57BL/6J mouse. Western blot analyses were performed after SDS-polyacrylamide gel electrophoresis separation of 100 μg of the nuclear proteins extracted from each tissue. (B) In vivo association of RARγ/RXR dimer with the DR4 region in the ABCA1 promoter as determined by ChIP analysis. Mouse peritoneal macrophages were treated or not treated (lane 1) with 1 μM ATRA for 24 h and subjected to ChIP assays. Lanes 1 and 5, rabbit anti-RARγ polyclonal antibody used for immunoprecipitation; lane 2, normal rabbit immunoglobulin G used for immunoprecipitation negative control; lane 3, rabbit anti-RARα polyclonal antibody used for immunoprecipitation; lane 4, rabbit anti-RARβ polyclonal antibody used for immunoprecipitation; lane 6, no DNA; lanes 7 to 12, input DNA used for PCR. (C) ABCA1 protein accumulates in TTNPB-treated RARγ−/− mouse peritoneal macrophages. Thioglycolate-elicited peritoneal macrophages from RARγ−/− and RARγ+/+ mice were treated with 5 μM TTNPB for 24 h in DMEM-10% lipoprotein-deficient serum-1% penicillin-streptomycin. The ABCA1 protein levels were then analyzed by Western blot analysis as described for Fig. ​Fig.1C.1C. (D) Upregulation of RARα in RARγ−/− mouse peritoneal macrophages. Nuclear protein extracts isolated from RARγ−/− and RARγ+/+ macrophages were separated by SDS-polyacrylamide gel electrophoresis, and the RARα protein level was determined by Western blot analysis.

Article Snippet: Membranes were probed with anti-ABCA1 antibody (Novus Biologicals, Littleton, Colo.) and anti-β-actin antibody (Sigma) according to the manufacturer's recommendations.

Techniques: Western Blot, Polyacrylamide Gel Electrophoresis, In Vivo, Immunoprecipitation, Negative Control, Isolation

Journal: PloS one

Article Title: Bone marrow deficiency of MCPIP1 results in severe multi-organ inflammation but diminishes atherogenesis in hyperlipidemic mice.

doi: 10.1371/journal.pone.0080089

Figure Lengend Snippet: Figure 9. MCPIP1 deficiency increased macrophage cholesterol efflux. A. Bone marrow-derived macrophages were loaded with ac-LDL and cholesterol efflux to DMEM, apoAI and HDL was measured. Data were presented as mean 6 SEM. N = 3 in each group. B. Bone marrow-derived macrophages were cultured in DMEM for 48 h with or without ac-LDL. Cell lysates were used for western blotting analysis for ABCA1 and ABCG1. Representative western blotting result was shown. C. Quantitative analysis of the western blots. Data were presented as mean 6 SEM. N = 4 in each group. Open column: WT macrophages; Black column, MCPIP12/2 macrophages. doi:10.1371/journal.pone.0080089.g009

Article Snippet: Rabbit antimouse ABCA1 and anti-mouse ABCG1 antibodies were from Novus Biologicals (Littleton, CO).

Techniques: Derivative Assay, Cell Culture, Western Blot

Journal: Frontiers in Immunology

Article Title: Ex vivo expanded human regulatory T cells promote cholesterol efflux and PON1 expression in oxLDL-exposed macrophages via gap junction-mediated cAMP transfer

doi: 10.3389/fimmu.2025.1662925

Figure Lengend Snippet: Treg exp increase ABCA1 expression by transferring cAMP into M IL4 . (A) Changes in the expression of ABCA1 and ABCG1 transcripts in M IL4 co-cultured with either Teffs or Treg exp . Gene expression quantified by qRT-PCR comparing mRNA levels in M IL4 alone (RQ = 1, shown as dashed line) with the same cells co-cultured for 4h with either Teffs or Tregs. UBC was used as reference gene. (B) Intracellular concentration of cAMP in Tregs exp alone, M IL4 alone, or M IL4 co-cultured with Tregs exp for 4h. cAMP levels were normalized to total cellular protein content. Statistical analysis was performed only between M IL4 and M IL4 + Tregs exp , as the aim was to assess whether cAMP levels in M IL4 increase upon co-culture. The cAMP level in Tregs exp is shown as a reference to highlight the high concentration of this molecule in these cells but was not included in the statistical comparison due to the difference in cell type. (C) Changes in the expression of ABCA1 mRNA in M IL4 co-cultured with Treg exp (ratio 1:1) after 1h preincubation or not with GAP27 (300 µM). (D) Changes in the expression of ABCA1 mRNA in M IL4 co-cultured with Tregs (ratio 1:1) after 1h preincubation or not with PKA inhibitor H89 (5 µM). (E) Western blot analysis of ABCA1 protein level in cell lysates of M IL4 alone or M IL4 co-cultured (ratio 1:1) with either Treg exp or Teff for 4h. Data were plotted as ABCA1 protein intensity normalised to GAPDH protein intensity. Statistical analysis was performed using one-way ANOVA followed by Tukey’s multiple comparison test. *p<0.05, **p<0.01.

