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Related Collections Immunobiology Signal Transduction Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Blood, 15 November 2001, Vol. 98, No. 10, pp. 3030-3034 IMMUNOBIOLOGY Protein tyrosine phosphatase C selectively inhibits interleukin-6- and interleukin- 10-induced JAK-STAT signaling Nobuhiro Tanuma, Hiroshi Shima, Koji Nakamura, and Kunimi Kikuchi From the Division of Biochemical Oncology and Immunology, Institute for Genetic Medicine, Hokkaido University, Sapporo, Japan. Protein tyrosine phosphatase (PTP)  (PTP) exists as 2 forms generated by alternative promoter usage. It has recently been reported that a cytosolic isoform of PTP (PTPC) when over-expressed in murine M1 myeloid cells inhibits interleukin-6 (IL-6)- and leukemia inhibitory factor-induced activation of Janus kinsases (JAKs), thereby suppressing STAT3 tyrosine phosphorylation and STAT3 signaling. This study characterizes an inhibitory action of PTPC on IL-6 signaling and also reveals that PTPC inhibitory activity is independent of other potential negative regulators, such as SHP-2 and SOCS family proteins. Furthermore, it analyzes the selectivity of PTPC action toward several cytokines. On IL-6 stimulation, expression of PTPC-DA, a catalytically inactive mutant of PTPC, results in an earlier onset of STAT3 tyrosine phosphorylation, suggesting different modes of action between PTPC and other negative regulators. In addition, the study shows PTPC-DA enhances activation of STAT1 by IL-6 as well. In terms of specificity to cytokines, over-expressed PTPC also inhibits IL-10-induced tyrosine phosphorylation of STAT3 in M1 cells, whereas PTPC does not affect either interferon-- and interferon--induced tyrosine phosphorylation of STATs or expression of STAT transcriptional targets. 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