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Interaction <t>of</t> <t>OPN</t> with integrin αVβ3 and CD44, and the roles of integrin αVβ3 and CD44 in S‐EMs‐induced VSMCs proliferation and migration of WKY and SHR. (A) Protein interactions of Spp1 predicted with STRING database. SPP1, Cd44 and Itgb3 are the protein coding gene of OPN, CD44 and integrin β3, respectively. (B and C) UMAP plot showing the classification of human aortic cells (B), and their expressions of OPN, integrin αV, integrin β3 and CD44 (C) according to single‐cell sequencing data of human aortic cells from three individuals according to the Single Cell database. VSMC, vascular smooth muscle cell; EC, endothelial cell; VAF, vascular adventitial fibroblast. (D) Molecular docking of OPN (red) and integrin αV (green) and β3 (blue), and molecular docking of OPN (red) and CD44 (green). (E) Levels of OPN, integrin αVβ3, and CD44 in VSMCs and EMs of WKY and SHR. (F) Representative Western blot images. (G) Effects of integrin αVβ3 inhibitor Cyclo <t>(‐RGDfK)</t> on S‐EMs‐induced VSMCs proliferation and migration of WKY and SHR. The integrin αVβ3 inhibitor Cyclo (‐RGDfK) (10 µM) was administered 2 h before S‐EMs (40 µg/mL). (H) Effects of CD44 knockdown (KD) on the S‐EMs‐induced VSMCs proliferation and migration of WKY and SHR. The si‐CD44 (50 nM) was administered 48 h before S‐EMs (40 µg/mL). VSMCs proliferation and migration were evaluated by the percentage of EdU‐positive cells and Boyden chamber assay 24 h after application of the S‐EMs. (I) Co‐immunoprecipitation (Co‐IP) and western blot images showing the binding of OPN with integrin αVβ3 in VSMCs. (J) Schematic of a gold surface with integrin αVβ3 protein immobilised on a sensor chip CM5 in surface plasmon resonance (SPR) assay. (K) Sensorgrams depicting interaction of OPN and integrin αVβ3. Values are mean ± SD. * p < 0.05 versus Ctrl; † p < 0.05 versus PBS; # p < 0.05 versus WKY. n = 4 in (E); n = 6 in others. Two‐way ANOVA followed by Bonferroni test (G–I). Unpaired Student's t ‐test (E).

Cyclo Rgdfk, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 94/100, based on 30 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/hy-p0023/Cyclo(-RGDfK)/pmc12326188-350-23-18
Average 94 stars, based on 30 article reviews

cyclo rgdfk - by Bioz Stars, 2026-10

94/100 stars

Images

1) Product Images from "Exomeres From Adventitial Fibroblasts of Spontaneously Hypertensive Rats Promote Vascular Remodelling via Transferring Osteopontin"

Article Title: Exomeres From Adventitial Fibroblasts of Spontaneously Hypertensive Rats Promote Vascular Remodelling via Transferring Osteopontin

Journal: Journal of Extracellular Vesicles

doi: 10.1002/jev2.70146

Interaction of OPN with integrin αVβ3 and CD44, and the roles of integrin αVβ3 and CD44 in S‐EMs‐induced VSMCs proliferation and migration of WKY and SHR. (A) Protein interactions of Spp1 predicted with STRING database. SPP1, Cd44 and Itgb3 are the protein coding gene of OPN, CD44 and integrin β3, respectively. (B and C) UMAP plot showing the classification of human aortic cells (B), and their expressions of OPN, integrin αV, integrin β3 and CD44 (C) according to single‐cell sequencing data of human aortic cells from three individuals according to the Single Cell database. VSMC, vascular smooth muscle cell; EC, endothelial cell; VAF, vascular adventitial fibroblast. (D) Molecular docking of OPN (red) and integrin αV (green) and β3 (blue), and molecular docking of OPN (red) and CD44 (green). (E) Levels of OPN, integrin αVβ3, and CD44 in VSMCs and EMs of WKY and SHR. (F) Representative Western blot images. (G) Effects of integrin αVβ3 inhibitor Cyclo (‐RGDfK) on S‐EMs‐induced VSMCs proliferation and migration of WKY and SHR. The integrin αVβ3 inhibitor Cyclo (‐RGDfK) (10 µM) was administered 2 h before S‐EMs (40 µg/mL). (H) Effects of CD44 knockdown (KD) on the S‐EMs‐induced VSMCs proliferation and migration of WKY and SHR. The si‐CD44 (50 nM) was administered 48 h before S‐EMs (40 µg/mL). VSMCs proliferation and migration were evaluated by the percentage of EdU‐positive cells and Boyden chamber assay 24 h after application of the S‐EMs. (I) Co‐immunoprecipitation (Co‐IP) and western blot images showing the binding of OPN with integrin αVβ3 in VSMCs. (J) Schematic of a gold surface with integrin αVβ3 protein immobilised on a sensor chip CM5 in surface plasmon resonance (SPR) assay. (K) Sensorgrams depicting interaction of OPN and integrin αVβ3. Values are mean ± SD. * p < 0.05 versus Ctrl; † p < 0.05 versus PBS; # p < 0.05 versus WKY. n = 4 in (E); n = 6 in others. Two‐way ANOVA followed by Bonferroni test (G–I). Unpaired Student's t ‐test (E).