Article Snippet: Equal amounts of total protein were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), transferred to polyvinylidene difluoride (PVDF) membrane and probed overnight at 4C with the respective antibodies: monoclonal anti-ABCA1 antibody (CellSignaling; Cat Number 96292), polyclonal anti-PON1 antibody (Proteintech; Cat Number 18155-1-AP), monoclonal anti-GAPDH antibody (CellSignaling; Cat Number 5174), recombinant monoclonal anti-ABCA1 (phosho-S2054) antibody (Abcam; Cat Number ab125064).

Techniques: Expressing, Transferring, Cell Culture, Gene Expression, Quantitative RT-PCR, Concentration Assay, Co-Culture Assay, Comparison, Western Blot

Journal: Cellular and Molecular Life Sciences: CMLS

Article Title: Dysregulated cholesterol uptake and efflux of bone marrow-derived α-SMA + macrophages contribute to atherosclerotic plaque formation

doi: 10.1007/s00018-025-05655-3

Figure Lengend Snippet: α-SMA promotes the lipid uptake and inhibits lipid efflux in macrophages. A , B Flow cytometric analysis of binding and uptake of DiI-Ox-LDL in vector- or Acta2 hi RAW264.7 cells A , and BMDMs from Acta2 f/f or Acta2 MKO mice B . The quantification results are shown on the right. n = 3. * P < 0.05, *** P < 0.001, **** P < 0.0001 by unpaired Student’s t-test. C , D SR-A, ABCA1, ABCG1 and α-SMA protein levels in vector- and Acta2 hi RAW264.7 cells C , and BMDMs from Acta2 Flox or Acta2 MKO mice D . n = 3. * P < 0.05 by unpaired Student’s t-test. E–F Co-staining and quantification of SR-A + MOMA-2 + E or ABCA1 + MOMA-2 + F cells in aortic roots from Acta2 f/f or Acta2 MKO mice treated with AAV -PCSK9 DY followed by a 12-week HFD. n = 7. * P < 0.05 by unpaired Student’s t-test. G–H Flow cytometric analysis of binding G and uptake H of DiI-Ox-LDL in Acta2 hi RAW264.7 cells treated with an SR-A blocking antibody (20 μg/mL) or IgG control for 2 h were detected by flow cytometry. n = 3. * P < 0.05 by unpaired Student’s t-test. AAV, adeno-associated virus; HFD, high-fat diet

Article Snippet: Primary antibodies used included mouse anti-mouse α-SMA (BM0002, Boster, USA), goat anti-mouse SR-A (af1797, R&D, USA), rabbit anti-mouse ABCA1 (PB0490, Boster, USA), human anti-mouse ABCG1 (bs-23382R, Bioss, China), rabbit anti-human CD36 (ab133625, Abcam, USA), mouse GAPDH (AF0006, Beyotime, China), rabbit anti-mouse p-Smad3 (AF1759, Beyotime, China), and rabbit anti-mammalian Smad3 (sc-101154, SANTA CRUZ, USA).

Techniques: Binding Assay, Plasmid Preparation, Staining, Blocking Assay, Control, Flow Cytometry, Virus

Journal: Cellular and Molecular Life Sciences: CMLS

Article Title: Dysregulated cholesterol uptake and efflux of bone marrow-derived α-SMA + macrophages contribute to atherosclerotic plaque formation

doi: 10.1007/s00018-025-05655-3

Figure Lengend Snippet: AKT pathway is involved in α-SMA-induced lipid accumulation. A Abca1 mRNA levels in vector or Acta2 hi RAW264.7 cells treated with 50 μg/ml Ox-LDL for 0, 6, 12, or 24 h. n = 3. * P < 0.05 by unpaired Student’s t-test. B Top 15 KEGG pathways of genes downregulated in Acta2 hi RAW264.7 cells incubated with Ox-LDL for 6 h. C Protein levels of p-AKT, AKT, p-ERK, ERK, p-STAT3, STAT3, CD36, SR-A, ABCA1 and α-SMA treated with 50 μg/ml Ox-LDL for 6 h. n = 3. * P < 0.05 by one-way ANOVA. D – F Flow cytometric analysis of binding ( D and E ) and uptake ( D and F ) of DiI-Ox-LDL in vector or Acta2 hi RAW264.7 cells incubated with or without SC79 (2 μg/mL). n = 3. * P < 0.05, ** P < 0.01, **** P < 0.0001 by one-way ANOVA. G – I Protein levels of CD36, SR-A, ABCA1 and α-SMA in Acta2 hi or vector RAW264.7 cells incubated with or without SC79 (2 μg/mL) and treated with 50 μg/ml Ox-LDL for 2 h. n = 3. * P < 0.05, ** P < 0.01, **** P < 0.0001 by one-way ANOVA

