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J. Biol. Chem., Vol. 281, Issue 50, 38905-38917, December 15, 2006

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S100A16, a Novel Calcium-binding Protein of the EF-hand Superfamily^*

Emmanuel Sturchler, Jos A. Cox, Isabelle Durussel, Mirjam Weibel, and Claus W. Heizmann¹

From the Department of Pediatrics, Division of Clinical Chemistry and Biochemistry, University of Zurich, Steinwiesstrasse 75, 8032 Zurich, Switzerland and the Department of Biochemistry, University of Geneva, 1211 Geneva, Switzerland

S100A16 protein is a new and unique member of the EF-hand Ca²⁺-binding proteins. S100 proteins are cell- and tissue-specific and are involved in many intra- and extracellular processes through interacting with specific target proteins. In the central nervous system S100 proteins are implicated in cell proliferation, differentiation, migration, and apoptosis as well as in cognition. S100 proteins became of major interest because of their close association with brain pathologies, for example depression or Alzheimer's disease. Here we report for the first time the purification and biochemical characterization of human and mouse recombinant S100A16 proteins. Flow dialysis revealed that both homodimeric S100A16 proteins bind two Ca²⁺ ions with the C-terminal EF-hand of each subunit, the human protein exhibiting a 2-fold higher affinity. Trp fluorescence variations indicate conformational changes in the orthologous proteins upon Ca²⁺ binding, whereas formation of a hydrophobic patch, implicated in target protein recognition, only occurs in the human S100A16 protein. In situ hybridization analysis and immunohistochemistry revealed a widespread distribution in the mouse brain. Furthermore, S100A16 expression was found to be astrocyte-specific. Finally, we investigated S100A16 intracellular localization in human glioblastoma cells. The protein was found to accumulate within nucleoli and to translocate to the cytoplasm in response to Ca²⁺ stimulation.

Received for publication, June 16, 2006 , and in revised form, September 21, 2006.

^* This work was supported by the National Centers of Competence in Research (NCCR) on Neural Plasticity and Repair and the Swiss National Science Foundation (Grant 3100A0-101970). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed: Dept. of Pediatrics, Division of Clinical Chemistry and Biochemistry, University of Zurich, Steinwiesstrasse 75, 8032 Zurich, Switzerland. Tel.: 41-(44)-266-7541; Fax: 41-(44)-266-7169; E-mail: claus.heizmann{at}kispi.unizh.ch.

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