Figure Legend Snippet: Interaction of OPN with integrin αVβ3 and CD44, and the roles of integrin αVβ3 and CD44 in S‐EMs‐induced VSMCs proliferation and migration of WKY and SHR. (A) Protein interactions of Spp1 predicted with STRING database. SPP1, Cd44 and Itgb3 are the protein coding gene of OPN, CD44 and integrin β3, respectively. (B and C) UMAP plot showing the classification of human aortic cells (B), and their expressions of OPN, integrin αV, integrin β3 and CD44 (C) according to single‐cell sequencing data of human aortic cells from three individuals according to the Single Cell database. VSMC, vascular smooth muscle cell; EC, endothelial cell; VAF, vascular adventitial fibroblast. (D) Molecular docking of OPN (red) and integrin αV (green) and β3 (blue), and molecular docking of OPN (red) and CD44 (green). (E) Levels of OPN, integrin αVβ3, and CD44 in VSMCs and EMs of WKY and SHR. (F) Representative Western blot images. (G) Effects of integrin αVβ3 inhibitor Cyclo (‐RGDfK) on S‐EMs‐induced VSMCs proliferation and migration of WKY and SHR. The integrin αVβ3 inhibitor Cyclo (‐RGDfK) (10 µM) was administered 2 h before S‐EMs (40 µg/mL). (H) Effects of CD44 knockdown (KD) on the S‐EMs‐induced VSMCs proliferation and migration of WKY and SHR. The si‐CD44 (50 nM) was administered 48 h before S‐EMs (40 µg/mL). VSMCs proliferation and migration were evaluated by the percentage of EdU‐positive cells and Boyden chamber assay 24 h after application of the S‐EMs. (I) Co‐immunoprecipitation (Co‐IP) and western blot images showing the binding of OPN with integrin αVβ3 in VSMCs. (J) Schematic of a gold surface with integrin αVβ3 protein immobilised on a sensor chip CM5 in surface plasmon resonance (SPR) assay. (K) Sensorgrams depicting interaction of OPN and integrin αVβ3. Values are mean ± SD. * p < 0.05 versus Ctrl; † p < 0.05 versus PBS; # p < 0.05 versus WKY. n = 4 in (E); n = 6 in others. Two‐way ANOVA followed by Bonferroni test (G–I). Unpaired Student's t ‐test (E).

Techniques Used: Migration, Single Cell, Sequencing, Western Blot, Knockdown, Boyden Chamber Assay, Immunoprecipitation, Co-Immunoprecipitation Assay, Binding Assay, SPR Assay

Integrin αVβ3‐FAK‐PI3K‐AKT signalling mediates the roles of S‐EMs in promoting VSMCs proliferation and migration of WKY and SHR. (A) Effects of integrin αVβ3 inhibitor Cyclo(‐RGDfK) (10 µM) on S‐EMs‐induced PI3K (p85α) and AKT phosphorylation in VSMCs. (B) Representative Western blot images. (C) Protein interactions of integrin β3 with PI3K according to STRING database. Itgb3, Pik3r1 and PIk2 are the protein coding gene of integrin β3, PI3K and FAK, respectively. (D) Molecular docking of integrin αV (green) and β3 (blue), and FAK (purple). (E) Effects of integrin αVβ3 inhibitor Cyclo(‐RGDfK) (10 µM) on S‐EMs‐induced FAK phosphorylation in VSMCs. (F) Effects of FAK inhibitor Y15 (2.5 µM), PI3K inhibitor LY294002 (5 µM) or AKT inhibitor AKTi1/2 (0.5 µM) on S‐EMs‐induced VSMC proliferation and migration. S‐EMs (40 µg/mL) was administered 2 h after application of the inhibitors. VSMCs proliferation and migration were evaluated by the percentage of EdU‐positive cells and Boyden chamber assay. Values are mean ± SD. * p < 0.05 versus Ctrl or DMSO; † p < 0.05 versus PBS; # p < 0.05 versus WKY. n = 4 in (A) and (E); n = 6 in (F). Two‐way ANOVA followed by Bonferroni test.

