promotes cell proliferation and affects glycolysis in breast cancer.

Phosphatase and tensin homolog (PTEN)-induced kinase 1 () is regarded as a tumor suppressor and plays an important role in cancer cell biology, while relatively few studies have examined in breast cancer, especially . The aims of this study were to investigate expression in different subtypes of breast cancer tissues and cell lines and explore the effect of protein on breast cancer. In these experiments, expression was investigated using the tissue microarray immunohistochemistry (TMA-IHC) method in 150 samples of breast cancer tissues with different subtypes, and strong staining of was significantly correlated with the histological grade of breast cancer ( = 0.015). In addition, messenger RNA (mRNA) displayed much higher expression levels in breast cancer cell lines than in MCF-10A breast epithelial cells. Moreover, proteomic data obtained by isobaric tags for relative and absolute quantification (iTRAQ) showed that deletion induced a distinct proteomic profile in MDA-MB-231 cells, and enrichment analysis showed that the differential proteins were concentrated mainly in energy metabolism-related pathways. Moreover, Seahorse XF analysis showed that knockout reduced the glycolytic ability of MDA-MB-231 cells. Our findings indicated that may be an indicator of malignancy in breast cancer and that it presents oncogenic properties in breast cancer, which raises another perspective for understanding the regulatory role of in breast cancer.