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Originally published In Press as doi:10.1074/jbc.M003495200 on June 16, 2000

J. Biol. Chem., Vol. 275, Issue 34, 26566-26575, August 25, 2000
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Cytokine Signaling through Stat3 Activates Integrins, Promotes Adhesion, and Induces Growth Arrest in the Myeloid Cell Line 32D*

David K. WootenDagger , Xiaoling XieDagger , David BartosDagger , Ruth A. BuscheDagger , Gregory D. Longmore§, and Stephanie S. WatowichDagger

From the Dagger  Department of Immunology, The University of Texas MD Anderson Cancer Center, Houston, Texas 77030 and § Departments of Medicine and Cell Biology, Washington University School of Medicine, St. Louis, Missouri 63110

Hematopoietic cell development and function is dependent on cytokines and on intercellular interactions with the microenvironment. Although the intracellular signaling pathways stimulated by cytokine receptors are well described, little is known about the mechanisms through which these pathways modulate hematopoietic cell adhesion events in the microenvironment. Here we show that cytokine-activated Stat3 stimulates the expression and function of cell surface adhesion molecules in the myeloid progenitor cell line 32D. We generated an erythropoietin receptor (EpoR) isoform (ER343/401-S3) that activates Stat3 rather than Stat5 by substituting the Stat3 binding/activation sequence motif from gp130 for the sequences surrounding tyrosines 343 and 401 in the receptor cytoplasmic region. Activation of Stat3 leads to homotypic cell aggregation, increased expression of intercellular adhesion molecule 1 (ICAM-1), CD18, and CD11b, and activation of signaling through CD18-containing integrins. Unlike the wild type EpoR, ER343/401-S3 is unable to support long term Epo-dependent proliferation in 32D cells. Instead, Epo-treated ER343/401-S3 cells undergo G1 arrest and express elevated levels of the cyclin-dependent kinase inhibitor p27Kip1. Sustained activation of Stat3 in these cells is required for their altered morphology and growth properties since constitutive SOCS3 expression abrogates homotypic cell aggregation, signaling through CD18-containing integrins, G1 arrest, and accumulation of p27Kip1. Collectively, our results demonstrate that cytokine-activated Stat3 stimulates the expression and function of cell surface adhesion molecules, indicating that a role for Stat3 is to regulate intercellular contacts in myeloid cells.

* This work was supported by National Institutes of Health (NCI) Grant CA 77447, Texas Higher Education Coordinating Board Grant 15-120, and a grant from the Gillson Longenbaugh Foundation (to S. S. W.) and by National Institutes of Health (NCI) Grant CA 75315 and American Heart Association Established Investigator Award 9940116N (to G. D. L.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: The University of Texas MD Anderson Cancer Center, Box 178, 1515 Holcombe Blvd., Houston, TX 77030. Tel.: 713-792-8376; Fax: 713-794-1322; E-mail: swatowic@mail.mdanderson.org.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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