[Changes in structure and functional properties of cytoskeletal elastic protein titin in dilated cardiomyopathy].
To elucidate the role of titin in the onset and development of dilated cardiomyopathy, the structure and functional properties of this protein from pathological myocardium (human left ventricle) were studied. By the use of SDS gel electrophoresis, a decrease in molecular weight of titin in dilated cardiomyopathy compared with norm (pig left ventricle) was revealed. The decrease correlated with the stage of the disease. A decrease in the length of molecules of pathological forms of titin was also found by electron microscopy, which confirms the results of electrophoresis tests. It was shown that, unlike titin from healthy muscle, pathological forms of titin do not activate but inhibit the main functional properties of control myosin: the actin-activated ATPase activity and its Ca2+ sensitivity. The direction of the changes in structure and functional properties of titin allows one to conclude about its contribution to the development of the pathology studied.
Makarenko
I V
IV
Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino, Moscow Region, 142290 Russia.
Shpagina
M D
MD
Vishnevskaia
Z I
ZI
Podlubnaia
Z A
ZA
D000251:Adenosine Triphosphatases / Q000737:chemistry; D000818:Animals; D002311:Cardiomyopathy, Dilated / Q000378:metabolism*; D064211:Connectin; D003598:Cytoskeletal Proteins / Q000737:chemistry* / Q000648:ultrastructure; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D008970:Molecular Weight; D009124:Muscle Proteins / Q000737:chemistry* / Q000648:ultrastructure; D009206:Myocardium / Q000737:chemistry*; D009218:Myosins / Q000737:chemistry; D011494:Protein Kinases / Q000737:chemistry* / Q000648:ultrastructure; D012518:Sarcomeres / Q000737:chemistry; D013552:Swine
D064211:Connectin; D003598:Cytoskeletal Proteins; D009124:Muscle Proteins; C577285:TTN protein, human; D011494:Protein Kinases; D000251:Adenosine Triphosphatases; D009218:Myosins