» Articles » PMID: 2275960

Hydrostatic Compression in Glycerinated Rabbit Muscle Fibers

Overview
Journal Biophys J
Publisher Cell Press
Specialty Biophysics
Date 1990 Dec 1
PMID 2275960
Citations 17
Authors
Affiliations
Soon will be listed here.
Abstract

Glycerinated muscle fibers isolated from rabbit psoas muscle, and a number of other nonmuscle elastic fibers including glass, rubber, and collagen, were exposed to hydrostatic pressures of up to 10 MPa (100 Atm) to determine the pressure sensitivity of their isometric tension. The isometric tension of muscle fibers in the relaxed state (passive tension) was insensitive to increased pressure, whereas the muscle fiber tension in rigor state increased linearly with pressure. The tension of all other fiber types (except rubber) also increased with pressure; the rubber tension was pressure insensitive. The pressure sensitivity of rigor tension was 2.3 kN/m2/MPa and, in comparison with force/extension relation determined at atmospheric pressure, the hydrostatic compression in rigor muscle fibers was estimated to be 0.03% Lo/MPa. As reported previously, the active muscle fiber tension is depressed by increased pressure. The possible underlying basis of the different pressure-dependent tension behavior in relaxed, rigor, and active muscle is discussed.

Citing Articles

Effects of Hydrostatic-Pressure on Muscle Contraction: A Look Back on Some Experimental Findings.

Ranatunga K, Geeves M Int J Mol Sci. 2023; 24(5).

PMID: 36902460 PMC: 10003533. DOI: 10.3390/ijms24055031.


High hydrostatic pressure induces slow contraction in mouse cardiomyocytes.

Yamaguchi Y, Nishiyama M, Kai H, Kaneko T, Kaihara K, Iribe G Biophys J. 2022; 121(17):3286-3294.

PMID: 35841143 PMC: 9463647. DOI: 10.1016/j.bpj.2022.07.016.


Temperature Effects on Force and Actin⁻Myosin Interaction in Muscle: A Look Back on Some Experimental Findings.

Ranatunga K Int J Mol Sci. 2018; 19(5).

PMID: 29786656 PMC: 5983754. DOI: 10.3390/ijms19051538.


Structure and functional characteristics of rat's left ventricle cardiomyocytes under antiorthostatic suspension of various duration and subsequent reloading.

Ogneva I, Mirzoev T, Biryukov N, Veselova O, Larina I J Biomed Biotechnol. 2012; 2012:659869.

PMID: 23093854 PMC: 3470902. DOI: 10.1155/2012/659869.


Bacterial motility measured by a miniature chamber for high-pressure microscopy.

Nishiyama M, Kojima S Int J Mol Sci. 2012; 13(7):9225-9239.

PMID: 22942763 PMC: 3430294. DOI: 10.3390/ijms13079225.


References
1.
Gulati J, Babu A . Kinetics of force redevelopment in isolated intact frog fibers in solutions of varied osmolarity. Biophys J. 1986; 49(4):949-55. PMC: 1329546. DOI: 10.1016/S0006-3495(86)83723-7. View

2.
Coates J, Criddle A, Geeves M . Pressure-relaxation studies of pyrene-labelled actin and myosin subfragment 1 from rabbit skeletal muscle. Evidence for two states of acto-subfragment 1. Biochem J. 1985; 232(2):351-6. PMC: 1152886. DOI: 10.1042/bj2320351. View

3.
Horowits R, PODOLSKY R . The positional stability of thick filaments in activated skeletal muscle depends on sarcomere length: evidence for the role of titin filaments. J Cell Biol. 1987; 105(5):2217-23. PMC: 2114850. DOI: 10.1083/jcb.105.5.2217. View

4.
Geeves M, Ranatunga K . Tension responses to increased hydrostatic pressure in glycerinated rabbit psoas muscle fibres. Proc R Soc Lond B Biol Sci. 1987; 232(1267):217-26. DOI: 10.1098/rspb.1987.0070. View

5.
Goldman Y, McCray J, Ranatunga K . Transient tension changes initiated by laser temperature jumps in rabbit psoas muscle fibres. J Physiol. 1987; 392:71-95. PMC: 1192294. DOI: 10.1113/jphysiol.1987.sp016770. View