Review

rantes receptor antagonist met-rantes (Serono)

About

News

Press Release

Team

Advisors

Partners

Contact

Bioz Stars

Bioz vStars

Buy from Supplier

Structured Review

Serono rantes receptor antagonist met-rantes
Rantes Receptor Antagonist Met Rantes, supplied by Serono, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/receptor+antagonist+met-rantes/rantes+receptor+antagonist+met+rantes/10__1096_slash_fj__201500088r-41-13-21
Average 90 stars, based on 1 article reviews

rantes receptor antagonist met-rantes - by Bioz Stars, 2026-09

90/100 stars

Images

other:

Article Title: Met-RANTES reduces endothelial progenitor cell homing to activated (glomerular) endothelium in vitro and in vivo.
Article Snippet: Maarten B. Rookmaaker, Marianne C. Verhaar, Hetty C. de Boer, Roel Goldschmeding, Jaap A. Joles, Hein A. Koomans, Hermann-Josef Gröne, and Ton J. Rabelink Department of Vascular Medicine, University Medical Center Utrecht, Utrecht; Department of Nephrology, Leiden University Medical Center, Leiden; Departments of Pathology and of Nephrology and Hypertension, University Medical Center Utrecht, Utrecht; and Department of Cellular and Molecular Pathology, German Cancer Research Center, Heidelberg, Germany

Image Search Results

CCL5 induction in DILI patients and an AILI mouse model. a ELISA analysis of serum CCL5 levels in DILI patients (n = 15) and healthy controls (n = 15). b Representative IHC images of hepatic CCL5 expression in DILI patients and healthy controls (original magnification = ×200, scale bar = 100 μm). c Dynamic serum CCL5 levels in WT mice after APAP challenge at the indicated time points (n = 4–6). d Representative IHC images of hepatic CCL5 expression in WT mice 24 h after APAP treatment and in normal controls (original magnification = ×200, scale bar = 100 μm). e Relative Ccl5 mRNA expression was determined in liver tissues, primary hepatocytes (PMHs), and nonparenchymal cells (NPCs) 6 h after APAP treatment (n = 3–4). The data are shown as means ± SEM, *P < 0.05, ****P < 0.0001

Journal: Cellular and Molecular Immunology

Article Title: CCL5 deficiency promotes liver repair by improving inflammation resolution and liver regeneration through M2 macrophage polarization

doi: 10.1038/s41423-019-0279-0

Figure Lengend Snippet: CCL5 induction in DILI patients and an AILI mouse model. a ELISA analysis of serum CCL5 levels in DILI patients (n = 15) and healthy controls (n = 15). b Representative IHC images of hepatic CCL5 expression in DILI patients and healthy controls (original magnification = ×200, scale bar = 100 μm). c Dynamic serum CCL5 levels in WT mice after APAP challenge at the indicated time points (n = 4–6). d Representative IHC images of hepatic CCL5 expression in WT mice 24 h after APAP treatment and in normal controls (original magnification = ×200, scale bar = 100 μm). e Relative Ccl5 mRNA expression was determined in liver tissues, primary hepatocytes (PMHs), and nonparenchymal cells (NPCs) 6 h after APAP treatment (n = 3–4). The data are shown as means ± SEM, *P < 0.05, ****P < 0.0001

Article Snippet: To evaluate the therapeutic potential of CCL5 inhibition, a CCL5-neutralizing antibody (anti-CCL5, AF478, R&D, USA); control IgG (AB-108-C, R&D, USA); or a CCL5 receptor antagonist (Met-CCL5, 335-RM/CF, R&D, USA) were reconstituted in sterile PBS and administered to WT mice (10 μg/injection, i.p) 6 and 24 h after APAP overdose.

