Published online before print March 13, 2008
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* Manitoba Institute of Cell Biology and Department of Biochemistry and Medical Genetics, University of Manitoba, Winnipeg, Manitoba, Canada;
|| Institute of Experimental Dermatology, Münster, Germany;
Departments of Biochemistry, Physics and Chemistry, Center for Structural Biology, Vanderbilt University, Nashville, Tennessee, USA;
Department of Clinical Biochemistry, School of Medicine, Zahedan University of Medical Science, Zahedan, Iran;
Department of Internal Medicine I, University of Tübingen, Tübingen, Germany; and
¶ BioApplications Enterprises, Winnipeg, Manitoba, Canada
3Correspondence: BioApplications Enterprises, 34 Vanier Dr., Winnipeg, R2V 2NG, MB, Canada. E-mail: mjelos{at}gmail.com
The complex formed by two members of the S100 calcium-binding protein family, S100A8/A9, exerts apoptosis-inducing activity against various cells, especially tumor cells. Here, we present evidence that S100A8/A9 also has cell growth-promoting activity at low concentrations. Receptor of advanced glycation end product (RAGE) gene silencing and cotreatment with a RAGE-specific blocking antibody revealed that this activity was mediated via RAGE ligation. To investigate the signaling pathways, MAPK phosphorylation and NF-
B activation were characterized in S100A8/A9-treated cells. S100A8/A9 caused a significant increase in p38 MAPK and p44/42 kinase phosphorylation, and the status of stress-activated protein kinase/JNK phosphorylation remained unchanged. Treatment of cells with S100A8/A9 also enhanced NF-
B activation. RAGE small interfering RNA pretreatment abrogated the S100A8/A9-induced NF-
B activation. Our data indicate that S100A8/A9-promoted cell growth occurs through RAGE signaling and activation of NF-
B.
Key Words: NF-
B proliferation MRP8 MRP14 endokines S100/calgranulins cytotoxic peptides
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