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At least 19 recordsLinked to original sources
PubMed1976

The effects of temperature and thermal acclimation upon the osmotic properties and nonelectrolyte permeability of liver and gill mitochondria from rainbow trout (Salmo gairdneri).

Thermal acclimation of rainbow trout (Salmo gairdneri) taken from 20 degrees C to 7 degrees C resulted in adaptation of mitochondrial function, as evidenced by increases in the specific activities of NADH- and succinate-cytochrome c reductase of 1.93- and 2.7-fold respectively. Mitochondria from both gill and liver obeyed the Boyle-van't Hoff relationship in the range from 400 to 60 mosM. Thermal acclimation had no effect on the osmotic properties of liver mitochondria, whereas gill mitochondria from cold-acclimated trout were more sensitive to osmotic swelling than mitochondria from warm-acclimated individuals. The non-electrolyte permeability of liver mitochondria was assessed by optically monitoring mitochondrial swelling rates in isosmotic solutions of urea, glycerol, mannitol and glucose. Two parameters of mitochondrial swelling were determined: (a) initial swelling rates, d(1/A)dt, and (b) swelling constants, ks, derived from the time required to swell a fixed volume. Regardless of the assay temperature or the permeant employed, liver mitochondria from cold-acclimated trout exhibited greater initial swelling rates than mitochondria from warm-acclimated trout, indicating properties of temperature-compensated permeability. The apparent ranking of nonelectrolyte permeabilities was urea greater than glycerol greater than mannitol greater than glucose. ks values for urea and glycerol from cold-acclimated trout were greater than values typical of warm-acclimated populations; however ks values for glucose and mannitol were not influenced by thermal acclimation. Regardless of the permeant considered, activation energies for ks values were 3- to 5-fold greater than those for initial swelling rates. The time course of mitochondrial swelling consists of two components, an initial rapid swelling phase characterized by a half-life of 3-12 seconds, and a slower swelling phase characterized by a half life of 1-6 minutes. Initial swelling rates, which approximate the rapid swelling component, are considered to be the least ambiguous index of permeability, whereas ks values are more complex and strongly influenced by the slower swelling component.

Acclimatization↗
PubMed1977

Turnover of cytochrome C in skeletal muscle of green sunfish (Lepomis cyanellus, R.) during thermal acclimation.

The concentration of cytochrome c in the skeletal muscle of the green sunfish (Lepomis cyanellus) increases with decreasing temperature of acclimation: 1.51 +/- 0.09, 1.17 +/- 0.03, and 0.98 +/- 0.07 nanomoles per gram wet weight from muscle of animals acclimated to 5 degrees, 15 degrees, and 25 degrees C, respectively. The roles of synthesis and degradation of cytochrome c during thermal acclimation were investigated by measurement of loss of specific radioactivity from cytochrome c and from total mitochondrial heme protein, and by analysis of the rate of change in concentration of cytochrome c. The radioisotope used was 14C-delta-aminolevulinic acid, a non-reutilizable heme precursor. At 25 degrees C, the half-life of cytochrome c was 7.1 days based on radioactivity measurements and 5.6 days based on change in concentration. Statistical analysis showed no significant difference in half-lives obtained by the two methods. The half-life of total mitochondrial heme protein was determined to be 5.7 days on the basis of radioactivity data, under the same conditions. No significant difference was found between the rate of turnover of the heme protein pool from mitochondria and either measurement for cytochrome c at 25 degrees C. At an acclimation temperature of 5 degrees C, the half-life of cytochrome c from skeletal muscle was 13.7 days based upon changes in concentration. At low acclimation temperature, radioactive label was retained in acid-soluble form by fish for many days, precluding measurement of half-life by this technique. Transfer of fish from 25 degrees to 5 degrees C resulted in a rapid decrease of approximately 40% in rates in synthesis of skeletal muscle cytochrome c, and a concomitant decrease in the degradation rate constant for this molecule of approximately 60%. The disproportionality in temperature-sensitivities of these two processes leads to an approximately 50% net increase in the concentration of cytochrome c during acclimation. In transfer from 5 degrees to 25 degrees C, the converse, rapid readjustments in synthetic and degradative parameters occur, resulting in the observed decrease in cytochrome c content.

