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Figure 6. Receptor expressions <t>of</t> <t>ALK2,</t> ALK4, ALK6, ALK5, ALK7, <t>BMPR-II</t> in pASC. Grouped representation of the respective receptor expression in the course of osteogenic differentiation (OM +/−BMP-2). From day 19, there is a significant induction of ALK 2, ALK 6, and ALK 5 with the addition of BMP-2. BMPR-II expression in the OM group decreased in OM and tended to stay increased under BMP-2 supplementation from day 19, but was not considered significant (* p ≤0.05, ** p ≤0.01; n = 6, BMP-2 450 ng/mL).
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Figure 6. Receptor expressions <t>of</t> <t>ALK2,</t> ALK4, ALK6, ALK5, ALK7, <t>BMPR-II</t> in pASC. Grouped representation of the respective receptor expression in the course of osteogenic differentiation (OM +/−BMP-2). From day 19, there is a significant induction of ALK 2, ALK 6, and ALK 5 with the addition of BMP-2. BMPR-II expression in the OM group decreased in OM and tended to stay increased under BMP-2 supplementation from day 19, but was not considered significant (* p ≤0.05, ** p ≤0.01; n = 6, BMP-2 450 ng/mL).
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Figure 6. Receptor expressions <t>of</t> <t>ALK2,</t> ALK4, ALK6, ALK5, ALK7, <t>BMPR-II</t> in pASC. Grouped representation of the respective receptor expression in the course of osteogenic differentiation (OM +/−BMP-2). From day 19, there is a significant induction of ALK 2, ALK 6, and ALK 5 with the addition of BMP-2. BMPR-II expression in the OM group decreased in OM and tended to stay increased under BMP-2 supplementation from day 19, but was not considered significant (* p ≤0.05, ** p ≤0.01; n = 6, BMP-2 450 ng/mL).
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FIGURE 4 The <t>processed</t> <t>BMP-10</t> CPLX binds robustly to BMP receptors whereas the unprocessed dimer shows no receptor interaction. Sensorgrams of SPR interaction studies of soluble BMP-10 GF, processed BMP-10 CPLX, and unprocessed BMP-10 dimer flowed over immobilized BMP receptors. Soluble analytes were injected onto immobilized <t>BMPRII,</t> ALK-1, and ENG at concentrations ranging from 0 to 80 nM. KDs were calculated from three independent experiments (N = 3).
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FIGURE 4 The <t>processed</t> <t>BMP-10</t> CPLX binds robustly to BMP receptors whereas the unprocessed dimer shows no receptor interaction. Sensorgrams of SPR interaction studies of soluble BMP-10 GF, processed BMP-10 CPLX, and unprocessed BMP-10 dimer flowed over immobilized BMP receptors. Soluble analytes were injected onto immobilized <t>BMPRII,</t> ALK-1, and ENG at concentrations ranging from 0 to 80 nM. KDs were calculated from three independent experiments (N = 3).
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FIGURE 4 The <t>processed</t> <t>BMP-10</t> CPLX binds robustly to BMP receptors whereas the unprocessed dimer shows no receptor interaction. Sensorgrams of SPR interaction studies of soluble BMP-10 GF, processed BMP-10 CPLX, and unprocessed BMP-10 dimer flowed over immobilized BMP receptors. Soluble analytes were injected onto immobilized <t>BMPRII,</t> ALK-1, and ENG at concentrations ranging from 0 to 80 nM. KDs were calculated from three independent experiments (N = 3).
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FIGURE 4 The <t>processed</t> <t>BMP-10</t> CPLX binds robustly to BMP receptors whereas the unprocessed dimer shows no receptor interaction. Sensorgrams of SPR interaction studies of soluble BMP-10 GF, processed BMP-10 CPLX, and unprocessed BMP-10 dimer flowed over immobilized BMP receptors. Soluble analytes were injected onto immobilized <t>BMPRII,</t> ALK-1, and ENG at concentrations ranging from 0 to 80 nM. KDs were calculated from three independent experiments (N = 3).
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FIG. 3. GDF9 pretreatment enhanced activin A-induced A- (A and B) and B (C and D)-mRNA level in hGL cells, effects attenuated in the presence of <t>BMPR2</t> ECD, a GDF9 antagonist. After 48 h preculture, hGL cells were cultured in low-serum media (containing only 0.5% FBS). hGL cells were preincubated with 100 ng/ml of GDF9 for 24 h in low-serum media before stimulation with 25 ng/ml of activin A. In neutralization experiments to render GDF9 inactive, 2 g/ml of BMPR2 ECD and 100 ng/ml of GDF9 were preincubated in low-serum media for 30 min before adding to cultured hGL cells. RNA of hGL cells were then isolated and mRNA contents were assessed by real-time PCR. Results were the means SEM from at least three sets of experiments (each from a separate patient), and in each set, measurements were made in triplicate. At each time point, means without a common letter are significantly different (P 0.05).
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Image Search Results


