The problem of tissue sampling from experimental animals with respect to freezing technique, anoxia, stress and narcosis

Faupel, R.P.; Seitz, Hans; Tarnowski, W.; Thiemann, Volker; Weiß, Ch.

doi:10.1016/0003-9861(72)90170-1

Cited by 204 publications

(43 citation statements)

References 36 publications

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“…In contrast with previous work on perfused livers and hepatocytes (Woods & Krebs, 1971;Seglen, 1974) our data indicate that hepatocytes from starved rats can form lactate when incubated with high glucose concentration. They also confirm the stimulation of glycolysis by anoxia and show, in addition, that incubation of hepatocytes from fed rats particularly in the presence of high glucose concentrations greatly diminishes the wellknown effect of anoxia on liver adenine nucleotides (Hems & Brosnan, 1970;Faupel et al, 1972;Sharma et al, 1980;Vincent et al, 1982 Uyeda et al, 1981) and the stimulation of glycolysis by glucose is best explained by the accumulation of this effector. Stimulation of glycolysis by anoxia, often referred to as the Pasteur effect, also involves the regulation of phosphofructokinase 1 (for reviews, see Krebs, 1972;Newsholme & Start, 1973;Ramaiah, 1974;Sols, 1976 Pi (Hems & Brosnan, 1970;Faupel et al, 1972;Faulkner & Jones, 1978;Sharma et al, 1980;Vincent et al, 1982; the present paper).…”

Section: Stimulation Ofglycolysis By Glucose and Anoxiamentioning

confidence: 59%

“…They also confirm the stimulation of glycolysis by anoxia and show, in addition, that incubation of hepatocytes from fed rats particularly in the presence of high glucose concentrations greatly diminishes the wellknown effect of anoxia on liver adenine nucleotides (Hems & Brosnan, 1970;Faupel et al, 1972;Sharma et al, 1980;Vincent et al, 1982 Uyeda et al, 1981) and the stimulation of glycolysis by glucose is best explained by the accumulation of this effector. Stimulation of glycolysis by anoxia, often referred to as the Pasteur effect, also involves the regulation of phosphofructokinase 1 (for reviews, see Krebs, 1972;Newsholme & Start, 1973;Ramaiah, 1974;Sols, 1976 Pi (Hems & Brosnan, 1970;Faupel et al, 1972;Faulkner & Jones, 1978;Sharma et al, 1980;Vincent et al, 1982; the present paper). IMP, hypoxanthine and uric acid, degradative products of the adenine nucleotides that accumulate during anoxia or ischaemia (Weber et al, 1977;Sharma, 1981;Vincent et al, 1982) From results reported here and previously (Van Schaftingen et al, 1980b;Hue et al, 198 la,b, 1982) (Hue et al, 1982).…”

Section: Stimulation Ofglycolysis By Glucose and Anoxiamentioning

confidence: 59%

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Role of fructose 2,6-bisphosphate in the stimulation of glycolysis by anoxia in isolated hepatocytes

Hue¹

1982

Biochemical Journal

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1. Incubation of hepatocytes from fed or starved rats with increasing glucose concentrations caused a stimulation of lactate production, which was further increased under anaerobic conditions. 2. When glycolysis was stimulated by anoxia, [fructose 2,6-bis-phosphate] was decreased, indicating that this ester could not be responsible for the onset of anaerobic glycolysis. In addition, the effect of glucose in increasing [fructose 2,6-bisphosphate] under aerobic conditions was greatly impaired in anoxic hepatocytes. [Fructose 2,6-bisphosphate] was also diminished in ischaemic liver, skeletal muscle and heart. 3. The following changes in metabolite concentration were observed in anaerobic hepatocytes: AMP, ADP, lactate and L-glycerol 3-phosphate were increased; ATP, citrate and pyruvate were decreased: phosphoenolpyruvate and hexose 6-phosphates were little affected. Concentrations of adenine nucleotides were, however, little changed by anoxia when hepatocytes from fed rats were incubated with 50 mM-glucose. 4. The activity of ATP:fructose 6-phosphate 2-phosphotransferase was not affected by anoxia but decreased by cyclic AMP. 5. The role of fructose 2,6-bisphosphate in the regulation of glycolysis is discussed.