Techniques: Enzyme-linked Immunosorbent Assay, Expressing

Ccl5−/− mice display rapid liver recovery after APAP treatment. a–c APAP treatment in both Ccl5−/− and WT mice at the indicated time points (n = 4–6). a Serum levels of ALT/AST of both genotypes. b Representative images of H&E staining (original magnification = ×100, scale bar = 200 μm) and the statistical quantification of hepatic necrosis. c Representative images of TUNEL staining (original magnification = ×200, scale bar = 100 μm) and the statistical quantification of TUNEL-positive cells. d Survival curve of Ccl5−/− and WT mice in response to a lethal dose of APAP (n = 15). The data are shown as means ± SEM, *P < 0.05, **P < 0.01

Journal: Cellular and Molecular Immunology

Article Title: CCL5 deficiency promotes liver repair by improving inflammation resolution and liver regeneration through M2 macrophage polarization

doi: 10.1038/s41423-019-0279-0

Figure Lengend Snippet: Ccl5−/− mice display rapid liver recovery after APAP treatment. a–c APAP treatment in both Ccl5−/− and WT mice at the indicated time points (n = 4–6). a Serum levels of ALT/AST of both genotypes. b Representative images of H&E staining (original magnification = ×100, scale bar = 200 μm) and the statistical quantification of hepatic necrosis. c Representative images of TUNEL staining (original magnification = ×200, scale bar = 100 μm) and the statistical quantification of TUNEL-positive cells. d Survival curve of Ccl5−/− and WT mice in response to a lethal dose of APAP (n = 15). The data are shown as means ± SEM, *P < 0.05, **P < 0.01

Techniques: Staining, TUNEL Assay

Enhanced inflammation resolution and liver regeneration in Ccl5−/− mice at the late phase of APAP treatment. a–e APAP treatment in both Ccl5−/− and WT mice at the indicated time points (n = 4–6). a ELISA analyses of the serum levels of IL-6 and TNFα. b Representative FACS plots and the statistical quantification of hepatic neutrophils (Ly6G+CD11b+). c Representative IHC images and the statistical quantification of hepatic Ly6G+ cells in liver sections (original magnification = ×400, scale bar = 50 μm). d Representative immunohistochemical staining of hepatic Ki67 in liver sections of Ccl5−/− and control mice at the indicated time points after APAP treatment and the quantification of Ki67-positive cells in liver sections (n = 4–6). e Western blot analysis showing the expression of hepatic PCNA in Ccl5−/− and control mice at the indicated time points after APAP treatment and the quantification of hepatic PCNA levels normalized to β-actin (n = 3–4). The data are shown as means ± SEM, *P < 0.05, **P < 0.01

Journal: Cellular and Molecular Immunology

Article Title: CCL5 deficiency promotes liver repair by improving inflammation resolution and liver regeneration through M2 macrophage polarization

doi: 10.1038/s41423-019-0279-0

Figure Lengend Snippet: Enhanced inflammation resolution and liver regeneration in Ccl5−/− mice at the late phase of APAP treatment. a–e APAP treatment in both Ccl5−/− and WT mice at the indicated time points (n = 4–6). a ELISA analyses of the serum levels of IL-6 and TNFα. b Representative FACS plots and the statistical quantification of hepatic neutrophils (Ly6G+CD11b+). c Representative IHC images and the statistical quantification of hepatic Ly6G+ cells in liver sections (original magnification = ×400, scale bar = 50 μm). d Representative immunohistochemical staining of hepatic Ki67 in liver sections of Ccl5−/− and control mice at the indicated time points after APAP treatment and the quantification of Ki67-positive cells in liver sections (n = 4–6). e Western blot analysis showing the expression of hepatic PCNA in Ccl5−/− and control mice at the indicated time points after APAP treatment and the quantification of hepatic PCNA levels normalized to β-actin (n = 3–4). The data are shown as means ± SEM, *P < 0.05, **P < 0.01

Techniques: Enzyme-linked Immunosorbent Assay, Immunohistochemical staining, Staining, Control, Western Blot, Expressing

