We wish to study the phosphorylation and dephosphorylation of various proteins of functionally different muscles in order to shed light on the molecular events of muscle contraction. Particular aspects of this long-range research aim are: Changes in the phosphate content of myosin light chains, tropomyosin, troponin-T, the 10,000 dalton acid chloroform-methanol soluble protein, and the proteins of the sarcoplasmic reticulum will be determined during a single isotonic or isometric tetanus of electrically stimulated frog muscle, electrical stimulation of the stretched muscle, and chemically induced contractures of the muscle. We plan to study the effect of denervation, neurotransmitters, and various drugs on the turnover of protein-bound phosphorus in skeletal muscle and the effect of inotropic agents on the phosphorylation of tropomyosin in perfused heart. We plan to compare the phosphorylation of tropomyosin in normal and hereditary dystrophic muscle. We plan to apply phosphorus nuclear magnetic resonance for the detection of phosphoryl tropomyosin and for the detection of changes in the environment of the tropomyosin-bound phosphate as a result of its interaction with the troponin complex and actomyosin. We plan to isolate the enzymes involved in the turnover of the tropomyosin-bound phosphate.

Agency
National Institute of Health (NIH)
Institute
National Institute of Arthritis and Musculoskeletal and Skin Diseases (NIAMS)
Type
Research Project (R01)
Project #
5R01AR034602-13
Application #
3156873
Study Section
Physiology Study Section (PHY)
Project Start
1984-09-01
Project End
1989-08-31
Budget Start
1987-09-01
Budget End
1988-08-31
Support Year
13
Fiscal Year
1987
Total Cost
Indirect Cost
Name
University of Illinois at Chicago
Department
Type
Overall Medical
DUNS #
121911077
City
Chicago
State
IL
Country
United States
Zip Code
60612
Barany, K; Barany, M; Giometti, C S (1995) Polyacrylamide gel electrophoretic methods in the separation of structural muscle proteins. J Chromatogr A 698:301-32
Barany, M; Barany, K (1993) Dissociation of relaxation and myosin light chain dephosphorylation in porcine uterine muscle. Arch Biochem Biophys 305:202-4
Barany, M; Barany, K (1993) Calponin phosphorylation does not accompany contraction of various smooth muscles. Biochim Biophys Acta 1179:229-33
Barany, M; Polyak, E; Barany, K (1992) Protein phosphorylation during the contraction-relaxation-contraction cycle of arterial smooth muscle. Arch Biochem Biophys 294:571-8
Barany, K; Polyak, E; Barany, M (1992) Protein phosphorylation in arterial muscle contracted by high concentration of phorbol dibutyrate in the presence and absence of Ca2+. Biochim Biophys Acta 1134:233-41
Barany, M; Rokolya, A; Barany, K (1991) Absence of calponin phosphorylation in contracting or resting arterial smooth muscle. FEBS Lett 279:65-8
Rokolya, A; Barany, M; Barany, K (1991) Modification of myosin light chain phosphorylation in sustained arterial muscle contraction by phorbol dibutyrate. Biochim Biophys Acta 1057:276-80
Barany, M; Rokolya, A; Barany, K (1991) Exchange of 20-kDa myosin light chain-bound phosphate during sustained contraction of arterial smooth muscle. Arch Biochem Biophys 287:199-203
Barany, K; Rokolya, A; Barany, M (1990) Stretch activates myosin light chain kinase in arterial smooth muscle. Biochem Biophys Res Commun 173:164-71
Barany, K; Rokolya, A; Barany, M (1990) Analysis of myosin light chain phosphopeptides in phorbol dibutyrate-contracted artery. Biochim Biophys Acta 1035:105-8

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