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Section: Stimulation Ofglycolysis By Glucose and Anoxiamentioning

confidence: 59%

Section: Stimulation Ofglycolysis By Glucose and Anoxiamentioning

confidence: 59%

Role of fructose 2,6-bisphosphate in the stimulation of glycolysis by anoxia in isolated hepatocytes

Hue¹

1982

Biochemical Journal

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“…Livers were extracted from unrestrained, unanesthesized rats by the double-hatched method [13]. By this method the livers were removed and frozcn in liquid nitrogen within 3 s.…”

Section: Ex Trtrc Lion Of Rat Liver In Vivomentioning

confidence: 99%

Role of plasma membrane transport in hepatic glutamine metabolism

Häussinger

Soboll

Meijer

et al. 1985

European Journal of Biochemistry

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1. In livers of fed rats and in perfused livers supplied with a physiological portal glutamine concentration of 0.6 mM, the mitochondria1 and cytosolic glutamine concentrations are 20 mM and 7 mM, respectively, thus, the mitochondrial/cytosolic glutatnine concentration gradient is 2 ~ 3.2. Uptake and release of glutamine by periportal and perivenous hepatocytes occurs predominantly by an N a -dependent transport system (so-called system 'N').3. Histidine in near-physiological concentrations inhibits both glutamine uptake by periportal hepatocytes and its release by perivenous hepatocytcs. This is not due to an inhibition of glutamine-metabolizing enzymes by histidine or its metabolites. With physiological portal glutamine concentrations (0.6 mM), stimulation of glutaminase flux or of glutamine transaminasc flux is followed by a decrease of hepatic glutamine levels to about 80% or 30%, respectively, glutamine levels are further decreased to 50% or 20% in the presence of histidine.4. When glutamine is synthesized endogeneously (no glutamine added), the histidine-induced inhibition of glutitmine release is paralleled by a 210%, increase or the hepatic tissue level of glutaminc.5. In experiments with and without iiiethioninc sulfoximine and in the absence of added glutamine, the glutamine content in the small perivenous hepatocyte population containing glutamine synthetase is estimatcd t o be about 3.5 pmol/g wet weight and that in the periportal hepatocytes as low as 0.3 pmol/g wet weight.6. In contrast to the prevailing view, it is concludcd that glutamine transport across the plasma mernbranc of hepatocytes is a potential regulatory site in glutamine degradation and synthcsis, especially under the influence of efrectors like histidine.Glutamine uptake into the hepatocytes occurs by an Nadependent transport system 'N', also shared by other amino acids likc histidine or asparagine [l -31 (for review see [4]). It has bccn shown that histidine and asparagine inhibit glutamine transport across the liver plasma inembrane [2, 31. In addition, facilitated diffusion allows hepatocytes to relcasc glutaniine when intracellular concentrations are elevated [3].It is assumed in the literature that glutamine transport across the plasma membrane of hepatocytes is not ratc-controlling for its catabolism [3 -61 and that regulation of hcpatic glutamine breakdown occurs at thc level of glutamine-metabolizing enzymes. However. these previous studies focused on glutaminc transport rather than its metabolism and they did not take into account the recently discovered hepatocyte hctcrogeneity with glutaminase being periportal [7] and glutamine synthetase being perivenous [7, 81 and the activity of glutamine transaminases in pcriportal as well perivenous hepatocytcs [9]. This unique distribution of glutamine-mctabolizing enzymes results in an intercellular glutamine cycle [7] (for review see [lo]): while glutamine is taken up by periportal hepatocytes, it is released by perivenous hepatocytes into the

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“…In dogs anaesthetized for 2 h with diethylether, there was a 15fold increase of ascorbic acid in liver urine over 24 h [20,21]. The following day the values were normal.…”

Section: Resultsmentioning

confidence: 99%