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Volume 272, Number 2, Issue of January 10, 1997 pp. 1283-1290
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

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Interferon -dependent Induction of Human Intercellular Adhesion Molecule-1 Gene Expression Involves Activation of a Distinct STAT Protein Complex

(Received for publication, February 27, 1996, and in revised form, September 10, 1996)

From the Emory Skin Diseases Research Core Center, Department of Dermatology, Emory University School of Medicine, Atlanta, Georgia 30322

In response to interferon  (IFN), intercellular adhesion molecule-1 (ICAM-1) is expressed on human keratinocytes, a cell type that is critically involved in cutaneous inflammation. An ICAM-1 5 regulatory region palindromic response element, pIRE, has been shown to confer IFN-dependent transcription enhancement. By electrophoretic mobility shift assays (EMSA), pIRE forms a distinct complex with proteins from IFN-treated human keratinocytes, termed  response factor (GRF). Binding of GRF is tyrosine phosphorylation-dependent, and mutations of pIRE that disrupt the palindromic sequence or alter its spatial relationship abrogate GRF binding. Supershift EMSAs using antibodies to characterized STAT proteins suggest that GRF contains a Stat1-like protein; however, non-ICAM-1 IFN-responsive elements (REs) known to bind Stat1 homodimers fail to compete for GRF binding in EMSA, and pIRE does not cross-compete with these REs that complex with homodimeric stat1. The pIRE·GRF complex also displays a distinctly different electrophoretic mobility compared to that of IFNREs complexed to homodimeric Stat1. These findings indicate that a distinct complex containing a Stat1-like protein mediates IFN-induced ICAM-1 gene transcription and identifies a subset of IFN-responsive genes that appear to be regulated by this complex.

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