Protein tyrosine phosphatase 1B (PTP1B) is dispensable for IgE-mediated cutaneous reaction in vivo

Ting Yang; Zhongping Xie; Hua Li; Lei Yue; Zheng Pang; Adam J. MacNeil; Michel L. Tremblay; Jin Tian Tang; Tong Jun Lin

doi:10.1016/j.cellimm.2016.05.005

Protein tyrosine phosphatase 1B (PTP1B) is dispensable for IgE-mediated cutaneous reaction in vivo

Ting Yang, Zhongping Xie, Hua Li, Lei Yue, Zheng Pang, Adam J. MacNeil, Michel L. Tremblay, Jin Tian Tang, Tong Jun Lin

Medicine

Medicine

Research output: Contribution to journal › Article › peer-review

4 Citations (Scopus)

Abstract

Mast cells play a critical role in allergic reactions. The cross-linking of FcεRI-bound IgE with multivalent antigen initiates a cascade of signaling events leading to mast cell activation. It has been well-recognized that cross linking of FcεRI mediates tyrosine phosphorylation. However, the mechanism involved in tyrosine dephosphorylation in mast cells is less clear. Here we demonstrated that protein tyrosine phosphatase 1B (PTP1B)-deficient mast cells showed increased IgE-mediated phosphorylation of the signal transducer and activator of transcription 5 (STAT5) and enhanced production of CCL9 (MIP-1γ) and IL-6 in IgE-mediated mast cells activation in vitro. However, IgE-mediated calcium mobilization, β-hexaosaminidase release (degranulation), and phosphorylation of IκB and MAP kinases were not affected by PTP1B deficiency. Furthermore, PTP1B deficient mice showed normal IgE-dependent passive cutaneous anaphylaxis and late phase cutaneous reactions in vivo. Thus, PTP1B specifically regulates IgE-mediated STAT5 pathway, but is redundant in influencing mast cell function in vivo.

Original language	English
Pages (from-to)	9-16
Number of pages	8
Journal	Cellular Immunology
Volume	306-307
DOIs	https://doi.org/10.1016/j.cellimm.2016.05.005
Publication status	Published - Aug 1 2016

Bibliographical note

Funding Information:
This work is supported by a grant from Natural Science Foundation of China (81471564) to TJL and a grant from Canadian Institutes of Health Research to TJL. MLT is the holder of the Jeanne and Jean-Louis Levesque Chair in Cancer Research. We would like to thank Fang Liu for her technical assistance with isolation of bone-marrow derived mast cells and IgE-dependent cutaneous reaction studies in vivo.

Publisher Copyright:
© 2016 Elsevier Inc.

ASJC Scopus Subject Areas

Immunology

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10.1016/j.cellimm.2016.05.005

Cite this

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title = "Protein tyrosine phosphatase 1B (PTP1B) is dispensable for IgE-mediated cutaneous reaction in vivo",

abstract = "Mast cells play a critical role in allergic reactions. The cross-linking of FcεRI-bound IgE with multivalent antigen initiates a cascade of signaling events leading to mast cell activation. It has been well-recognized that cross linking of FcεRI mediates tyrosine phosphorylation. However, the mechanism involved in tyrosine dephosphorylation in mast cells is less clear. Here we demonstrated that protein tyrosine phosphatase 1B (PTP1B)-deficient mast cells showed increased IgE-mediated phosphorylation of the signal transducer and activator of transcription 5 (STAT5) and enhanced production of CCL9 (MIP-1γ) and IL-6 in IgE-mediated mast cells activation in vitro. However, IgE-mediated calcium mobilization, β-hexaosaminidase release (degranulation), and phosphorylation of IκB and MAP kinases were not affected by PTP1B deficiency. Furthermore, PTP1B deficient mice showed normal IgE-dependent passive cutaneous anaphylaxis and late phase cutaneous reactions in vivo. Thus, PTP1B specifically regulates IgE-mediated STAT5 pathway, but is redundant in influencing mast cell function in vivo.",

