Journal: Frontiers in Cardiovascular Medicine

Article Title: Up-regulated expression of two-pore domain K + channels, KCNK1 and KCNK2, is involved in the proliferation and migration of pulmonary arterial smooth muscle cells in pulmonary arterial hypertension

doi: 10.3389/fcvm.2024.1343804

Figure Lengend Snippet: Specific primers of KCNK channel genes for qPCR.

Article Snippet: The membrane was blocked with Tris-buffered saline containing bovine serum albumin (5%) and Tween 20 (0.1%; MilliporeSigma) at room temperature (25°C) for 3 h and then treated with a primary antibody for KCNK1 (1:800; APC-110), KCNK2 (1:800; APC-047), KCNK3 (1:800; APC-024), KCNK6 (1:800; APC-040, Alomone Labs, Jerusalem, Israel), JNK (1:1000; #9252), or phospho ( p )-JNK (1:1000; #4668, Cell Signaling Technology, Danvers, MA, USA) at 4°C for 18 h. Immunoblotted membranes were then exposed to an anti-rabbit HRP-conjugated IgG secondary antibody (1:5000; #170-6515, Bio-Rad Laboratories, Hercules, CA, USA) at room temperature for 1 h. Blotting signals were detected using an ImmunoStar LD reagent (Fujifilm Wako Pure Chemical) and observed with the Imager 600 system (GE HealthCare Technologies, Chicago, IL, USA).

Techniques:

Journal: Frontiers in Cardiovascular Medicine

Article Title: Up-regulated expression of two-pore domain K + channels, KCNK1 and KCNK2, is involved in the proliferation and migration of pulmonary arterial smooth muscle cells in pulmonary arterial hypertension

doi: 10.3389/fcvm.2024.1343804

Figure Lengend Snippet: Expression profiles of KCNK family members in PASMCs from IPAH patients. The expression of KCNK channel family members (KCNK1 to 18, except for 8, 11, and 14) in normal- and IPAH-PASMCs was examined by qPCR and Western blotting. ( A ) Expression of KCNK family members in normal- and IPAH-PASMCs at the mRNA level ( n = 4). The mRNA expression level of KCNK was normalized to that of β-actin. Inset , the expression ratios of KCNK1, 2, 3, and 6 in IPAH-PASMCs to normal-PASMCs ( n = 4). ( B ) Protein expression of KCNK1, 2, 3, and 6 channels in normal- and IPAH-PASMCs ( n = 6–8). The protein expression of KCNK channels was normalized to that of β-actin and normal-PASMCs. Note that the expression of KCNK1/TWIK1 and KCNK2/TREK1 was up-regulated, whereas that of KCNK3/TASK1 and KCNK6/TWIK2 was down-regulated in IPAH-PASMCs. Data are presented as means ± S.E. * p < 0.05, ** p < 0.01 vs. normal-PASMCs (Mann–Whitney U test).

Article Snippet: The membrane was blocked with Tris-buffered saline containing bovine serum albumin (5%) and Tween 20 (0.1%; MilliporeSigma) at room temperature (25°C) for 3 h and then treated with a primary antibody for KCNK1 (1:800; APC-110), KCNK2 (1:800; APC-047), KCNK3 (1:800; APC-024), KCNK6 (1:800; APC-040, Alomone Labs, Jerusalem, Israel), JNK (1:1000; #9252), or phospho ( p )-JNK (1:1000; #4668, Cell Signaling Technology, Danvers, MA, USA) at 4°C for 18 h. Immunoblotted membranes were then exposed to an anti-rabbit HRP-conjugated IgG secondary antibody (1:5000; #170-6515, Bio-Rad Laboratories, Hercules, CA, USA) at room temperature for 1 h. Blotting signals were detected using an ImmunoStar LD reagent (Fujifilm Wako Pure Chemical) and observed with the Imager 600 system (GE HealthCare Technologies, Chicago, IL, USA).

