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Bioinorganic Chemistry and Applications
Volume 2010 (2010), Article ID 294169, 8 pages
http://dx.doi.org/10.1155/2010/294169
Research Article

The 33-35 Mutant -Domain Containing -Domain-Like Cluster Exhibits the Function of -Domain with Cluster in Human Growth Inhibitory Factor

1Institute of Biomedical Science, Fudan University, 220 Handan Road, Shanghai 200433, China
2Department of Chemistry, Fudan University, Shanghai 200433, China

Received 30 December 2009; Accepted 4 March 2010

Academic Editor: Spyros Perlepes

Copyright © 2010 Qingui Bao et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

Neuronal growth inhibitory factor (GIF), also known as metallothionein (metallothionein-3), impairs the survival and neurite formation of cultured neurons. It is known that the - domain-domain interaction of hGIF is crucial to the neuron growth inhibitory bioactivity although the exact mechanism is not clear. Herein, the (MT3)- (MT3) mutant and the hGIF-truncated 33-35 mutant were constructed, and their biochemical properties were characterized by pH titration, EDTA, and DTNB reactions. Their inhibitory activity toward neuron survival and neurite extension was also examined. We found that the 33-35 mutant -domain containing -domain-like cluster exhibits the function of -domain with cluster in hGIF. These results showed that the stability and solvent accessibility of the metal-thiolate cluster in -domain is very significant to the neuronal growth inhibitory activity of hGIF and also indicated that the particular primary structure of -domain is pivotal to domain-domain interaction in hGIF.