Acclimatization↗
PubMed1978

Carbonic anhydrase (acetazolamide-sensitive esterase) activity in the blood, gill and kidney of the thermally acclimated rainbow trout, Salmo gairdneri.

1. Gill, kidney and blood levels of acetazolamide-sensitive esterase (carbonic anhydrase) activity were estimated at acclimation temperature and at a common temperature (25 degrees C) in rainbow trout acclimated to 2, 10 and 18 degrees C. Plasma levels of sodium, potassium and chloride were also examined for possible acclimatory variations. 2. Plasma sodium and chloride levels, and the sodium:chloride ratio were unaffected by thermal acclimation; potassium concentrations were significantly elevated at 18 degrees C. 3. Significant, but modest changes in renal and branchial carbonic anhydrase activity were observed under physiologically realistic incubation temperature conditions. Blood carbonic anhydrase activity was sharply elevated at higher acclimation temperatures. 4. The data are discussed in relation to the hypothesis that carbonic anhydrase in this relatively stenothermal freshwater salmonid, through its intimate association with the coupled HCO-3/CL- and H+ +NH+4/Na+ exchange systems may provide for relatively thermostable basal rates of sodium and chloride uptake from the medium and recovery from urine. The renal, and more notably the branchial (Na+/K+)-stimulated ATPase systems, and erythrocytic carbonic anhydrase may then serve primarily as high-temperature amplifiers of sodium and chloride recruitment respectively.

Acclimatization↗
PubMed1979

Significance of the variation in isozymes of liver lactate dehydrogenase with thermal acclimation in goldfish--II. Effect of pH.

1. Effect of pH on liver lactate dehydrogenase (LDH) and its isozymes was examined in the goldfish acclimated to different temperatures and some purification of the LDH was attempted. 2. The optimal pH and the Km value at 30 degrees C of the enzyme were independent of acclimation temperature. 3. the optimal pH of isozyme was more basic in the order of LDH-1, LDH-2, LDH-3, LDH-4 and LDH-5. Km values of isozymes at 30 degrees C were higher in the order of LDH-1, LDH-3 and LDH-5. 4. There was no change in the enzyme activity during thermal acclimation.

Acclimatization↗
PubMed1979

Enzyme changes accompanying thermal acclimation in two species of pleurocerid snails.

Goniobasis cahawbensis is a stream snail that experiences an annual temperature cycle. G. cochliaris is limited in distribution to springs, and their immediate vicinities, which are characterized by nearly constant annual temperatures. The present study sought to determine whether temperature dependent biochemical differences exist that might account for the differential distribution of these congeneric pleurocerid snails. Eight enzymes were examined following acclimation to 10 degrees, 17 degrees and 24 degrees C. No significant temperature dependent qualitative differences in enzyme phenotypes were demonstrable in either species by starch-gel electrophoresis for malate dehydrogenase, glucose-6-phosphate dehydrogenase, phosphogluconate dehydrogenase, phosphoglucomutase, superoxide dismutase and acetyl and butyryl esterases. Significant quantitative differences were observed in three of these enzymes. G. cahawbensis cytosol malate dehydrogenase activity increased significantly with increasing acclimation temperature, while G. cochliaris malate dehydrogenase activity remained unchanged. The activities of glucose-6-phosphate dehydrogenase did not differ significantly between acclimation temperatures for either species; however, the overall activity of both enzymes was significantly higher for G. cochliaris. Appreciable levels of LDH activity were not demonstrable by electrophoresis or enzymatic assay.

Adaptation, Physiological↗
PubMed1979

Fatty acid and sterol synthesis by hepatocytes of thermally acclimated rainbow trout (Salmo gairdneri).

