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Medical AI Inquiry: You was designed to assist in medical decision-making based on the provided user questions. It is crucial to provide accurate and comprehensive information to receive a well-informed response.  Labels: OBJECTIVE, METHODS, RESULTS. Meshes: Adenocarcinoma, Animals, Bone Neoplasms, Breast Neoplasms, Cell Differentiation, Cell Line, Tumor, Culture Media, Conditioned, Interleukin-6, Interleukin-8, Mice, Neoplasm Proteins, Osteoclasts, Phosphorylation, Phosphotyrosine, Protein Isoforms, Protein Processing, Post-Translational, Protein Tyrosine Phosphatases, Proto-Oncogene Proteins, RANK Ligand, RAW 264.7 Cells, RNA Interference, RNA, Small Interfering, src-Family Kinases.
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Does low Molecular Weight Protein Tyrosine Phosphatase Slow Isoform Knockdown in MDA-MB-435 Cells decrease RAW 264.7 Osteoclastic Differentiation? Context: During the bone metastatic process, tumor cells and bone cells drive a vicious cycle stimulating growth and activity of each other. We here address how low molecular weight protein tyrosine phosphatase (LMW-PTP) could be involved in this process. We targeted LMW-PTP by siRNA and evaluated the effect of various soluble factors released to the culture medium by the MDA-MB-435 breast cancer cell line, in RAW 264.7 osteoclastogenesis. We showed that these soluble factors did not change RAW 264.7 osteoclastogenic potential. The knockdown of the LMW-PTP slow isoform decreased osteoclastogenesis of RAW 264.7, showing less active Src. The knockdown of LMW-PTP and its slow isoform decreased the release of IL-8 but not IL-6 in MDA-MB-435.
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The LMW-PTP slow isoform can be an important protein in bone metastatic disease, with a fundamental role in the interplay between tumor cells and osteoclasts, through the regulation of Src activity and IL-8 secretion. Final Decision: yes