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Originally published In Press as doi:10.1074/jbc.M105726200 on July 6, 2001

J. Biol. Chem., Vol. 276, Issue 36, 33938-33946, September 7, 2001
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Tumor Necrosis Factor-alpha -induced Adipose-related Protein (TIARP), a Cell-surface Protein That Is Highly Induced by Tumor Necrosis Factor-alpha and Adipose Conversion*

Marthe MoldesDagger , Françoise Lasnier, Xavier Gauthereau, Christophe Klein§, Jacques Pairault, Bruno Fève, and Anne-Marie Chambaut-Guérin

From the UMR 7079 CNRS and § INSERM IFR58, Université Pierre et Marie Curie, Centre de Recherche Biomédicale des Cordeliers, 15 rue de l'Ecole de Médecine, 75270 Paris Cedex 06, France

Tumor necrosis factor-alpha (TNFalpha ) is involved in the physiological and biological abnormalities found in two opposite metabolic situations: cachexia and obesity. In an attempt to identify novel genes and proteins that could mediate the effects of TNFalpha on adipocyte metabolism and development, we have used a differential display technique comparing 3T3-L1 cells exposed or not to the cytokine. We have isolated a novel adipose cDNA encoding a TNFalpha -inducible 470-amino acid protein termed TIARP, with six putative transmembrane regions flanked by a large amino-terminal and a short carboxyl-terminal domain, a structure reminiscent of channel and transporter proteins. Commitment into the differentiation process is required for cytokine responsiveness. The differentiation process per se is accompanied by a sharp emergence of TIARP mRNA transcripts, in parallel with the expression of the protein at the plasma membrane. Transcripts are present at high levels in white and brown adipose tissues, and are also detectable in liver, kidney, heart, and skeletal muscle. Whereas the biological function of TIARP is presently unknown, its pattern of expression during adipose conversion and in response to TNFalpha exposure as a transmembrane protein mainly located at the cell surface suggest that TIARP might participate in adipocyte development and metabolism and mediate some TNFalpha effects on the fat cell as a channel or a transporter.

* This work was supported in part by the Centre National de la Recherche Scientifique and the Université Paris VI.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.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AJ319746.

Dagger Recipient of a research fellowship from the Fondation pour la Recherche Médicale.

To whom correspondence should be addressed: UMR 7079 CNRS, Université Pierre et Marie Curie, Centre de Recherche Biomédicale des Cordeliers, 15 rue de l'Ecole de Médecine, 75270 Paris Cedex 06, France. Tel.: 33-1-42-34-68-93; Fax: 33-1-46-34-59-73; E-mail: guerin@bhdc.jussieu.fr.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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