Increased M2 macrophages in Ccl5−/− mice at the late phase of APAP treatment. a–d APAP treatment in both Ccl5−/− and WT mice at 36 h. a Representative MoMF (CD11bhighF4/80int) and KC (CD11bint F4/80high) profiles of CD45+ liver nongranulocytes from Ccl5−/− and WT mice 36 h after APAP treatment and the quantification of the proportion of MoMFs and KCs relative to total CD45+ liver nongranulocytes (n = 4–6). b Representative FACS plots and the statistical quantification of CD206+ hepatic macrophages (hMφ) (n = 4–6). c The relative expression of M1 markers (iNOS, IL-1β, and TNFα) and M2 markers (Arg1, Ym1, and CD206) was determined in FACS-sorted hepatic macrophages (CD45+CD11b+F4/80+) (n = 4). d Representative images and the statistical quantification of hepatic cells positive for CD68 (a panmacrophage marker) and Ym1 (an M2 macrophage marker) in liver sections (original magnification = ×400, scale bar = 50 μm). The data are shown as the means ± SEM, *P < 0.05, **P < 0.01. hMφ hepatic macrophages

Journal: Cellular and Molecular Immunology

Article Title: CCL5 deficiency promotes liver repair by improving inflammation resolution and liver regeneration through M2 macrophage polarization

doi: 10.1038/s41423-019-0279-0

Figure Lengend Snippet: Increased M2 macrophages in Ccl5−/− mice at the late phase of APAP treatment. a–d APAP treatment in both Ccl5−/− and WT mice at 36 h. a Representative MoMF (CD11bhighF4/80int) and KC (CD11bint F4/80high) profiles of CD45+ liver nongranulocytes from Ccl5−/− and WT mice 36 h after APAP treatment and the quantification of the proportion of MoMFs and KCs relative to total CD45+ liver nongranulocytes (n = 4–6). b Representative FACS plots and the statistical quantification of CD206+ hepatic macrophages (hMφ) (n = 4–6). c The relative expression of M1 markers (iNOS, IL-1β, and TNFα) and M2 markers (Arg1, Ym1, and CD206) was determined in FACS-sorted hepatic macrophages (CD45+CD11b+F4/80+) (n = 4). d Representative images and the statistical quantification of hepatic cells positive for CD68 (a panmacrophage marker) and Ym1 (an M2 macrophage marker) in liver sections (original magnification = ×400, scale bar = 50 μm). The data are shown as the means ± SEM, *P < 0.05, **P < 0.01. hMφ hepatic macrophages

Techniques: Expressing, Marker

CCL5 directly regulates macrophage polarization. Mouse peritoneal macrophages (PMφ) and bone marrow-derived macrophages (BMMφ) were stimulated with 100 ng/ml rmCCL5 for 6 h, and the expression of M1 macrophage markers (iNOS, IL-1β, and TNFα) was detected by qPCR in PMφ (a) and BMMφ (b). PMφ and BMMφ were stimulated with 20 ng/ml IL4 and with or without 100 ng/ml rmCCL5 for 6 h, and the expression of M2 macrophage markers (Arg1, Ym1, and CD206) was detected by qPCR in PMφ (c) and BMMφ (d). PMφ and BMMφ were stimulated with 20 ng/ml IL4 and with or without 100 ng/ml rmCCL5 for 24 h, and the expression of M2 macrophage markers (Arg1, Ym1, and CD206) was detected by western blot analysis in PMφ (e) and BMMφ (f). The data are represented as the mean ± SEM of at least three independent experiments. **P < 0.01, ***P < 0.001

