Prof. Dr. Michael Meyer

Forschungsmodulprojekt

Calcium-binding proteins

We are trying to understand cell biology and physiology of calcium-binding proteins. Calcium is a major and universal signaling molecule. Calcium-binding proteins help to shape intracellular calcium levels and thereby regulate many physiological processes, such as growth, migration and adhesion, differentiation, secretion and cell communication. They have also been implicated in degenerative diseases particularly of the nervous system.
Our focus is on EF hand proteins, a specific class of calcium-binding proteins.
Questions we address are (1) How is the intracellular localization of these proteins regulated? (2) Do they interact with other proteins in situ in cells? (3) What is the physiological and pathophysiological significance of specific localization and interaction? (4) What determines cytoprotective as opposed to cell damaging effects? (5) Are these proteins useful as disease biomarkers? (6) Is there a basis for their therapeutic application? Questions may change and new questions may be developed.

_{Selected literature:}

_{Celio, M. R. (1990). "Calbindin D-28k and parvalbumin in the rat nervous system." Neuroscience 35(2): 375-475.
Barski, J. J., et al. (2003). "Calbindin in cerebellar Purkinje cells is a critical determinant of the precision of motor coordination." J Neurosci 23(8): 3469-3477.
Schwaller, B., et al. (2002). "'New' functions for 'old' proteins: the role of the calcium-binding proteins calbindin D-28k, calretinin and parvalbumin, in cerebellar physiology. Studies with knockout mice." Cerebellum 1(4): 241-258.
Guo, Q., et al. (1998). "Calbindin D28k blocks the proapoptotic actions of mutant presenilin 1: reduced oxidative stress and preserved mitochondrial function." Proc Natl Acad Sci U S A 95(6): 3227-3232.
Christakos, S. and Y. Liu (2004). "Biological actions and mechanism of action of calbindin in the process of apoptosis." J Steroid Biochem Mol Biol 89-90(1-5): 401-404.
Schwaller, B. (2009). "The continuing disappearance of "pure" Ca2+ buffers." Cell Mol Life Sci 66(2): 275-300.}