Both Ca2+ and Zn2+ are essential for S100A12 protein oligomerization and function.

ABSTRACT:

Background

Human S100A12 is a member of the S100 family of EF-hand calcium-modulated proteins that are associated with many diseases including cancer, chronic inflammation and neurological disorders. S100A12 is an important factor in host/parasite defenses and in the inflammatory response. Like several other S100 proteins, it binds zinc and copper in addition to calcium. Mechanisms of zinc regulation have been proposed for a number of S100 proteins e.g. S100B, S100A2, S100A7, S100A8/9. The interaction of S100 proteins with their targets is strongly dependent on cellular microenvironment.

Results

The aim of the study was to explore the factors that influence S100A12 oligomerization and target interaction. A comprehensive series of biochemical and biophysical experiments indic

SUBMITTER: Moroz OV 

PROVIDER: S-EPMC2686732 | biostudies-literature | 2009 Apr

REPOSITORIES: biostudies-literature