Figure 6. Receptor expressions of ALK2, ALK4, ALK6, ALK5, ALK7, BMPR-II in pASC. Grouped representation of the respective receptor expression in the course of osteogenic differentiation (OM +/−BMP-2). From day 19, there is a significant induction of ALK 2, ALK 6, and ALK 5 with the addition of BMP-2. BMPR-II expression in the OM group decreased in OM and tended to stay increased under BMP-2 supplementation from day 19, but was not considered significant (* p ≤0.05, ** p ≤0.01; n = 6, BMP-2 450 ng/mL).

Journal: Biology

Article Title: BMP-2-Driven Osteogenesis: A Comparative Analysis of Porcine BMSCs and ASCs and the Role of TGF-β and FGF Signaling.

doi: 10.3390/biology14060610

Figure Lengend Snippet: Figure 6. Receptor expressions of ALK2, ALK4, ALK6, ALK5, ALK7, BMPR-II in pASC. Grouped representation of the respective receptor expression in the course of osteogenic differentiation (OM +/−BMP-2). From day 19, there is a significant induction of ALK 2, ALK 6, and ALK 5 with the addition of BMP-2. BMPR-II expression in the OM group decreased in OM and tended to stay increased under BMP-2 supplementation from day 19, but was not considered significant (* p ≤0.05, ** p ≤0.01; n = 6, BMP-2 450 ng/mL).

Article Snippet: The respective conjugated antibodies were used for the expressions of ALK3 (Cat. No.: AF436), ALK 5 (Cat. No.: FAB5871), ALK6 (Cat. No.: FAB5051A), TGF-β2-RII (Cat. No.: FAB532P), ALK7 (Cat. No.: FAB77491A), ALK2 (Cat. No.: AF637), ALK4 (Cat. No.: MAB2221), and BMPR-II (Cat. No.: AF811) (by R&D Systems, Minneapolis, MN, USA), and the pASCs and pBMSCs were compared for their expressions of the specific surface antigens CD45 (Cat. No.: MCA1568GA, BioRad, Hercules, CA, USA), HLA-DR (human leukocyte antigen–antigen D-related surface molecule) (Cat. No.: MCA2314F, Bio-Rad, Hercules, CA, USA), CD29 (Cat. No.: 561,496, BD Pharmingen, Franklin Lakes, NJ, USA), CD79alpha (Bio-Rad, Cat. No.: MCA2538GA), CD14 (Cat. No.: MCA1568GA, Bio-Rad, Hercules, CA, USA), CD31 (Cat. No.: AF3387, R&D Systems, Minneapolis, MN, USA), CD105 (Cat. No.: NB110-58718APC, Novus Biologicals, Minneapolis, MN, USA), CD26 (, Cat. No.: NB600-552APC, Novus Biologicals, Minneapolis, MN, USA), CD73 (, Cat. No.: AF4488, R&D Systems, Minneapolis, MN, USA), CD90 (Cat. No.: 559,869, BD Pharmingen, Franklin Lakes, NJ, USA), CD34 (Cat. No.: 81289, abcam, Cambridge, UK), and CD44 (Cat. No.: 5531, BD Pharmingen, Franklin Lakes, NJ, USA).

Techniques: Expressing

FIGURE 4 The processed BMP-10 CPLX binds robustly to BMP receptors whereas the unprocessed dimer shows no receptor interaction. Sensorgrams of SPR interaction studies of soluble BMP-10 GF, processed BMP-10 CPLX, and unprocessed BMP-10 dimer flowed over immobilized BMP receptors. Soluble analytes were injected onto immobilized BMPRII, ALK-1, and ENG at concentrations ranging from 0 to 80 nM. KDs were calculated from three independent experiments (N = 3).

Journal: The FASEB Journal

Article Title: Prodomain processing controls BMP‐10 bioactivity and targeting to fibrillin‐1 in latent conformation

doi: 10.1096/fj.202401694r

Figure Lengend Snippet: FIGURE 4 The processed BMP-10 CPLX binds robustly to BMP receptors whereas the unprocessed dimer shows no receptor interaction. Sensorgrams of SPR interaction studies of soluble BMP-10 GF, processed BMP-10 CPLX, and unprocessed BMP-10 dimer flowed over immobilized BMP receptors. Soluble analytes were injected onto immobilized BMPRII, ALK-1, and ENG at concentrations ranging from 0 to 80 nM. KDs were calculated from three independent experiments (N = 3).

