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Papers In Press, published online ahead of print June 16, 2000
J. Biol. Chem, 10.1074/jbc.M003495200
Submitted on April 25, 2000
Revised on June 2, 2000
Accepted on June 16, 2000

Cytokine signaling through Stat3 activates integrins, promotes adhesion, and induces growth arrest in the myeloid cell line 32D

David K. Wooten, Xiaoling Xie, David Bartos, Ruth A. Busche, Gregory D. Longmore, and Stephanie S. Watowich

Department of Immunology, The University of Texas MD Anderson Cancer Center, Houston, TX 77030

Corresponding Author: swatowic{at}mail.mdanderson.org

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 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 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.


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