+ Site Statistics
+ Search Articles
+ PDF Full Text Service
How our service works
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ Translate
+ Recently Requested

Temperature acclimation in the common carp force velocity characteristics and myosin subunit composition of slow muscle fibers



Temperature acclimation in the common carp force velocity characteristics and myosin subunit composition of slow muscle fibers



Journal of Experimental Biology 155: 291-304



Live slow fibre bundles were isolated from the superficial region of the pectoral fin abductor superficialis muscle of common carp (Cyprinus carpio L.) acclimated to either 8 or 20.degree. C. The maximum tetanic tension (P0) fibre bundles was similar when measured at the acclimation temperature of each group. However, at 8.degree. C, P0 was significantly higher in 8.degree. C- than in 20.degree. C-acclimated fish (202 .+-. 8 versus 153 .+-. 4 kN m-2, respectively). For isometric tetani at 8.degree. C, the times to 50% peak force and from peak force to 50% relaxation were 15-20% faster in preparations from cold- than from warm-acclimated carp. Force-velocity (P-V) curves were fitted using a hyperbolic-linear equation. The curvature of the P-V relationship was found to be independent of acclimation temperature. Unloaded contraction velocity (Vmax) was 17% higher at 8.degree. C in fibres from fish acclimated to 8.degree. than in fish acclimated to 20.degree. C (1.18 .+-. 0.04 and 0.98 .+-. 0.04 muscle lengths s-1, respectively). Calculated values for maximum power output at 8.degree. C were 26.5 W kg-1 for cold-acclimated and 18.0 W kg-1 for warm-acclimated fish. Native myosin was purified from isolated fibre bundles using sodium pyrophosphate gel electrophoresis. The mobility of myosin hevy chains on 8% SDS-PAGE gels was similar for both acclimation groups. Myosin light chain subunits were separated on 15% SDS-PAGE gels. Fibre bundles from warm-acclimated fish contained almost exclusively slow myosin light chains (LC12 and LC2s). Preparations from cold-acclimated fish contained a significant proportion of fast myosin light chains (LC1f and LC2f) in addition to LC1s and LC2s. Histochemical studies revealed no differences in the fibre composition of preparations from warm- and cold-acclimated fish: both contained an average of 3% fast oxidative fibres in addition to slow fibres. It is concluded that cold-acclimation results in modest improvements in the contractile performance of slow muscle fibres at low temperatures. The mechanism may involve the expression of myosin light chain isoforms normally associated with faster-contracting fibre types.

Please choose payment method:






(PDF emailed within 1 workday: $29.90)

Accession: 007865793

Download citation: RISBibTeXText


Related references

Force velocity characteristics and metabolism of carp cyprinus carpio muscle fibers following temperature acclimation. Journal of Experimental Biology 119: 239-250, 1985

Force-velocity characteristics and metabolism of carp muscle fibres following temperature acclimation. Journal of Experimental Biology 119: 239-249, 1985

Effects of decreased muscle activity on the velocity of shortening and myosin isozyme composition of single fibers from mammalian fast and slow muscles. Biophysical Journal 49(2 Part 2): 422A, 1986

Skinned single fibers from chicken slow muscle velocity of shortening maximum contractile velocity myosin isozymes and developmental implications. Biophysical Journal 49(2 Part 2): 267A, 1986

Study on the mechanism of low temperature adaptation in fish. 2. Effects of acclimation temperature on fatty acid composition and cholesterol content in mitochondrial membranes of muscle tissue of the grass carp and mud carp. Journal of South China Agricultural University 12(Suppl.): 45-49, 1991

Multiple isoforms of myosin light chain 1 in pig diaphragm slow fibers: correlation with maximal shortening velocity and force generation. Archives of Biochemistry and Biophysics 456(2): 112-118, 2006

Plasticity of myosin heavy chain mRNA expression with temperature acclimation is gradually acquired during ontogeny in the common carp. Comparative Biochemistry & Physiology Part A Molecular & Integrative Physiology 126A(Suppl 1): S30, 2000

Force velocity relation of isolated twitch and slow muscle fibers. Acta Physiologica Scandinavica Supplementum 440: 87, 1976

Plasticity of myosin heavy chain expression with temperature acclimation is gradually acquired during ontogeny in the common carp (Cyprinus carpio L.). Journal of Comparative Physiology B Biochemical Systemic and Environmental Physiology 171(4): 321-326, 2001

The force velocity relation of isolated twitch and slow muscle fibers of xenopus laevis. Journal of Physiology (Cambridge) 283: 501-522, 1978

Velocity, force, power, and Ca2+ sensitivity of fast and slow monkey skeletal muscle fibers. Journal of Applied Physiology 84(5): 1776-1787, 1998

Comparison of force and shortening velocity in fast and slow rabbit muscle fibers at different temperatures. Biofizika 59(5): 967-972, 2015