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Effect of a Bone Morphogenetic Protein-2-derived peptide on the expression of tumor marker ZNF217 in osteoblasts and MCF-7 cells.

ABSTRACT: Zinc Finger Protein 217 (ZNF217), a transcription factor and oncogene product, has been found to dysregulate Bone Morphogenetic Protein (BMP) signaling and induce invasion in breast tumors. In this study, the effect of BMP-2 or an active BMP-2 peptide, AISMLYLDEN, on the expression of ZNF217, BMP4 and CDK-inhibitor p21 gene, CDKN1A, was investigated in MCF-7 breast cancer cells. In parallel, the entire protein (BMP-2) as well as the aforementioned peptide were investigated in hDPSCs during osteogenic differentiation. The treatment of MCF-7 cancer cells with different concentrations of peptide AISMLYLDEN showed that the addition of 22.6 ng/ml was more effective in comparison to the other used concentrations. In particular, 48 h after treatment, CDKN1A and BMP4 mRNA levels were substantially increased in contrast to ZNF217 mRNA levels which were decreased. These results are strongly supported by BrdU assay that clearly indicated inhibition of cancer cell proliferation. Taken together, these results open ways for a concurrent use, at appropriate concentrations, of the peptide AISMLYLDEN during conventional therapeutic treatment in breast tumors with a metastatic tendency to the bones. Regarding the effect of the entire protein as well as its peptide on hDPSCs differentiation into osteocytes, the mRNA levels of osteocalcin, an osteogenic marker, showed that the peptide enhanced osteogenesis at a higher degree in comparison to the entire BMP-2 without however altering ZNF217, CDKN1A and BMP4 expression levels, which remained as expected of non-cancer cells.

SUBMITTER: Mantsou A

PROVIDER: S-EPMC8487976 | biostudies-literature |

REPOSITORIES: biostudies-literature

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Project description:Two experiments were conducted to study the effect of bone morphogenetic protein 2 (BMP2) or extracellular signal-regulated kinase 1 (ERK1) silencing on phosphorus (P) utilization and related parameters in primary broiler osteoblasts. Experiment 1 was carried out to select the most efficacious siRNAs against BMP2 or ERK1 for the subsequent experiment. In experiment 2, with or without the siRNA against BMP2 or ERK1, primary broiler osteoblasts were incubated in the medium supplemented with 0.0 or 2.0 mmol/L of P as NaH2PO4 for 12 days. The osteoblastic P utilization and related parameters were determined. The results showed that the si980 and si1003 were the most effective (P < 0.05) in inhibiting BMP2 and ERK1 expressions, respectively. The BMP2 silencing reduced (P < 0.004) the osteoblastic P retention rate, alkaline phosphatase (ALP) activity, BMP2 mRNA and protein expressions. Supplemental P increased (P = 0.0008) ALP activity. Significant interactions (P < 0.04) between the gene silencing and supplemental P level were observed in both mineralization formation and bone gal protein (BGP) content. The BMP2 silencing decreased (P < 0.05) mineralization formation at both 0.0 and 2.0 mmol/L of added P levels, but the decreased degree was greater at 2.0 mmol/L of added P level, while BMP2 silencing reduced (P < 0.05) BGP content at only 2.0 mmol/L of added P level. The ERK1 silencing decreased (P < 0.004) mineralization formation, ALP activity, BGP content, ERK1 mRNA, ERK1 and p-ERK1 protein expressions. Supplemental P increased (P < 0.03) mineralization formation, ALP activity, BGP content and p-ERK1 protein expression, but inhibited (P = 0.014) ERK1 protein expression. There was an interaction (P < 0.03) between the gene silencing and supplemental P level in the osteoblastic P retention rate. The ERK1 silencing decreased (P < 0.05) it regardless of 0.0 or 2.0 mmol/L of added P level, but the reduced degree was greater at 2.0 mmol/L of added P level. It was concluded that either BMP2 or ERK1 silencing suppressed P utilization, and thus either of them participated in regulating P utilization in primary broiler osteoblasts.

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Effect of a Bone Morphogenetic Protein-2-derived peptide on the expression of tumor marker ZNF217 in osteoblasts and MCF-7 cells.

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