Abstract

The aims of the program are to study the mechanism of contraction in cardia muscle. The focus is on fundamental properties, i.e., on the manner in whic force is generated and regulated. Several specific issues are to be investigated using complementary methodologies. In Project I, several ultrastructural features will be examined with optical microscopy and electron microscopy of quickly frozen specimens. In Project II, the molecular events attendant with Ca activation will be studied using a fluorescent probe, radioactively labelled tracers, and the electron microprobe. In Project III the mechanism underlying the influence of sarcomere length on myofilament sensitivity to calcium will be studied using mechanical and microprobe methods. Project IV will employ unique peptides to inhibit actomyosin interaction and thereby allow study o interaction between actin and myosin.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Heart, Lung, and Blood Institute (NHLBI)
Type
Research Program Projects (P01)
Project #
5P01HL031962-08
Application #
3098248
Study Section
Heart, Lung, and Blood Research Review Committee A (HLBA)
Project Start
1984-04-01
Project End
1994-06-30
Budget Start
1991-08-02
Budget End
1992-06-30
Support Year
8
Fiscal Year
1991
Total Cost
Indirect Cost

  Institution

Name
University of Washington
Department
Type
Schools of Medicine
DUNS #
135646524
City
Seattle
State
WA
Country
United States
Zip Code
98195

  Publications

Chase, P B; Denkinger, T M; Kushmerick, M J (1998) Effect of viscosity on mechanics of single, skinned fibers from rabbit psoas muscle. Biophys J 74:1428-38
deBeer, E L; Sontrop, A M; Kellermayer, M S et al. (1997) Actin-filament motion in the in vitro motility assay has a periodic component. Cell Motil Cytoskeleton 38:341-50
Wiseman, R W; Beck, T W; Chase, P B (1996) Effect of intracellular pH on force development depends on temperature in intact skeletal muscle from mouse. Am J Physiol 271:C878-86
Kellermayer, M S; Pollack, G H (1996) Rescue of in vitro actin motility halted at high ionic strength by reduction of ATP to submicromolar levels. Biochim Biophys Acta 1277:107-14
Hancock, W O; Martyn, D A; Huntsman, L L et al. (1996) Influence of Ca2+ on force redevelopment kinetics in skinned rat myocardium. Biophys J 70:2819-29
Kellermayer Jr, M S; Hinds, T R; Pollack, G H (1995) Persisting in vitro actin motility at nanomolar adenosine triphosphate levels: comparison of skeletal and cardiac myosins. Physiol Chem Phys Med NMR 27:167-78
Martyn, D A; Chase, P B (1995) Faster force transient kinetics at submaximal Ca2+ activation of skinned psoas fibers from rabbit. Biophys J 68:235-42
Chase, P B; Kushmerick, M J (1995) Effect of physiological ADP concentrations on contraction of single skinned fibers from rabbit fast and slow muscles. Am J Physiol 268:C480-9
Chase, P B; Martyn, D A; Hannon, J D (1994) Activation dependence and kinetics of force and stiffness inhibition by aluminiofluoride, a slowly dissociating analogue of inorganic phosphate, in chemically skinned fibres from rabbit psoas muscle. J Muscle Res Cell Motil 15:119-29
Martyn, D A; Chase, P B; Hannon, J D et al. (1994) Unloaded shortening of skinned muscle fibers from rabbit activated with and without Ca2+. Biophys J 67:1984-93

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