Techniques: Expressing, Western Blot, MANN-WHITNEY

Journal: Frontiers in Cardiovascular Medicine

Article Title: Up-regulated expression of two-pore domain K + channels, KCNK1 and KCNK2, is involved in the proliferation and migration of pulmonary arterial smooth muscle cells in pulmonary arterial hypertension

doi: 10.3389/fcvm.2024.1343804

Figure Lengend Snippet: Up-regulated expression of KCNK1 and KCNK2 channels in PASMs from MCT-PH rats. The protein expression of KCNK1 and KCNK2 channels in PASMs from MCT-PH rats was examined by Western blotting and immunohistochemical staining. ( A,B ) Protein expression of KCNK1 ( A ) and KCNK2 ( B ) channels in PASMCs from control and MCT-PH rats ( n = 8). Protein expression was normalized to that of β-actin and the control group. ( C,D ) Representative immunohistochemical images of the lung sections of control and MCT-PH rats stained with a KCNK1 ( C ; green ), KCNK2 ( D ; green ), or α -SMA ( red ) antibody. Cell nuclei were stained with DAPI ( blue ). Similar results were obtained from six independent experiments. Note that the expression of KCNK1/TWIK1 and KCNK2/TREK1 was up-regulated in PASMs from MCT-PH rats. Data are presented as means ± S.E. ** p < 0.01, *** p < 0.001 vs. the control (Mann–Whitney U test).

Article Snippet: The membrane was blocked with Tris-buffered saline containing bovine serum albumin (5%) and Tween 20 (0.1%; MilliporeSigma) at room temperature (25°C) for 3 h and then treated with a primary antibody for KCNK1 (1:800; APC-110), KCNK2 (1:800; APC-047), KCNK3 (1:800; APC-024), KCNK6 (1:800; APC-040, Alomone Labs, Jerusalem, Israel), JNK (1:1000; #9252), or phospho ( p )-JNK (1:1000; #4668, Cell Signaling Technology, Danvers, MA, USA) at 4°C for 18 h. Immunoblotted membranes were then exposed to an anti-rabbit HRP-conjugated IgG secondary antibody (1:5000; #170-6515, Bio-Rad Laboratories, Hercules, CA, USA) at room temperature for 1 h. Blotting signals were detected using an ImmunoStar LD reagent (Fujifilm Wako Pure Chemical) and observed with the Imager 600 system (GE HealthCare Technologies, Chicago, IL, USA).

Techniques: Expressing, Western Blot, Immunohistochemical staining, Staining, Control, MANN-WHITNEY

Journal: Frontiers in Cardiovascular Medicine

Article Title: Up-regulated expression of two-pore domain K + channels, KCNK1 and KCNK2, is involved in the proliferation and migration of pulmonary arterial smooth muscle cells in pulmonary arterial hypertension

doi: 10.3389/fcvm.2024.1343804

Figure Lengend Snippet: Expression of KCNK1 and KCNK2 channels in PASMs from SuHx-PH rats and hypoxia-PH mice. The protein expression of KCNK1 and KCNK2 channels in PASMs from SuHx-PH rats and hypoxia-PH mice was examined by Western blotting. ( A,B ) Protein expression of KCNK1 ( A ) and KCNK2 ( B ) channels in PASMs from control and SuHx-PH rats ( n = 6). Protein expression was normalized to that of β-actin and the control group. ( C,D ) Protein expression of KCNK1 ( C ) and KCNK2 ( D ) channels in PASMs from normoxia and hypoxia-PH mice ( n = 6). Protein expression was normalized to that of β-actin and the normoxia group. Data are presented as means ± S.E. * p < 0.05, ** p < 0.01 vs. the control or normoxia group (Mann–Whitney U test).

Article Snippet: The membrane was blocked with Tris-buffered saline containing bovine serum albumin (5%) and Tween 20 (0.1%; MilliporeSigma) at room temperature (25°C) for 3 h and then treated with a primary antibody for KCNK1 (1:800; APC-110), KCNK2 (1:800; APC-047), KCNK3 (1:800; APC-024), KCNK6 (1:800; APC-040, Alomone Labs, Jerusalem, Israel), JNK (1:1000; #9252), or phospho ( p )-JNK (1:1000; #4668, Cell Signaling Technology, Danvers, MA, USA) at 4°C for 18 h. Immunoblotted membranes were then exposed to an anti-rabbit HRP-conjugated IgG secondary antibody (1:5000; #170-6515, Bio-Rad Laboratories, Hercules, CA, USA) at room temperature for 1 h. Blotting signals were detected using an ImmunoStar LD reagent (Fujifilm Wako Pure Chemical) and observed with the Imager 600 system (GE HealthCare Technologies, Chicago, IL, USA).

