title: Antibody Array Revealed PRL-3 Affects Protein Phosphorylation and Cytokine Secretion.
abstract: 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 IL-1α secretion was regulated by NF-κB and Jak2-Stat3 pathways and inhibiting IL-1α 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.
authors.affiliation: Key Laboratory of Carcinogenesis and Translational Research (Ministry of Education), Department of Biochemistry and Molecular Biology, Peking University Cancer Hospital & Institute, Beijing, China.
authors.forename: Yongyong
authors.initials: Y
authors.lastname: Yang
authors.affiliation: Key Laboratory of Carcinogenesis and Translational Research (Ministry of Education), Department of Biochemistry and Molecular Biology, Peking University Cancer Hospital & Institute, Beijing, China.|Key Laboratory of Carcinogenesis and Translational Research (Ministry of Education), Department of pathology, Peking University Cancer Hospital & Institute, Beijing, China.
authors.forename: Shenyi
authors.initials: S
authors.lastname: Lian
authors.affiliation: Key Laboratory of Carcinogenesis and Translational Research (Ministry of Education), Department of Biochemistry and Molecular Biology, Peking University Cancer Hospital & Institute, Beijing, China.
authors.forename: Lin
authors.initials: L
authors.lastname: Meng
authors.affiliation: Key Laboratory of Carcinogenesis and Translational Research (Ministry of Education), Department of Biochemistry and Molecular Biology, Peking University Cancer Hospital & Institute, Beijing, China.
authors.forename: Like
authors.initials: L
authors.lastname: Qu
authors.affiliation: Key Laboratory of Carcinogenesis and Translational Research (Ministry of Education), Department of Biochemistry and Molecular Biology, Peking University Cancer Hospital & Institute, Beijing, China.
authors.forename: Chengchao
authors.initials: C
authors.lastname: Shou
mesh_terms: D045744:Cell Line, Tumor; D002465:Cell Movement / Q000235:genetics; D016207:Cytokines / Q000235:genetics / Q000378:metabolism*; D015870:Gene Expression; D055785:Gene Knockdown Techniques; D006801:Humans; D053614:Janus Kinase 2 / Q000378:metabolism; D016328:NF-kappa B / Q000378:metabolism; D009363:Neoplasm Proteins / Q000235:genetics / Q000378:metabolism*; D010750:Phosphoproteins / Q000378:metabolism; D010766:Phosphorylation; D017027:Protein Tyrosine Phosphatases / Q000235:genetics / Q000378:metabolism*; D020543:Proteome; D040901:Proteomics / Q000379:methods; D015398:Signal Transduction
chemical_list: D016207:Cytokines; D016328:NF-kappa B; D009363:Neoplasm Proteins; D010750:Phosphoproteins; D020543:Proteome; C507924:JAK2 protein, human; D053614:Janus Kinase 2; C484730:PTP4A3 protein, human; D017027:Protein Tyrosine Phosphatases