Journal: Cellular and Molecular Immunology

Article Title: CCL5 deficiency promotes liver repair by improving inflammation resolution and liver regeneration through M2 macrophage polarization

doi: 10.1038/s41423-019-0279-0

Figure Lengend Snippet: CCL5 directly regulates macrophage polarization. Mouse peritoneal macrophages (PMφ) and bone marrow-derived macrophages (BMMφ) were stimulated with 100 ng/ml rmCCL5 for 6 h, and the expression of M1 macrophage markers (iNOS, IL-1β, and TNFα) was detected by qPCR in PMφ (a) and BMMφ (b). PMφ and BMMφ were stimulated with 20 ng/ml IL4 and with or without 100 ng/ml rmCCL5 for 6 h, and the expression of M2 macrophage markers (Arg1, Ym1, and CD206) was detected by qPCR in PMφ (c) and BMMφ (d). PMφ and BMMφ were stimulated with 20 ng/ml IL4 and with or without 100 ng/ml rmCCL5 for 24 h, and the expression of M2 macrophage markers (Arg1, Ym1, and CD206) was detected by western blot analysis in PMφ (e) and BMMφ (f). The data are represented as the mean ± SEM of at least three independent experiments. **P < 0.01, ***P < 0.001

Techniques: Derivative Assay, Expressing, Western Blot

CCL5 regulates macrophage polarization mainly through CCR1- and CCR5-related MAPK/NF-κB pathways. a Mouse peritoneal macrophages (PMφ) were stimulated with 100 ng/ml rmCCL5 for 0–60 min, and the signaling activation of the MAPK and NF-κB pathways was detected by western blot analysis. b PMφ were pretreated with a CCR1/3/5 antagonist separately for 1 h and then stimulated with 100 ng/ml rmCCL5 for 30 min. The signaling activation of the MAPK and NF-κB pathways was detected by western blot analysis. c PMφ were pretreated with a CCR1/3/5 antagonist separately for 1 h and then stimulated with 100 ng/ml rmCCL5 for 6 h. qPCR analysis of M1 marker and M2 marker expression was performed (n = 4). d, e Raw 264.7 cells were pretreated with control, CCR1, or CCR5 siRNA separately for 48 h. d Western blot analysis detected the knockdown of CCR1 and CCR5. siRNA-treated cells were stimulated with 100 ng/ml rmCCL5 for 30 min, and the signaling activation of the MAPK and NF-κB pathways was detected by western blot analysis. e siRNA-treated cells were stimulated with 100 ng/ml rmCCL5 for 6 h, and qPCR analysis of M1 marker and M2 marker expression was performed (n = 4). The data are shown as means ± SEM, *P < 0.05. **P < 0.01, ***P < 0.001

Journal: Cellular and Molecular Immunology

Article Title: CCL5 deficiency promotes liver repair by improving inflammation resolution and liver regeneration through M2 macrophage polarization

doi: 10.1038/s41423-019-0279-0

Figure Lengend Snippet: CCL5 regulates macrophage polarization mainly through CCR1- and CCR5-related MAPK/NF-κB pathways. a Mouse peritoneal macrophages (PMφ) were stimulated with 100 ng/ml rmCCL5 for 0–60 min, and the signaling activation of the MAPK and NF-κB pathways was detected by western blot analysis. b PMφ were pretreated with a CCR1/3/5 antagonist separately for 1 h and then stimulated with 100 ng/ml rmCCL5 for 30 min. The signaling activation of the MAPK and NF-κB pathways was detected by western blot analysis. c PMφ were pretreated with a CCR1/3/5 antagonist separately for 1 h and then stimulated with 100 ng/ml rmCCL5 for 6 h. qPCR analysis of M1 marker and M2 marker expression was performed (n = 4). d, e Raw 264.7 cells were pretreated with control, CCR1, or CCR5 siRNA separately for 48 h. d Western blot analysis detected the knockdown of CCR1 and CCR5. siRNA-treated cells were stimulated with 100 ng/ml rmCCL5 for 30 min, and the signaling activation of the MAPK and NF-κB pathways was detected by western blot analysis. e siRNA-treated cells were stimulated with 100 ng/ml rmCCL5 for 6 h, and qPCR analysis of M1 marker and M2 marker expression was performed (n = 4). The data are shown as means ± SEM, *P < 0.05. **P < 0.01, ***P < 0.001