Techniques: Expressing, Western Blot, Control, MANN-WHITNEY

Journal: Frontiers in Cardiovascular Medicine

Article Title: Up-regulated expression of two-pore domain K + channels, KCNK1 and KCNK2, is involved in the proliferation and migration of pulmonary arterial smooth muscle cells in pulmonary arterial hypertension

doi: 10.3389/fcvm.2024.1343804

Figure Lengend Snippet: siRNA knockdown of KCNK1 and KCNK2 channels in IPAH-PASMCs. The effects of KCNK1 and KCNK2 siRNAs on the expression of KCNK1, KCNK2, KCNK3, and KCNK6 channels in IPAH-PASMCs were examined by qPCR and Western blotting. ( A,B ) Knockdown efficiency at the mRNA level of siRNA targeting KCNK1 ( A ) or KCNK2 ( B ) in IPAH-PASMCs ( n = 6). mRNA expression was normalized to that of β-actin and control siRNA. ( C,D ) Knockdown efficiency at the protein level of siRNA targeting KCNK1 ( C ) or KCNK2 ( D ) in IPAH-PASMCs ( n = 6). Protein expression was normalized to that of β-actin and control siRNA. Data are presented as means ± S.E. ** p < 0.01 vs. control siRNA (Mann–Whitney U test).

Article Snippet: The membrane was blocked with Tris-buffered saline containing bovine serum albumin (5%) and Tween 20 (0.1%; MilliporeSigma) at room temperature (25°C) for 3 h and then treated with a primary antibody for KCNK1 (1:800; APC-110), KCNK2 (1:800; APC-047), KCNK3 (1:800; APC-024), KCNK6 (1:800; APC-040, Alomone Labs, Jerusalem, Israel), JNK (1:1000; #9252), or phospho ( p )-JNK (1:1000; #4668, Cell Signaling Technology, Danvers, MA, USA) at 4°C for 18 h. Immunoblotted membranes were then exposed to an anti-rabbit HRP-conjugated IgG secondary antibody (1:5000; #170-6515, Bio-Rad Laboratories, Hercules, CA, USA) at room temperature for 1 h. Blotting signals were detected using an ImmunoStar LD reagent (Fujifilm Wako Pure Chemical) and observed with the Imager 600 system (GE HealthCare Technologies, Chicago, IL, USA).

Techniques: Knockdown, Expressing, Western Blot, Control, MANN-WHITNEY

Journal: Frontiers in Cardiovascular Medicine

Article Title: Up-regulated expression of two-pore domain K + channels, KCNK1 and KCNK2, is involved in the proliferation and migration of pulmonary arterial smooth muscle cells in pulmonary arterial hypertension

doi: 10.3389/fcvm.2024.1343804

Figure Lengend Snippet: Contribution of KCNK1 and KCNK2 channels to the proliferation and migration of IPAH-PASMCs. The involvement of KCNK1 and KCNK2 channels in the proliferation and migration of IPAH-PASMCs was examined by siRNA knockdown methods. ( A,B ) Inhibitory effects of the transfection with KCNK1 ( A ) or KCNK2 ( B ) siRNA for 48 h on the growth of IPAH-PASMCs using the Cell Counting Kit-8 assay ( n = 4). Absorbance was normalized by control siRNA. ( C,D ) Inhibitory effects of the transfection with KCNK1 ( C ) or KCNK2 ( D ) siRNA for 48 h on the excessive proliferation of IPAH-PASMCs using the BrdU incorporation assay ( n = 4). Absorbance was normalized by control siRNA. ( E ) Anti-migratory effects of the transfection with KCNK1 or KCNK2 siRNA on the migration of IPAH-PASMCs for 24 h using the Transwell assay ( n = 4). Data are presented as means ± S.E. * p < 0.05, ** p < 0.001 vs. control siRNA (Student's t -test ( A–D ) or Steel's test following Kruskal-Wallis test ( E )).

Article Snippet: The membrane was blocked with Tris-buffered saline containing bovine serum albumin (5%) and Tween 20 (0.1%; MilliporeSigma) at room temperature (25°C) for 3 h and then treated with a primary antibody for KCNK1 (1:800; APC-110), KCNK2 (1:800; APC-047), KCNK3 (1:800; APC-024), KCNK6 (1:800; APC-040, Alomone Labs, Jerusalem, Israel), JNK (1:1000; #9252), or phospho ( p )-JNK (1:1000; #4668, Cell Signaling Technology, Danvers, MA, USA) at 4°C for 18 h. Immunoblotted membranes were then exposed to an anti-rabbit HRP-conjugated IgG secondary antibody (1:5000; #170-6515, Bio-Rad Laboratories, Hercules, CA, USA) at room temperature for 1 h. Blotting signals were detected using an ImmunoStar LD reagent (Fujifilm Wako Pure Chemical) and observed with the Imager 600 system (GE HealthCare Technologies, Chicago, IL, USA).

