The effects of temperature and adrenergic agonists on cardiac myocytes of perch (Perca fluviatilis) in cell culture conditions

1. 1. Isolated cardiac myocytes of perch, Perca fluviatilis, were kept in culture conditions for 1–2 months at 12 or 22°C. In the culture most myocytes flattened, lost their spindle-shaped morphology, protruded pseudopod-like branches and many of them started visible contractions in 1–2 weeks and continued beating for several months. Myocytes did not divide in the sparse cell population used. Typical intracellular structures could be seen in electron micrographs still after 1–2 months, but the sarcoplasmic organization became gradually more irregular in the culture.

2. 2. Beat rates showed linear temperature relationship on the Arrhenius plot. Myocytes cultivated at 22°C showed higher frequencies and slightly less dependence on temperature than myocytes cultivated at 12°C (apparent activation energies (E_a) 86 and 107 kJ/mol, respectively).

3. 3. Temperature dependence of frequencies was related to the presence of added serum or adrenergic agonists: β-adrenergic agonists increased the frequencies and rendered the cells less dependent on temperature; apparent activation energy was 43 kJ/mol for isoprenaline or adrenaline and 108 kJ/mol for noradrenaline and control group.

4. 4. Heat tolerance was greater in myocytes cultivated at 22°C than in myocytes cultivated at 12°C, and the change in tolerance appeared in 12 h after the alteration of culture temperature and the increased tolerance was persistent after that.

5. 5. It is suggested, that the processes of quick heat-hardening and of slower but persistent heat resistance acclimation developed in these cells in culture conditions but not the capacity acclimation, which seems to be dependent on adrenergic regulation of beat rate.

Effects of bovine colostrum supplementation on serum IGF-I, IgG, hormone, and saliva IgA during training

Mero, Antti, Heidi Miikkulainen, Jarmo Riski, RaimoPakkanen, Jouni Aalto, and Timo Takala. Effects of bovinecolostrum supplementation on serum IGF-I, IgG, hormone, and saliva IgAduring training. J. Appl. Physiol.83(4): 1144-1151, 1997.The purpose of this study was to examinethe effects of bovine colostrum supplementation (Bioenervi) on seruminsulin-like growth factor I (IGF-I), immunoglobulin G, hormone, andamino acid and saliva immunoglobulin A concentrations during a strengthand speed training period. Nine male sprinters and jumpersunderwent three randomized experimental training treatments of 8 daysseparated by 13 days. The only difference in the treatments was thedrink of 125 ml consumed per day. Posttraining increases were noticedfor serum IGF-I in the 25-ml Bioenervi treatment (125 ml contained 25 ml Bioenervi) and especially in the 125-ml Bioenervi treatment (125 mlcontained 125 ml Bioenervi) compared with the placebo (normal milkwhey) treatment (P < 0.05). The change in IGF-I concentration during the 8-day periods correlated positively with the change in insulin concentration during the sameperiods with 25-ml Bioenervi treatment(r = 0.68;P = 0.045) and with 125-ml Bioenervitreatment (r = 0.69;P = 0.038). Serum immunoglobulin G,hormone, and amino acid and saliva immunoglobulin A responses weresimilar during the three treatments. It appears that a bovine colostrumsupplement (Bioenervi) may increase serum IGF-I concentration inathletes during strength and speed training.

     

Thermoacclimatory changes in blood oxygen binding properties and gill secondary lamellar structure ofSalmo gairdneri

Summary The blood oxygen binding properties and gill secondary lamellar structure of rainbow trout acclimated to several temperatures were studied. The blood oxygen carrying capacity decreased as acclimation temperature increased from 2 to 15 °C; the decrease was probably caused by an increase in plasma volume. Also the blood oxygen affinity decreased as the acclimation temperature increased from 2 to 15 °C. This change had no effect on the oxygen loading in gills, since the efferent arterial oxygen tension was adequate for approximately 100% erythrocytic O₂ saturation at all acclimation temperatures, but facilitated the oxygen unloading in tissues. At the highest acclimation temperature (18 °C) the oxygen loading in gills was facilitated by the changes in the secondary lamellar structure; the proportion of erythrocytes in the secondary lamellar capillaries was higher than at the other acclimation temperatures (2 and 10 °C).     