Techniques: Activation Assay, Western Blot, Marker, Expressing, Control, Knockdown

CCL5 neutralization or inhibition facilitates liver recovery after acute liver injury. a A schematic of CCL5 inhibition by anti-CCL5 or Met-CCL5 in the APAP overdose model. The dose of anti-CCL5 and Met-CCL5 was 10 μg. b Serum levels of ALT/AST were detected after anti-CCL5- or Met-CCL5-mediated CCL5 blockage (n = 4–6). c Representative images of H&E staining (original magnification = ×100, scale bar = 200 μm) and the statistical quantification of hepatic necrosis upon anti-CCL5- or Met-CCL5-mediated CCL5 inhibition (n = 4–6). d Representative images and the statistical quantification of hepatic Ly6G+ cells in liver sections (original magnification = ×400, scale bar = 50 μm) upon anti-CCL5- or Met-CCL5-mediated CCL5 inhibition (n = 4–6). e Representative FACS plots and the statistical quantification of CD206+ hepatic macrophages (hMφ) upon anti-CCL5- or Met-CCL5-mediated CCL5 inhibition (n = 4–6). f Survival curves of mice (n = 10–12) in response to a lethal dose of APAP treatment upon anti-CCL5- or Met-CCL5-mediated CCL5 inhibition. The data are shown as means ± SEM, *P < 0.05

Journal: Cellular and Molecular Immunology

Article Title: CCL5 deficiency promotes liver repair by improving inflammation resolution and liver regeneration through M2 macrophage polarization

doi: 10.1038/s41423-019-0279-0

Figure Lengend Snippet: CCL5 neutralization or inhibition facilitates liver recovery after acute liver injury. a A schematic of CCL5 inhibition by anti-CCL5 or Met-CCL5 in the APAP overdose model. The dose of anti-CCL5 and Met-CCL5 was 10 μg. b Serum levels of ALT/AST were detected after anti-CCL5- or Met-CCL5-mediated CCL5 blockage (n = 4–6). c Representative images of H&E staining (original magnification = ×100, scale bar = 200 μm) and the statistical quantification of hepatic necrosis upon anti-CCL5- or Met-CCL5-mediated CCL5 inhibition (n = 4–6). d Representative images and the statistical quantification of hepatic Ly6G+ cells in liver sections (original magnification = ×400, scale bar = 50 μm) upon anti-CCL5- or Met-CCL5-mediated CCL5 inhibition (n = 4–6). e Representative FACS plots and the statistical quantification of CD206+ hepatic macrophages (hMφ) upon anti-CCL5- or Met-CCL5-mediated CCL5 inhibition (n = 4–6). f Survival curves of mice (n = 10–12) in response to a lethal dose of APAP treatment upon anti-CCL5- or Met-CCL5-mediated CCL5 inhibition. The data are shown as means ± SEM, *P < 0.05

Techniques: Neutralization, Inhibition, Staining

Figure 1. Presence of RANTES in PMPs and endothelial RANTES deposition by PMPs. A, RANTES concentrations were determined in supernatants of nonactivated and activated platelets (nonact./act. platelet sup), in PMPs, and PMP supernatants (PMP sup). Data represent meanSEM (n3). B, The presence of RANTES on the surface of PMPs was analyzed by ﬂow cytometry. Representative histograms for RANTES staining (open) or isotype control (ﬁlled) are shown (n3). C, Representative immuno- blots for RANTES, P-selectin, and PF4 in nonactivated platelets (1), PMPs (2), and positive control (3; n3). D, Immunoﬂuores- cence of IL-1–activated HMVECs perfused with PMPs (left) or assay buffer (right). Bar20 m. Shown are representative images (n5). E, Activated HMVECs were perfused or incubated in stasis with PMPs, PMP supernatants, or assay buffer (control), and RANTES deposition was quantiﬁed by immunoﬂuorescence. Data are expressed as percentage of control and represent meanSEM (n4). *P0.01 vs PMPs in ﬂow.