Figure Legend Snippet: Integrin αVβ3‐FAK‐PI3K‐AKT signalling mediates the roles of S‐EMs in promoting VSMCs proliferation and migration of WKY and SHR. (A) Effects of integrin αVβ3 inhibitor Cyclo(‐RGDfK) (10 µM) on S‐EMs‐induced PI3K (p85α) and AKT phosphorylation in VSMCs. (B) Representative Western blot images. (C) Protein interactions of integrin β3 with PI3K according to STRING database. Itgb3, Pik3r1 and PIk2 are the protein coding gene of integrin β3, PI3K and FAK, respectively. (D) Molecular docking of integrin αV (green) and β3 (blue), and FAK (purple). (E) Effects of integrin αVβ3 inhibitor Cyclo(‐RGDfK) (10 µM) on S‐EMs‐induced FAK phosphorylation in VSMCs. (F) Effects of FAK inhibitor Y15 (2.5 µM), PI3K inhibitor LY294002 (5 µM) or AKT inhibitor AKTi1/2 (0.5 µM) on S‐EMs‐induced VSMC proliferation and migration. S‐EMs (40 µg/mL) was administered 2 h after application of the inhibitors. VSMCs proliferation and migration were evaluated by the percentage of EdU‐positive cells and Boyden chamber assay. Values are mean ± SD. * p < 0.05 versus Ctrl or DMSO; † p < 0.05 versus PBS; # p < 0.05 versus WKY. n = 4 in (A) and (E); n = 6 in (F). Two‐way ANOVA followed by Bonferroni test.

Techniques Used: Migration, Phospho-proteomics, Western Blot, Boyden Chamber Assay

Effects of intravenous injections of VAFs‐derived EMs (200 µg, every 2 days, 10 times) on vascular remodelling and related signalling pathway in aorta and MA of WKY and SHR. (A) Media thickness, lumen diameter and the ratio of lumen diameter to media thickness of the aorta and mesentery artery. (B) Representative images showing the Masson’ staining of aorta and MA. (C) Bar graph showing the relative fluorescent intensity of OPN. (D) Representative images showing OPN immunofluorescence staining. (E) OPN mRNA level; (F) OPN, integrin αV and integrin β3 protein expressions. (G) PI3K, AKT and FAK protein expressions and their phosphorylation levels. (H) Representative Western blot images. (I) Effects of integrin αVβ3 inhibitor Cyclo (‐RGDfK) (10 mg/kg, ip, every 2 days, 10 times) on the roles of S‐EMs (200 µg, iv, every 2 days, 10 times) in promoting vascular remodelling in aorta of WKY. (J) Representative images of the Masson’ staining. Values are mean ± SD. * p < 0.05 versus S‐EMs; † p < 0.05 versus PBS; ‡ p < 0.05 versus W‐EMs; # p < 0.05 versus WKY. n = 6 in (A), (C) and (I); n = 4 in (E–G). Two‐way ANOVA followed by Bonferroni test.

Figure Legend Snippet: Effects of intravenous injections of VAFs‐derived EMs (200 µg, every 2 days, 10 times) on vascular remodelling and related signalling pathway in aorta and MA of WKY and SHR. (A) Media thickness, lumen diameter and the ratio of lumen diameter to media thickness of the aorta and mesentery artery. (B) Representative images showing the Masson’ staining of aorta and MA. (C) Bar graph showing the relative fluorescent intensity of OPN. (D) Representative images showing OPN immunofluorescence staining. (E) OPN mRNA level; (F) OPN, integrin αV and integrin β3 protein expressions. (G) PI3K, AKT and FAK protein expressions and their phosphorylation levels. (H) Representative Western blot images. (I) Effects of integrin αVβ3 inhibitor Cyclo (‐RGDfK) (10 mg/kg, ip, every 2 days, 10 times) on the roles of S‐EMs (200 µg, iv, every 2 days, 10 times) in promoting vascular remodelling in aorta of WKY. (J) Representative images of the Masson’ staining. Values are mean ± SD. * p < 0.05 versus S‐EMs; † p < 0.05 versus PBS; ‡ p < 0.05 versus W‐EMs; # p < 0.05 versus WKY. n = 6 in (A), (C) and (I); n = 4 in (E–G). Two‐way ANOVA followed by Bonferroni test.

Techniques Used: Derivative Assay, Staining, Immunofluorescence, Phospho-proteomics, Western Blot

Concentration Assay:

Article Title: Remodeling the immunosuppressive microenvironment of KARS-LKB1 co-mutant non-small cell lung cancer via targeted PGAM5 siRNA delivery for enhanced immunotherapy
Article Snippet: KRAS–LKB1 (KL) co-mutant non-small cell lung cancer (NSCLC) is characterized by an immunologically “cold” tumor immune microenvironment (TIME), and resultantly exhibits intrinsic resistance to immune checkpoint inhibitor (ICI) therapy.. Developing effective strategies to remodel the TIME and overcome ICI resistance remains an urgent clinical need.. Single-cell RNA sequencing (scRNA-seq) identified PGAM5 as a therapeutic target in patients with KL co-mutant NSCLC.