Article Snippet: Primary antibodies used included mouse anti-mouse α-SMA (BM0002, Boster, USA), goat anti-mouse SR-A (af1797, R&D, USA), rabbit anti-mouse ABCA1 (PB0490, Boster, USA), human anti-mouse ABCG1 (bs-23382R, Bioss, China), rabbit anti-human CD36 (ab133625, Abcam, USA), mouse GAPDH (AF0006, Beyotime, China), rabbit anti-mouse p-Smad3 (AF1759, Beyotime, China), and rabbit anti-mammalian Smad3 (sc-101154, SANTA CRUZ, USA).

Techniques: Plasmid Preparation, Incubation, Binding Assay

Journal: Cellular and Molecular Life Sciences: CMLS

Article Title: Dysregulated cholesterol uptake and efflux of bone marrow-derived α-SMA + macrophages contribute to atherosclerotic plaque formation

doi: 10.1007/s00018-025-05655-3

Figure Lengend Snippet: Schematic diagram illustrating the role of bone marrow-derived α-SMA + macrophages in atherosclerotic plaque formation. Macrophage-expressed α-SMA enhances SR-A expression via the AKT signaling pathway, leading to increased lipid binding and uptake. Concurrently, α-SMA suppresses ABCA1 expression, thereby reducing lipid efflux. This imbalance promotes lipid accumulation and contributes to atherosclerotic plaque formation

Article Snippet: Primary antibodies used included mouse anti-mouse α-SMA (BM0002, Boster, USA), goat anti-mouse SR-A (af1797, R&D, USA), rabbit anti-mouse ABCA1 (PB0490, Boster, USA), human anti-mouse ABCG1 (bs-23382R, Bioss, China), rabbit anti-human CD36 (ab133625, Abcam, USA), mouse GAPDH (AF0006, Beyotime, China), rabbit anti-mouse p-Smad3 (AF1759, Beyotime, China), and rabbit anti-mammalian Smad3 (sc-101154, SANTA CRUZ, USA).

Techniques: Derivative Assay, Expressing, Binding Assay

Journal: Molecular medicine reports

Article Title: Effect of triptolide on the regulation of ATP‑binding cassette transporter A1 expression in lipopolysaccharide‑induced acute lung injury of rats.

doi: 10.3892/mmr.2014.2636

Figure Lengend Snippet: Figure 5. ABCA1 protein expression in lung tissue. *P<0.05 compared with the N and C groups. ΔP<0.05 compared with the L group. N, normal group; C, control group; L, LPS‑treated group; TP1‑3, triptolide‑treated group at 25, 50 or 100 µg/kg respectively; ABCA1, ATP‑binding cassette transporter A1.

Article Snippet: ABCA1 monoclonal antibody (article no. p3490RB) was purchased from R&D Systems (Minneapolis, MN, USA), GAPDH antibody (article no. sz‐293072) was obtained from Santa Cruz Biotechnology, Inc., (Santa Cruz, CA, USA) and rabbit anti-mouse immunoglobulin G (IgG) (article no. KTB4027) was purchased from Shanghai Boyao Biological Technology Co., Ltd., (Shanghai, China).

Techniques: Expressing, Control

Journal: Molecular medicine reports

Article Title: Effect of triptolide on the regulation of ATP‑binding cassette transporter A1 expression in lipopolysaccharide‑induced acute lung injury of rats.

doi: 10.3892/mmr.2014.2636

Figure Lengend Snippet: Figure 4. Changes in ABCA1 mRNA expression in the lung tissue of rats in all groups. *P<0.05 compared with the N and C groups. ΔP<0.05 compared with the L group. N, normal group; C, control group; L, LPS‑treated group; TP1‑3, triptolide treated group at 25, 50 or 100 µg/kg, respectively; ABCA1, ATP‑binding cassette transporter A1.

Article Snippet: ABCA1 monoclonal antibody (article no. p3490RB) was purchased from R&D Systems (Minneapolis, MN, USA), GAPDH antibody (article no. sz‐293072) was obtained from Santa Cruz Biotechnology, Inc., (Santa Cruz, CA, USA) and rabbit anti-mouse immunoglobulin G (IgG) (article no. KTB4027) was purchased from Shanghai Boyao Biological Technology Co., Ltd., (Shanghai, China).

Techniques: Expressing, Control