Journal: Arteriosclerosis, Thrombosis, and Vascular Biology

Article Title: Platelet Microparticles

doi: 10.1161/01.atv.0000170133.43608.37

Figure Lengend Snippet: Figure 1. Presence of RANTES in PMPs and endothelial RANTES deposition by PMPs. A, RANTES concentrations were determined in supernatants of nonactivated and activated platelets (nonact./act. platelet sup), in PMPs, and PMP supernatants (PMP sup). Data represent meanSEM (n3). B, The presence of RANTES on the surface of PMPs was analyzed by ﬂow cytometry. Representative histograms for RANTES staining (open) or isotype control (ﬁlled) are shown (n3). C, Representative immuno- blots for RANTES, P-selectin, and PF4 in nonactivated platelets (1), PMPs (2), and positive control (3; n3). D, Immunoﬂuores- cence of IL-1–activated HMVECs perfused with PMPs (left) or assay buffer (right). Bar20 m. Shown are representative images (n5). E, Activated HMVECs were perfused or incubated in stasis with PMPs, PMP supernatants, or assay buffer (control), and RANTES deposition was quantiﬁed by immunoﬂuorescence. Data are expressed as percentage of control and represent meanSEM (n4). *P0.01 vs PMPs in ﬂow.

Article Snippet: Human microvascular endothelial cells (HMVECs; PromoCell) and monocytic Mono Mac 6 cells were cultured as described.6 The RANTES receptor antagonist Met-RANTES was provided by A. Proudfoot (Serono Pharmaceutical Research Institute, Geneva).

Techniques: Cytometry, Staining, Control, Western Blot, Positive Control, Incubation

Figure 2. Transient interactions of PMPs with activated endo- thelium promote RANTES deposition. A, Immunoﬂuorescence staining of RANTES after perfusion of HMVECs with DiI-labeled PMPs for correlation of RANTES immobilization and ﬁrm PMP adhesion. Bar50 m. B, ScEM analysis (SE mode) of adherent PMPs after perfusion on HMVECs. Bar2 m. C, ScEM studies (BSE mode) show RANTES immobilized on HMVECs after PMP perfusion without colocalization to adherent PMPs (circle). Bar2 m. D, Mixed SE/BSE mode image of 1 adherent PMP with endothelial RANTES staining beyond its immediate vicinity. Bar0.5 m. Shown are representative images (n3).

Journal: Arteriosclerosis, Thrombosis, and Vascular Biology

Article Title: Platelet Microparticles

doi: 10.1161/01.atv.0000170133.43608.37

Figure Lengend Snippet: Figure 2. Transient interactions of PMPs with activated endo- thelium promote RANTES deposition. A, Immunoﬂuorescence staining of RANTES after perfusion of HMVECs with DiI-labeled PMPs for correlation of RANTES immobilization and ﬁrm PMP adhesion. Bar50 m. B, ScEM analysis (SE mode) of adherent PMPs after perfusion on HMVECs. Bar2 m. C, ScEM studies (BSE mode) show RANTES immobilized on HMVECs after PMP perfusion without colocalization to adherent PMPs (circle). Bar2 m. D, Mixed SE/BSE mode image of 1 adherent PMP with endothelial RANTES staining beyond its immediate vicinity. Bar0.5 m. Shown are representative images (n3).

