V. Pelouch et M. Vornanen, EFFECTS OF THERMAL-ACCLIMATION ON VENTRICLE SIZE, PROTEIN-COMPOSITION, AND CONTRACTILE PROPERTIES OF CRUCIAN CARP HEART, Journal of thermal biology, 21(1), 1996, pp. 1-9
1. The aim of the study was to find out how thermal adaptation affects
ventricular size, protein composition and functional properties of th
e contractile machinery of the fish heart. For that purpose crucian ca
rp (Carassius carassius L.) were acclimated in laboratory to 2 degrees
and 22 degrees C for three months. 2. Long-term acclimation to 2 degr
ees increased-the relative ventricular mass by 86% in comparison to fi
sh acclimated to 22 degrees C. 3. The cold-induced cardiac enlargement
was associated with a remodelling of protein composition of the ventr
icular muscle. Total concentration of proteins, including non-collagen
ous proteins of myocytes and collagenous proteins of extracellular mat
rix, was increased from 96 to 109 mg g(-1) (p < 0.05) tissue wet weigh
t. The increase was exclusively due to increased concentration of coll
agenous proteins, since concentration of sarcoplasmic proteins was unc
hanged and concentration of myofibrillar proteins was reduced. Total h
ydroxyproline concentration was lower in cold-acclimated animals; the
elevated concentration of collagenous proteins is, therefore, not due
to collagen but other proteins of the extracellular matrix. Thus, accl
imation to cold increases protein concentration of extracellular matri
x but reduces protein concentration of the myocytes in crucian carp he
art. 4. Effects of caffeine (5 mM) on the contractile properties of ve
ntricular myocardium were studied to find out if thermal acclimation a
lters Ca activation of contraction. Caffeine increased force of contra
ction more in the hearts of warm-acclimated (110%) than cold-acclimate
d fish (40%). Furthermore, relaxation rate and time-course of contract
ion were differently affected by caffeine in cold- and warm-acclimated
fish. These findings suggest that thermal acclimation changes the fun
ction of proteins responsible for excitation-contraction coupling.