Techniques: Migration, Knockdown, Transfection, Cell Counting, Control, BrdU Incorporation Assay, Transwell Assay

Journal: Frontiers in Cardiovascular Medicine

Article Title: Up-regulated expression of two-pore domain K + channels, KCNK1 and KCNK2, is involved in the proliferation and migration of pulmonary arterial smooth muscle cells in pulmonary arterial hypertension

doi: 10.3389/fcvm.2024.1343804

Figure Lengend Snippet: Contribution of KCNK1 and KCNK2 channels to the resting membrane potential and [Ca 2+ ] cyt in IPAH-PASMCs. The effects of the siRNA knockdown of KCNK1 and KCNK2 on the resting membrane potential and [Ca 2+ ] cyt were measured in IPAH-PASMCs. Membrane potential was monitored with the voltage-sensitive fluorescent indicator, DiBAC 4 (3). Fluorescent intensity of DiBAC 4 (3) (F/F 140K ) was increased and decreased by membrane depolarization and hyperpolarization, respectively. Fluorescent intensity signal was normalized by the maximum fluorescent intensity in the 140-mM K + HEPES-buffered solution (theoretically 0 mV). [Ca 2+ ] cyt (F 340 /F 380 ) was measured using the Ca 2+ -sensitive fluorescent indicator, fura-2/AM. ( A ) Time courses of the membrane potential in IPAH-PASMCs transfected with control ( n = 115), KCNK1 ( n = 131), or KCNK2 ( n = 98) siRNA before and after the perfusion with 140 mM K + HEPES-buffered solution. ( B ) Summarized data of the resting membrane potential in control ( n = 115), KCNK1 ( n = 131), or KCNK2 ( n = 98) siRNA-treated IPAH-PASMCs. The resting membrane potential was defined as the average value of F/F 140K for 5 min before the perfusion with 140 mM K + HEPES-buffered solution. ( C ) Resting [Ca 2+ ] cyt levels in IPAH-PASMCs transfected with control ( n = 73), KCNK1 ( n = 63), or KCNK2 ( n = 48) siRNA. ( D ) Summarized data of the resting [Ca 2+ ] cyt in control ( n = 73), KCNK1 ( n = 63), or KCNK2 ( n = 48) siRNA-treated IPAH-PASMCs. The resting [Ca 2+ ] cyt was defined as the average value of F 340 /F 380 for 5 min after the beginning of the experiment. Data are presented as means ± S.E. *** p < 0.001 vs. control siRNA (Scheffé's test following ANOVA).

Article Snippet: The membrane was blocked with Tris-buffered saline containing bovine serum albumin (5%) and Tween 20 (0.1%; MilliporeSigma) at room temperature (25°C) for 3 h and then treated with a primary antibody for KCNK1 (1:800; APC-110), KCNK2 (1:800; APC-047), KCNK3 (1:800; APC-024), KCNK6 (1:800; APC-040, Alomone Labs, Jerusalem, Israel), JNK (1:1000; #9252), or phospho ( p )-JNK (1:1000; #4668, Cell Signaling Technology, Danvers, MA, USA) at 4°C for 18 h. Immunoblotted membranes were then exposed to an anti-rabbit HRP-conjugated IgG secondary antibody (1:5000; #170-6515, Bio-Rad Laboratories, Hercules, CA, USA) at room temperature for 1 h. Blotting signals were detected using an ImmunoStar LD reagent (Fujifilm Wako Pure Chemical) and observed with the Imager 600 system (GE HealthCare Technologies, Chicago, IL, USA).