Techniques: Staining, Labeling

Figure 3. Differential role of PMP-expressed adhesion receptors in PMP functions. A, Rolling of PMPs. DiI-labeled PMPs were perfused on activated HMVECs, and images were recorded with an exposure time of 100 ms. Bar50 m. Shown are representative images (n4). B, The presence of P-selectin, GPIb, GPIIb/IIIa, JAM-A, and CX3CR1 on the surface of PMP was analyzed by ﬂow cytometry. Representative histograms for staining with speciﬁc antibodies (open) or isotype controls (ﬁlled) are shown (n3). C, DiI-labeled PMPs left untreated (control) or pretreated with control or blocking agents were perfused over activated HMVECs. Quantiﬁcation of PMP roll- ing (left), shear-resistant PMP adhesion (middle), and PMP-mediated RANTES deposition (right). D, RANTES deposition (left) by PMPs obtained from healthy individuals or a patient with Glanzmann’s thrombasthenia (GT). Dot plot analysis (side scatter [SSC] vs forward scatter [FSC]) of thrombin/collagen-stimulated PMP formation (right) vs baseline (middle) in thrombasthenic platelets. Data are expressed as percentage of control and represent meanSEM (n4). *P0.01 vs control.

Journal: Arteriosclerosis, Thrombosis, and Vascular Biology

Article Title: Platelet Microparticles

doi: 10.1161/01.atv.0000170133.43608.37

Figure Lengend Snippet: Figure 3. Differential role of PMP-expressed adhesion receptors in PMP functions. A, Rolling of PMPs. DiI-labeled PMPs were perfused on activated HMVECs, and images were recorded with an exposure time of 100 ms. Bar50 m. Shown are representative images (n4). B, The presence of P-selectin, GPIb, GPIIb/IIIa, JAM-A, and CX3CR1 on the surface of PMP was analyzed by ﬂow cytometry. Representative histograms for staining with speciﬁc antibodies (open) or isotype controls (ﬁlled) are shown (n3). C, DiI-labeled PMPs left untreated (control) or pretreated with control or blocking agents were perfused over activated HMVECs. Quantiﬁcation of PMP roll- ing (left), shear-resistant PMP adhesion (middle), and PMP-mediated RANTES deposition (right). D, RANTES deposition (left) by PMPs obtained from healthy individuals or a patient with Glanzmann’s thrombasthenia (GT). Dot plot analysis (side scatter [SSC] vs forward scatter [FSC]) of thrombin/collagen-stimulated PMP formation (right) vs baseline (middle) in thrombasthenic platelets. Data are expressed as percentage of control and represent meanSEM (n4). *P0.01 vs control.

Techniques: Labeling, Cytometry, Staining, Control, Blocking Assay, Shear

Figure 4. Monocyte recruitment on acti- vated endothelium. A, HMVECs were preperfused with PMPs or PMP superna- tants treated with or without RANTES mAb or assay buffer (control). Untreated or Met-RANTES–treated monocytes were perfused, and the number of adherent cells was determined. *P0.01 vs PMPs; #P0.01 vs PMP supernatant (sup; with untreated monocytes). B, Role of PMP adhesion receptors in PMP-mediated arrest of monocytes. Activated HMVECs were preperfused with assay buffer (con- trol) or with PMPs pretreated with block- ing or control agents. Data are expressed as percentage of control and represent meanSEM (n6). *P0.01 vs PMPs.

Journal: Arteriosclerosis, Thrombosis, and Vascular Biology

Article Title: Platelet Microparticles

doi: 10.1161/01.atv.0000170133.43608.37

Figure Lengend Snippet: Figure 4. Monocyte recruitment on acti- vated endothelium. A, HMVECs were preperfused with PMPs or PMP superna- tants treated with or without RANTES mAb or assay buffer (control). Untreated or Met-RANTES–treated monocytes were perfused, and the number of adherent cells was determined. *P0.01 vs PMPs; #P0.01 vs PMP supernatant (sup; with untreated monocytes). B, Role of PMP adhesion receptors in PMP-mediated arrest of monocytes. Activated HMVECs were preperfused with assay buffer (con- trol) or with PMPs pretreated with block- ing or control agents. Data are expressed as percentage of control and represent meanSEM (n6). *P0.01 vs PMPs.

Techniques: Control, Blocking Assay

Review

rantes receptor antagonist met-rantes (Serono)

Structured Review

Images

Related Articles

other:

Similar Products

Image Search Results