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(Journal of Leukocyte Biology. 2001;69:825-830.)
© 2001 by Society for Leukocyte Biology

Sulfhydryl-2 domain-containing protein tyrosine phosphatase-1 is not a negative regulator of interleukin-4 signaling in murine mast cells

Division of Pulmonary Medicine, Allergy, and Clinical Immunology, Department of Pediatrics, Children’s Hospital Medical Center, Cincinnati, Ohio

Correspondence: Gurjit K. Khurana Hershey, M.D., Ph.D., Division of Pulmonary Medicine, Allergy, and Clinical Immunology, Children’s Hospital Medical Center, 3333 Burnet Ave., Cincinnati OH 45229. E-mail: Gurjit.Hershey{at}chmcc.org

Sulfhydryl-2 domain-containing tyrosine phosphatase-1 (SHP-1) has an important role in the negative regulation of many receptors including the interleukin (IL)-4 receptor. Motheaten mice (me/me) have a homozygous mutation in SHP-1 and do not possess functional SHP-1. Pre-B-cell lines derived from me/me mice have been reported to display prolonged IL-4-dependent activation of signal transducer and activator of transcription-6 (Stat6). We evaluated IL-4-dependent Stat6 activation and Fc receptor 1 (FcRI) modulation in bone marrow-derived mast cells (BMMCs) from me/me and wild-type mice. IL-4 down-regulated FcRI expression in wild-type BMMCs but had no effect on FcRI expression in me/me BMMCs. Furthermore, me/me mast cells did not exhibit enhanced or prolonged IL-4-induced Stat6 activation compared with wild-type cells, indicating that mast cells possess alternative tyrosine phosphatases that are responsible for down-regulating Stat6 or can substitute for SHP-1. Thus, SHP-1 is not a negative regulator of IL-4 signaling in BMMCs. These results demonstrate the complexity and cellular specificity of these signaling pathways and indicate a previously unrecognized role for SHP-1 in murine mast cells.

Key Words: mast cells/basophils • protein kinases/phosphatases • signal transduction • cytokine receptors

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