Techniques: Membrane, Knockdown, Transfection, Control

Journal: Frontiers in Cardiovascular Medicine

Article Title: Up-regulated expression of two-pore domain K + channels, KCNK1 and KCNK2, is involved in the proliferation and migration of pulmonary arterial smooth muscle cells in pulmonary arterial hypertension

doi: 10.3389/fcvm.2024.1343804

Figure Lengend Snippet: Effects of KCNK1 and KCNK2 channel knockdown on the phosphorylation of JNK in IPAH-PASMCs. The expression and phosphorylation levels of JNK in normal- and IPAH-PASMCs and the effects of the siRNA knockdown of KCNK1 and KCNK2 channels were examined by Western blotting. ( A ) The phosphorylation levels of JNK in normal- and IPAH-PASMCs ( n = 6). Protein expression was normalized to that of β-actin and normal-PASMCs. ( B ) The effects of the siRNA knockdown of KCNK1 channels on the phosphorylation levels of JNK in IPAH-PASMCs ( n = 6). Protein expression was normalized to that of β-actin and control siRNA. ( C ) The effects of the siRNA knockdown of KCNK2 channels on the phosphorylation levels of JNK in IPAH-PASMCs ( n = 6). Protein expression was normalized to that of β-actin and control siRNA. Data are presented as means ± S.E. ** p < 0.01, ** p < 0.01 vs. normal-PASMCs or control siRNA (Mann–Whitney U test).

Article Snippet: The membrane was blocked with Tris-buffered saline containing bovine serum albumin (5%) and Tween 20 (0.1%; MilliporeSigma) at room temperature (25°C) for 3 h and then treated with a primary antibody for KCNK1 (1:800; APC-110), KCNK2 (1:800; APC-047), KCNK3 (1:800; APC-024), KCNK6 (1:800; APC-040, Alomone Labs, Jerusalem, Israel), JNK (1:1000; #9252), or phospho ( p )-JNK (1:1000; #4668, Cell Signaling Technology, Danvers, MA, USA) at 4°C for 18 h. Immunoblotted membranes were then exposed to an anti-rabbit HRP-conjugated IgG secondary antibody (1:5000; #170-6515, Bio-Rad Laboratories, Hercules, CA, USA) at room temperature for 1 h. Blotting signals were detected using an ImmunoStar LD reagent (Fujifilm Wako Pure Chemical) and observed with the Imager 600 system (GE HealthCare Technologies, Chicago, IL, USA).

Techniques: Knockdown, Phospho-proteomics, Expressing, Western Blot, Control, MANN-WHITNEY

Journal: Advanced Functional Materials

Article Title: Remotely Actuated Magnetic Nanocarpets for Bone Tissue Engineering: Non‐Invasive Modulation of Mechanosensitive Ion Channels for Enhanced Osteogenesis

doi: 10.1002/adfm.202201311

Figure Lengend Snippet: Figure 1. Schematic of the synthesis of TREK1 and Piezo1 functionalized GOMNPs.

Article Snippet: The prepared GOMNPs were functionalized with TREK1 antibody (Almone labs, APC-047, Israel) and Piezo1 polyclonal antibody (Proteintech, UK) as described elsewhere[13] and hereby called as T-GOMPs and P-GOMNPs respectively.

Techniques:

Journal: Advanced Functional Materials

Article Title: Remotely Actuated Magnetic Nanocarpets for Bone Tissue Engineering: Non‐Invasive Modulation of Mechanosensitive Ion Channels for Enhanced Osteogenesis

doi: 10.1002/adfm.202201311

Figure Lengend Snippet: Figure 5. Concentration dependent CCK-8 biocompatibility assay of A) GO-MNPs and B) Piezo1 and TREK1 tagged GO-MNPs and live/dead staining (FDA/PI) showing the viability of MG63 cells after 72 h with C) Control, D) Piezo1-GOMNPs, and E) TREK1-GOMNPs respectively (scale bar 150 µm).

Article Snippet: The prepared GOMNPs were functionalized with TREK1 antibody (Almone labs, APC-047, Israel) and Piezo1 polyclonal antibody (Proteintech, UK) as described elsewhere[13] and hereby called as T-GOMPs and P-GOMNPs respectively.

Techniques: Concentration Assay, CCK-8 Assay, Staining, Control

Journal: Advanced Functional Materials

Article Title: Remotely Actuated Magnetic Nanocarpets for Bone Tissue Engineering: Non‐Invasive Modulation of Mechanosensitive Ion Channels for Enhanced Osteogenesis

doi: 10.1002/adfm.202201311

Figure Lengend Snippet: Figure 6. Prussian blue staining shows the concentration dependent intracellular localization of TREK1-GOMNPs in MG63 cells, A) Control cells, B) 5 µg mL−1, C) 10 µg mL−1, D) 15 µg mL−1, and E) 25 µg mL−1 of GOMNPs (scale bar 20 µm).