Incorporation of tritium from tritiated water into lipid fractions was measured in isolated hepatocytes from rainbow trout (Salmo gairdneri) acclimated to 5 degrees C and 20 degrees C. Hepatocytes from cold-acclimated trout exhibited significantly higher rates of tritium incorporation into both fatty acid and sterol fractions at assay temperatures of 15 degrees C and 20 degrees C than did hepatocytes from warm-acclimated trout. Tritium incorporation into the fatty acid fraction was nearly temperature independent in hepatocytes from warm-acclimated trout (Q10 = 1.39) but markedly temperature dependent (Q10 = 2.63) in hepatocytes from cold-acclimated trout; in contrast, rates of sterol synthesis were more temperature dependent in warm-acclimated trout. At 5 degrees C, fatty acid lipogenesis comprised a significantly greater percentage of the total tritium incorporation in hepatocytes from warm-acclimated trout and the percentage of total lipogenesis attributable to fatty acids decreased significantly in warm-acclimated trout as the assay temperature increased; the opposite trends were observed in cold-acclimated trout.

Adaptation, Physiological↗
PubMed1979

Significance of the variation in isozymes of liver lactate dehydrogenase with thermal acclimation in goldfish--I. Thermostability and temperature dependency.

1. Total and isozyme properties as well as isozyme pattern were examined in liver lactate dehydrogenase (LDH) from goldfish acclimated to different temperatures. 2. LDH of warm-acclimated fish were thermostable and exhibited higher Q10 in low temperature range as compared with that of co ld-acclimated fish. 3. The relative activities of LDH-1, LDH-2 and LDH-3, which were more thermostable, increased and LDH-4 and LDH-5, which were more heat sensitive, decreased during warm acclimation. Q10 in the low temperature range for LDH-5 was lower than that for LDH-1.

Acclimatization↗
PubMed1979

Influence of thermal acclimation on membrane lipid composition of rainbow trout liver.

Rainbow trout (Salmo gairdneri) acclimated to 5 degrees C possessed larger livers and less neutral lipid per gram of liver than 20 degrees C-acclimated animals; quantities of liver glycolipid, phospholipid, and cholesterol did not vary significantly with acclimation temperature. The relative proportions of phosphatidylethanolamine increased significantly following cold exposure, whereas the quantities of sphingomyelin and cardiolipin declined. For all phosphatides examined (phosphatidylethanolamine, phosphatidylcholine, phosphatidylserine, phosphatidylinositol, lysolecithin, cardiolipin, sphingomyelin) cold acclimation resulted in 1) an increase in the quantity of polyunsaturated fatty acids, 2) a reduction in the level of saturated fatty acids, and 3) little change in the total content of monoenes and dienes. The increased content of polyunsaturated fatty acids in choline and ethanolamine phosphatides following cold acclimation was confined to the 2-position and occurred at the expense of monoenes and dienes. The relative proportions of n - 3 fatty acids, and less frequently n - 6 fatty acids, increased in phosphatides of cold-acclimated trout, whereas the relative proportions of n - 9 fatty acids declined. These data suggest a preferential incorporation of fatty acids belonging to the linolenic acid family at reduced temperatures. Temperature-induced changes in the chemical composition of trout liver phospholipids counteracted the effects of acute temperature change on nonelectrolyte permeability of isolated liposomes.

Adaptation, Physiological↗
PubMed1979

Structural studies of natural actomyosin from thermally acclimated frogs.

Natural actomyosin was isolated from skeletal muscle of frogs (Rana catesbeiana) acclimated at 25 degrees C and 5 degrees C. It was found that preparations isolated from warm-acclimated frogs may display considerable degradation of myosin heavy chains as compared with preparations isolated from cold-acclimated frogs. However, degradation may be minimized by inclusion of protease inhibitors during purification, indicating enhanced protease activity in preparations of natural actomyosin from warm-acclimated frogs. When purified in the presence of protease inhibitors, natural actomyosin from both warm-acclimated and cold-acclimated frogs exhibits comparable subunit composition of SDS-gel electrophoresis. The overall gel pattern is similar to that obtained from rabbit natural actomyosin except that in the frog, troponin-T and troponin-C appear to co-migrate with tropomyosin and myosin light chain 2, respectively.

Acclimatization↗