Inhibition:

Article Title: Parvimonas micra exacerbates periodontitis by infiltrating host cells through TmpC and circumventing lysosomal elimination via AppA.
Article Snippet: .. For integrin α v β 3 inhibition, Cyclo(-RGDfK) (1 mg per rat) (MCE, HY-P0023) was injected intraperitoneally 3 times a week for 4 weeks. .. At the end of the experiment, the rats were sacrificed, and their maxillae were harvested and fixed in 4% paraformaldehyde (Solarbio, P1110).

Article Title: Parvimonas micra exacerbates periodontitis by infiltrating host cells through TmpC and circumventing lysosomal elimination via AppA
Article Snippet: .. For integrin α v β 3 inhibition, Cyclo(-RGDfK) (1 mg per rat) (MCE, HY-P0023) was injected intraperitoneally 3 times a week for 4 weeks. .. At the end of the experiment, the rats were sacrificed, and their maxillae were harvested and fixed in 4% paraformaldehyde (Solarbio, P1110).

Injection:

Recombinant:

Article Title: Legumain Restrains Granuloma Formation by Inhibiting mTORC1/STAT1‐Mediated M1 Macrophage Polarization in Sarcoidosis
Article Snippet: For M1 polarization, BMDMs were treated with 50 ng/mL LPS (Sigma‐Aldrich, Merck KGaA, Darmstadt, Germany) and 20 ng/mL recombinant mouse IFN‐γ (PeproTech, Cranbury, NJ, USA) and harvested at the indicated time points (0, 3, 6, and 12 h) for time‐course experiments, or at 12 h for all other experiments. .. For M2 polarization, BMDMs were treated with 20 ng/mL recombinant mouse IL‐4 (PeproTech, Cranbury, NJ, USA) and 20 ng/mL recombinant mouse IL‐13 (PeproTech, Cranbury, NJ, USA) for 24 or 48 h. For the indicated experiments, 10 μM Cyclo(‐RGDfK) (MedChemExpress, Shanghai, China), 1 μM Rapa (MedChemExpress, Shanghai, China), or 50 μM F‐ara‐A (MedChemExpress, Shanghai, China) was added during M1 polarization. .. For M1 polarization, BMDMs were treated with 50 ng/mL LPS (Sigma‐Aldrich, Merck KGaA, Darmstadt, Germany) and 20 ng/mL recombinant mouse IFN‐γ (PeproTech, Cranbury, NJ, USA) and harvested at the indicated time points (0, 3, 6, and 12 h) for time‐course experiments, or at 12 h for all other experiments.

Article Title: Legumain Restrains Granuloma Formation by Inhibiting mTORC1/STAT1-Mediated M1 Macrophage Polarization in Sarcoidosis.
Article Snippet: For M1 polarization, BMDMs were treated ith 50 ng/mL LPS (Sigma-Aldrich, Merck KGaA, Darmstadt, ermany) and 20 ng/mL recombinant mouse IFN- γ (PeproTech, ranbury, NJ, USA) and harvested at the indicated time points 0, 3, 6, and 12 h) for time-course experiments, or at 12 h for all ther experiments. .. For M2 polarization, BMDMs were treated ith 20 ng/mL recombinant mouse IL-4 (PeproTech, Cranbury, J, USA) and 20 ng/mL recombinant mouse IL-13 (PeproTech, ranbury, NJ, USA) for 24 or 48 h. For the indicated experiments, 0 μM Cyclo(-RGDfK) (MedChemExpress, Shanghai, China), 1 M Rapa (MedChemExpress, Shanghai, China), or 50 μM F-ara(MedChemExpress, Shanghai, China) was added during M1 olarization. .. Whole-slide images were acquired using a Pannoramic MIDI Digital Scanner (3DHISTECH, Budapest, Hungary).

Centrifugation:

Article Title: Shear-Electrostatic Synergistic Hydrogels with Biomimetic Microchannels for Vascularized Maxillofacial Bone Regeneration.
Article Snippet: Injectable hydrogels for maxillofacial bone repair often sacrifice structural integrity or bioactivity to achieve surgical adaptability.. To overcome this limitation, we developed a shear-responsive nanoarchitectonic hydrogel by integrating montmorillonite (MMT) nanosheets and RGD peptides.. During minimally invasive injection, MMT-guided self-assembly generates interconnected microchannels while significantly enhancing mechanical properties.

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