Antibody Array Revealed PRL-3 Affects Protein Phosphorylation and Cytokine Secretion

作者：Yang, Yongyong; Lian, Shenyi; Meng, Lin; Qu, Like; Shou, Chengchao^*

来源：PLos One, 2017, 12(1): e0169665.

DOI：10.1371/journal.pone.0169665

• EPITHELIAL-MESENCHYMAL TRANSITION
• METASTASIS-ASSOCIATED PHOSPHATASE
• LYMPH-NODE METASTASIS
• KAPPA-B ACTIVATION
• TYROSINE-PHOSPHATASE
• REGENERATING LIVER-3
• COLORECTAL-CANCER
• SIGNALING PATHWAY
• MYELOID-LEUKEMIA
• CELL-MIGRATION

Phosphatase of regenerating liver 3 (PRL-3) promotes cancer metastasis and progression via increasing cell motility and invasiveness, however the mechanism is still not fully understood. Previous reports showed that PRL-3 increases the phosphorylation of many important proteins and suspected that PRL-3-enhanced protein phosphorylation may be due to its regulation on cytokines. To investigate PRL-3's impact on protein phosphorylation and cytokine secretion, we performed antibody arrays against protein phosphorylation and cytokines separately. The data showed that PRL-3 could enhance tyrosine phosphorylation and serine/threonine phosphorylation of diverse signaling proteins. Meanwhile, PRL-3 could affect the secretion of a subset of cytokines. Furthermore, we discovered the PRL-3-increased IL1 alpha secretion was regulated by NF-kappa B and Jak2-Stat3 pathways and inhibiting IL-1 alpha could reduce PRL-3-enhanced cell migration. Therefore, our result indicated that PRL-3 promotes protein phosphorylation by acting as an 'activator kinase' and consequently regulates cytokine secretion.

• 出版日期2017-1-9
• 单位北京大学