Molecular Muscle Physiology

Kontrahierende Muskelzelle

Head of the Group

Prof. Dr. Ingo Morano

31.1: Max Delbrück House (Hochbau)

Room 0114.1

Tel. 9406-2313

Fax. 9406-2277

Contact


Secretariat

Manuela Kaada

31.1: Max Delbrück House (Hochbau)

Room 0116

Tel. 2209

Fax. 2579

Contact


Contraction of all muscle types is elicited by increasing myoplasmic Ca2+ and interaction of Type II myosins with thin (actin) filaments. In striated muscle, Ca2+ bind to troponin C, which turn the thin filament “on”, allowing myosin force-generating actin interactions. In smooth muscle cells, Ca2+ bind to calmodulin which then activate myosin light chain kinase. Phosphorylation of the 20kDa light chain of smooth muscle myosins then allows forcegenerating actin interaction. We are studying the functional roles of subunits of key proteins of Ca2+ handling and force generation, i.e. the L-type Ca2+ channel and type II myosins in striated and smooth muscle. Any change of these proteins by mutation, differential gene expression, alternative splicing of the transcripts, or post-translational modification modulate striated and smooth muscle function. Understanding muscle contraction regulation at the molecular and functional levels provide the opportunity to develop new therapeutic strategies for the treatment of cardiovascular and skeletal muscle dysfunction.

 

Figure left: Contracting adult rat cardiomyocyte electrically stimulated at 1Hz