Article Snippet: To assess the binding affinity of BMP- 10 processing variants to BMP receptors, the human IgG1- Fc- fusion ectodomains of BMPRII (#811- BR- 100/CF, R&D Systems), ALK- 1 (#370- AL- 100/CF, R&D Systems) as well as ENG (#1097- EN- 025/CF, R&D Systems) were immobilized at 500 or 800 RUs on a CM5 chip via amine coupling.

Techniques: Injection

FIG. 3. GDF9 pretreatment enhanced activin A-induced A- (A and B) and B (C and D)-mRNA level in hGL cells, effects attenuated in the presence of BMPR2 ECD, a GDF9 antagonist. After 48 h preculture, hGL cells were cultured in low-serum media (containing only 0.5% FBS). hGL cells were preincubated with 100 ng/ml of GDF9 for 24 h in low-serum media before stimulation with 25 ng/ml of activin A. In neutralization experiments to render GDF9 inactive, 2 g/ml of BMPR2 ECD and 100 ng/ml of GDF9 were preincubated in low-serum media for 30 min before adding to cultured hGL cells. RNA of hGL cells were then isolated and mRNA contents were assessed by real-time PCR. Results were the means SEM from at least three sets of experiments (each from a separate patient), and in each set, measurements were made in triplicate. At each time point, means without a common letter are significantly different (P 0.05).

Journal: Endocrinology

Article Title: Growth differentiation factor 9 enhances activin a-induced inhibin B production in human granulosa cells.

doi: 10.1210/en.2009-0267

Figure Lengend Snippet: FIG. 3. GDF9 pretreatment enhanced activin A-induced A- (A and B) and B (C and D)-mRNA level in hGL cells, effects attenuated in the presence of BMPR2 ECD, a GDF9 antagonist. After 48 h preculture, hGL cells were cultured in low-serum media (containing only 0.5% FBS). hGL cells were preincubated with 100 ng/ml of GDF9 for 24 h in low-serum media before stimulation with 25 ng/ml of activin A. In neutralization experiments to render GDF9 inactive, 2 g/ml of BMPR2 ECD and 100 ng/ml of GDF9 were preincubated in low-serum media for 30 min before adding to cultured hGL cells. RNA of hGL cells were then isolated and mRNA contents were assessed by real-time PCR. Results were the means SEM from at least three sets of experiments (each from a separate patient), and in each set, measurements were made in triplicate. At each time point, means without a common letter are significantly different (P 0.05).

Article Snippet: In neutralization experiments to render GDF9 inactive, 2 g/ml of recombinant extracellular domain (ECD) fused to the Fc region of human IgG (receptor-ECD/Fc chimera) of human BMPR2 (BMPR2 ECD; R&D Systems, Minneapolis, MN) and The Endocrine Society.

Techniques: Cell Culture, Neutralization, Isolation, Real-time Polymerase Chain Reaction

FIG. 6. GDF9 pretreatment for 24 h transiently enhanced phosphorylation of Smad3 (Ser423/425) and Smad2 (Ser465/467) induced by activin A, effects that were neutralized by BMPR2 ECD. The culture and treatment conditions were similar to those in Fig. 3 except for the time scale of activin A treatment. Cell lysates were collected and assessed by Western blot analysis for the expression of phosphorylated Smad3 (Ser423/425) (A), phosphorylated Smad2 (Ser465/467) (B), and phosphorylated Smad2 (Ser245/250/255) (C). -Actin was used as the internal control. Results are representative of at least three sets of experiments (each from a separate patient).

Journal: Endocrinology

Article Title: Growth differentiation factor 9 enhances activin a-induced inhibin B production in human granulosa cells.

doi: 10.1210/en.2009-0267

Figure Lengend Snippet: FIG. 6. GDF9 pretreatment for 24 h transiently enhanced phosphorylation of Smad3 (Ser423/425) and Smad2 (Ser465/467) induced by activin A, effects that were neutralized by BMPR2 ECD. The culture and treatment conditions were similar to those in Fig. 3 except for the time scale of activin A treatment. Cell lysates were collected and assessed by Western blot analysis for the expression of phosphorylated Smad3 (Ser423/425) (A), phosphorylated Smad2 (Ser465/467) (B), and phosphorylated Smad2 (Ser245/250/255) (C). -Actin was used as the internal control. Results are representative of at least three sets of experiments (each from a separate patient).

Article Snippet: In neutralization experiments to render GDF9 inactive, 2 g/ml of recombinant extracellular domain (ECD) fused to the Fc region of human IgG (receptor-ECD/Fc chimera) of human BMPR2 (BMPR2 ECD; R&D Systems, Minneapolis, MN) and The Endocrine Society.

Techniques: Phospho-proteomics, Western Blot, Expressing, Control