author = "Ting Yang and Zhongping Xie and Hua Li and Lei Yue and Zheng Pang and MacNeil, {Adam J.} and Tremblay, {Michel L.} and Tang, {Jin Tian} and Lin, {Tong Jun}",

note = "Funding Information: This work is supported by a grant from Natural Science Foundation of China (81471564) to TJL and a grant from Canadian Institutes of Health Research to TJL. MLT is the holder of the Jeanne and Jean-Louis Levesque Chair in Cancer Research. We would like to thank Fang Liu for her technical assistance with isolation of bone-marrow derived mast cells and IgE-dependent cutaneous reaction studies in vivo. Publisher Copyright: {\textcopyright} 2016 Elsevier Inc.",

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doi = "10.1016/j.cellimm.2016.05.005",

language = "English",

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AU - Yang, Ting

AU - Xie, Zhongping

AU - Li, Hua

AU - Yue, Lei

AU - Pang, Zheng

AU - MacNeil, Adam J.

AU - Tremblay, Michel L.

AU - Tang, Jin Tian

AU - Lin, Tong Jun

N1 - Funding Information: This work is supported by a grant from Natural Science Foundation of China (81471564) to TJL and a grant from Canadian Institutes of Health Research to TJL. MLT is the holder of the Jeanne and Jean-Louis Levesque Chair in Cancer Research. We would like to thank Fang Liu for her technical assistance with isolation of bone-marrow derived mast cells and IgE-dependent cutaneous reaction studies in vivo. Publisher Copyright: © 2016 Elsevier Inc.

PY - 2016/8/1

Y1 - 2016/8/1

N2 - Mast cells play a critical role in allergic reactions. The cross-linking of FcεRI-bound IgE with multivalent antigen initiates a cascade of signaling events leading to mast cell activation. It has been well-recognized that cross linking of FcεRI mediates tyrosine phosphorylation. However, the mechanism involved in tyrosine dephosphorylation in mast cells is less clear. Here we demonstrated that protein tyrosine phosphatase 1B (PTP1B)-deficient mast cells showed increased IgE-mediated phosphorylation of the signal transducer and activator of transcription 5 (STAT5) and enhanced production of CCL9 (MIP-1γ) and IL-6 in IgE-mediated mast cells activation in vitro. However, IgE-mediated calcium mobilization, β-hexaosaminidase release (degranulation), and phosphorylation of IκB and MAP kinases were not affected by PTP1B deficiency. Furthermore, PTP1B deficient mice showed normal IgE-dependent passive cutaneous anaphylaxis and late phase cutaneous reactions in vivo. Thus, PTP1B specifically regulates IgE-mediated STAT5 pathway, but is redundant in influencing mast cell function in vivo.

AB - Mast cells play a critical role in allergic reactions. The cross-linking of FcεRI-bound IgE with multivalent antigen initiates a cascade of signaling events leading to mast cell activation. It has been well-recognized that cross linking of FcεRI mediates tyrosine phosphorylation. However, the mechanism involved in tyrosine dephosphorylation in mast cells is less clear. Here we demonstrated that protein tyrosine phosphatase 1B (PTP1B)-deficient mast cells showed increased IgE-mediated phosphorylation of the signal transducer and activator of transcription 5 (STAT5) and enhanced production of CCL9 (MIP-1γ) and IL-6 in IgE-mediated mast cells activation in vitro. However, IgE-mediated calcium mobilization, β-hexaosaminidase release (degranulation), and phosphorylation of IκB and MAP kinases were not affected by PTP1B deficiency. Furthermore, PTP1B deficient mice showed normal IgE-dependent passive cutaneous anaphylaxis and late phase cutaneous reactions in vivo. Thus, PTP1B specifically regulates IgE-mediated STAT5 pathway, but is redundant in influencing mast cell function in vivo.

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Protein tyrosine phosphatase 1B (PTP1B) is dispensable for IgE-mediated cutaneous reaction in vivo

Abstract

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