Article Snippet: The prepared GOMNPs were functionalized with TREK1 antibody (Almone labs, APC-047, Israel) and Piezo1 polyclonal antibody (Proteintech, UK) as described elsewhere[13] and hereby called as T-GOMPs and P-GOMNPs respectively.

Techniques: Staining, Concentration Assay, Control

Journal: Advanced Functional Materials

Article Title: Remotely Actuated Magnetic Nanocarpets for Bone Tissue Engineering: Non‐Invasive Modulation of Mechanosensitive Ion Channels for Enhanced Osteogenesis

doi: 10.1002/adfm.202201311

Figure Lengend Snippet: Figure 7. Immunocytochemistry imaging of MG63 cell lines with antibodies against A) TREK- and C) Piezo1 1 (green = TREK1/Piezo channel expres- sions; blue = DAPI). Control cells without secondary antibodies B) TREK1 and D) Piezo1. F) Immunocytochemistry imaging of TREK1 functionalized fluorescent GOMNPs demonstrating targeted intracellular binding E) compared to the control group pretreated with TREK1 blocking peptide, H) Piezo1 functionalized fluorescent GOMNPs G) compared to the control group pretreated with Piezo 1 antibodies (scale bar 150 µm).

Article Snippet: The prepared GOMNPs were functionalized with TREK1 antibody (Almone labs, APC-047, Israel) and Piezo1 polyclonal antibody (Proteintech, UK) as described elsewhere[13] and hereby called as T-GOMPs and P-GOMNPs respectively.

Techniques: Immunocytochemistry, Imaging, Control, Binding Assay, Blocking Assay

Journal: Advanced Functional Materials

Article Title: Remotely Actuated Magnetic Nanocarpets for Bone Tissue Engineering: Non‐Invasive Modulation of Mechanosensitive Ion Channels for Enhanced Osteogenesis

doi: 10.1002/adfm.202201311

Figure Lengend Snippet: Figure 8. Osteogenic differentiation potential of TREK1-GOMNPs and Piezo-GOMNPs with and without MICA treatment. A) ALP enzymatic activity of MG63 cells under MICA on day 7 and 14, B) Digital images of ALP stained well plates under MICA on day 7 and 14 and C) Alizarin red calcium quantifica- tion on day 14 and 21 respectively and D) optical microscopic images of Alizarin red-stained MG63 cells under MICA (scale bar 50 µm), qPCR analysis of expression of E) RUNX2, F) OCN, G) ALP, and H) COL1A1 with Piezo1/TREK1-GO-MNPs with/without MICA on days 7 and 14. Data represented as mean ± standard deviation (n = 3) and student’s t-test or one way ANOVA test was performed for comparison between two groups or among multiple groups respectively and statistically significant differences were marked with * for p < 0.05, **for p < 0.01, and ***for p < 0.001.

Article Snippet: The prepared GOMNPs were functionalized with TREK1 antibody (Almone labs, APC-047, Israel) and Piezo1 polyclonal antibody (Proteintech, UK) as described elsewhere[13] and hereby called as T-GOMPs and P-GOMNPs respectively.

Techniques: Activity Assay, Staining, Expressing, Standard Deviation, Comparison

Journal: Advanced Functional Materials

Article Title: Remotely Actuated Magnetic Nanocarpets for Bone Tissue Engineering: Non‐Invasive Modulation of Mechanosensitive Ion Channels for Enhanced Osteogenesis

doi: 10.1002/adfm.202201311

Figure Lengend Snippet: Figure 9. Osteogenic differentiation potential of TREK1-GOMNPs and Piezo-GOMNPs with and without MICA treatment with Y201 MSCs. A) ALP enzy- matic activity of Y201 MSCs under MICA on days 7 and 14, B) optical microscopic images of ALP stained well plates under MICA on days 7 and 14, and C) optical microscopic images of Alizarin red-stained Y201 MSCs cells under MICA. Data represented as mean ± standard deviation (n = 3) and one way ANOVA test was performed and statistically significant differences are marked with * for p < 0.05, **for p < 0.01, and ***for p < 0.001 (scale bar 50 µm).

Article Snippet: The prepared GOMNPs were functionalized with TREK1 antibody (Almone labs, APC-047, Israel) and Piezo1 polyclonal antibody (Proteintech, UK) as described elsewhere[13] and hereby called as T-GOMPs and P-GOMNPs respectively.

Techniques: Activity Assay, Staining, Standard Deviation