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Ignite Proteomics Announces Publication of Study Demonstrating Superiority of Protein Activation Analysis in Predicting Breast Cancer Therapy Response

Core Insights - The study emphasizes the importance of measuring activated proteins in the AKT–mTOR signaling pathway for predicting patient responses to targeted cancer therapies [2][3][11] Group 1: Study Overview - Ignite Proteomics LLC published a significant study in the British Journal of Cancer, highlighting the functional activation of the AKT–mTOR signaling axis in metastatic breast cancer [2] - The research indicates that direct assessment of protein activation is a superior method for predicting therapeutic outcomes compared to genomic profiling alone [3][6] Group 2: Key Findings - Enhanced clinical outcomes were observed through proteomic profiling, allowing for better identification of patients likely to benefit from endocrine therapy combined with a CDK4/6 inhibitor [5] - The study found that patients with functional activation of the AKT–mTOR signaling axis had significantly worse responses to standard first-line treatment with a CDK4/6 inhibitor [8] - There was no correlation between genomic mutations in key genes (PIK3CA, PTEN, AKT) and the activation status of corresponding proteins, indicating that genomic alterations do not reflect protein activity [8][9] Group 3: Implications for Cancer Treatment - The AKT–mTOR pathway is crucial for cell growth and survival, and its dysregulation is linked to various cancers, including metastatic breast cancer [6] - The findings support the integration of proteomic analysis into clinical practice to personalize cancer treatment based on functional protein activity [10][12] Group 4: Technological Advancements - Ignite Proteomics offers a clinically validated assay that measures both expression and activation levels of drug targets in breast tumors, providing actionable insights for oncologists [13][14] - The Reverse Phase Protein Array (RPPA)-based assay quantifies the phosphorylation status of proteins, focusing on protein function rather than genetic mutations [9][10]