Complexing of glycofuranosides with calcium ion,and its effect on their acid-catalysed solvolysis

Stability constants for the calcium-ion complexes of several methyl aldo-furanosides have been determined in aqueous solution by using a potentiostatic technique with an electrode that is selective for calcium ions. The results obtained have been verified by examining the chromatographic behaviour of the compounds on a strong cation-exchange resin in the Ca²⁺ form. The rate constants for the acid-catalyzed hydrolysis and methanolysis of a few 4-chlorophenyl aldofuranosides having different complexing abilities have been determined at various concentrations of calcium chloride. The dependences of the observed salt effects on the complexing ability of the substrate are discussed.     

Hemoglobin adducts and urinary mercapturic acids in rats as biological indicators of butadiene exposure

Binding of 1,2-epoxy-3-butene, the primary metabolite of butadiene, to hemoglobin (Hb) and excretion of its mercapturic acid in urine were studies as potential indicators of butadiene exposure. Four groups of Wistar rats were exposed to butadiene at 0, 250, 500 and 1000 ppm 6 h/day, 5 days/week, during 2 weeks. Blood was collected at the end of exposure and 17 days later for analysis of hemoglobin adducts and adduct stability. Urine was collected each day during exposure (afternoon samples) and in between exposures (morning samples). Adducts of 1,2-epoxy-3-butene to N-terminal valine in Hb were measured using the N-alkyl Edman procedure and GC/MS of the thiohydantoin derivatives. The corresponding mercapturic acid was analysed, after deacetylation, through derivatization with phthaldialdehyde and HPLC with fluorescence detection. The Hb adducts proved to be stable and are therefore useful for dosimetry of long-term exposure to butadiene. The adduct levels increased linearly with exposure dose up to 1000 ppm (3 nmol/g Hb at 1000 ppm). The increase with exposure dose of the mercapturic acid concentration in urine was also compatible with a linear does response up to 1000 ppm. The sensitivity of both analytical methods needs to be improved for their application to human samples.     

Fatty acids and long-chain bases of gangliosides of human gastrointestinal mucosa

The fatty acid and long-chain base composition of five major gangliosides from human stomach and small and large intestine mucosa were analyzed with gas chromatography. All the gangliosides greatly resembled each other in the fatty acid pattern. The main fatty acids were C_16:0, C_18:0 and C_24:0. No hydroxy fatty acids could be detected. In all the gangliosides 4-sphingenine was the predominant long-chain base (70–75%). About 15% of the long-chain bases had 20 carbon atoms in their chain. No trihydroxy long-chain bases could be detected.     

Fibroblast surface antigen (SF): Molecular properties,distribution in vitro and in vivo,and altered expression in transformed cells

We have recently described a cell type-specific surface (SF) antigen that is deleted in chick fibroblasts transformed by Rous sarcoma virus. SF antigen is a major surface component and makes up about 0.5% of the total protein on normal cultured fibroblasts. The antigen is shed from normal cells and is present in circulation (serum, plasma), and in vivo, also, in tissue boundary membranes. The molecular equivalents of both cellular and serum SF antigen are distinct, large polypeptides, one of which (SF210, MW 210,000) is glycosylated and, on the cell surface, highly susceptible to proteases and accessible to surface iodination. Immunofluorescence and scanning electron microscopy have indicated that the antigen is located in fibrillar structures of the cell surface, membrane ridges, and processes. Human SF antigen is present in human fibroblasts and in human serum. We have recently shown that human SF antigen is identical to what has been known as the “cold-insoluble globulin” and that it shows affinity toward fibrin and fibrinogen. Our results also indicate that loss of the transformation-sensitive surface proteins is due not to loss of synthesis but to lack of insertion of the protein in the neoplastic cell surface. Both normal and transformed cells produce the SF antigen, but the latter do not retain it in the cell surface. The loss of SF antigen, a major cell surface component, from malignant cells creates an impressive difference between the surface properties of normal and malignant cells. The possible significance of SF antigen to the integrity of the normal membrane and its interaction to surrounding structures is discussed.