Journal articles: 'Biosynthesis of rat adrenaline'

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Peltsch, Heather, Sandhya Khurana, Collin J. Byrne, Phong Nguyen, Neelam Khaper, Aseem Kumar, and T. C. Tai. "Cardiac phenylethanolamine N-methyltransferase: localization and regulation of gene expression in the spontaneously hypertensive rat." Canadian Journal of Physiology and Pharmacology 94, no. 4 (April 2016): 363–72. http://dx.doi.org/10.1139/cjpp-2015-0303.

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Phenylethanolamine N-methyltransferase (PNMT) is the terminal enzyme in the catecholamine biosynthetic pathway responsible for adrenaline biosynthesis. Adrenaline is involved in the sympathetic control of blood pressure; it augments cardiac function by increasing stroke volume and cardiac output. Genetic mapping studies have linked the PNMT gene to hypertension. This study examined the expression of cardiac PNMT and changes in its transcriptional regulators in the spontaneously hypertensive (SHR) and wild type Wistar-Kyoto (WKY) rats. SHR exhibit elevated levels of corticosterone, and lower levels of the cytokine IL-1β, revealing systemic differences between SHR and WKY. PNMT mRNA was significantly increased in all chambers of the heart in the SHR, with the greatest increase in the right atrium. Transcriptional regulators of the PNMT promoter show elevated expression of Egr-1, Sp1, AP-2, and GR mRNA in all chambers of the SHR heart, while protein levels of Sp1, Egr-1, and GR were elevated only in the right atrium. Interestingly, only AP-2 protein-DNA binding was increased, suggesting it may be a key regulator of cardiac PNMT in SHR. This study provides the first insights into the molecular mechanisms involved in the dysregulation of cardiac PNMT in a genetic model of hypertension.

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Simonyi, Agnes, Bela Kanyicska, Tibor Szentendrei, and Marton I. K. Fekete. "Effect of chronic morphine treatment on the adrenaline biosynthesis in adrenals and brain regions of the rat." Biochemical Pharmacology 37, no. 4 (February 1988): 749–52. http://dx.doi.org/10.1016/0006-2952(88)90150-5.

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Shimbhu, Dawan, Kohichi Kojima, and Toshiharu Nagatsu. "A SENSITIVE ASSAY FOR NON-SPECIFIC N-METHYLTRANSFERASE ACTIVITY IN RAT TISSUES BY HIGH-PERFORMANCE LIQUID CHROMATOGRAPHY ELECTROCHEMICAL DETECTION." ASEAN Journal on Science and Technology for Development 19, no. 1 (December 10, 2017): 63–68. http://dx.doi.org/10.29037/ajstd.318.

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Phenylethanolamine N-methyltransferase (PNMT) and non-specific N -methyltransferase (EC 2.1.1.28) catalyze the N-methylation of aromatic amines. PNMT is specific for phenylethanolamines such as noradrenaline (NA). and catalyzes the step in catecholamine biosynthesis, forming adrenaline (AD) from NA. PNMT activity is high in adrenal gland, whereas non-specific N-methyltransferase is distributed in various tissues such as the lungs. Borchardt et al. first reported a method to detect PNMT activity by high-performance liquid chromatography electrochemical detection (HPLC-EICD), which could demonstrate the activity only in the adrenal medulla and hypothalamus. Recently, Troeewicz et al. reported a highly sensitive assay method for PNMT using HPLC-EICD by which the activity in all regions of rat brains could be measured. The activity of non-specific N-methyltransferase in brain regions and peripheral tissues of the rat could be detected by a radioassay. However, there has been no repot on an assay method for non-specific N-methyltransferase using HPLC-EICD. In this paper, we describe a highly sensitive assay procedure for the activity of non-specific N-methyltransferase by high-performance reversed-phase ion pair chromatography with electrochemical detection. By this method, the non-specific N-methyltransferase activity could be determined in various rat brain regions and peripheral tissues.

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Shimojo, M., C. B. Whorwood, and P. M. Stewart. "11β-Hydroxysteroid dehydrogenase in the rat adrenal." Journal of Molecular Endocrinology 17, no. 2 (October 1996): 121–30. http://dx.doi.org/10.1677/jme.0.0170121.

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ABSTRACT 11β-Hydroxysteroid dehydrogenase (11β-HSD) catalyses the interconversion of biologically active cortisol to inactive cortisone in man, and corticosterone to 11-dehydrocorticosterone in rodents. As such, this enzyme has been shown to confer aldosterone-selectivity on the mineralocorticoid receptor and to modulate cortisol/corticosterone access to the glucocorticoid receptor (GR). Two kinetically distinct isoforms of this enzyme have been characterized in both rodents and man; a low-affinity NADP(H)-dependent enzyme (11β-HSD1) which predominantly acts as an oxo-reductase and, more recently, a high-affinity NAD-dependent uni-directional dehydrogenase (11β-HSD2). In this study we have analysed the expression of both 11β-HSD1 and 11β-HSD2 isoforms in rat adrenal cortex and medulla and have investigated their possible roles with respect to glucocorticoid-regulated enzymes mediating catecholamine biosynthesis in adrenal medullary chromaffin cells. Using a rat 11β-HSD1 probe and a recently cloned in-house mouse 11β-HSD2 cDNA probe, Northern blot analyses revealed expression of mRNA species encoding both 11β-HSD1 (1·4kb) and 11β-HSD2 (1·9kb) in the whole adrenal. Consistent with this, 11β-dehydrogenase activity (pmol 11-dehydrocorticosterone formed/mg protein per h, mean ± s.e.m.) in adrenal homogenates, when incubated with 50 nm corticosterone in the presence of 200 μm NAD, was 97·0 ± 9·0 and with 500 nm corticosterone in the presence of 200 μm NADP, was 98·0 ± 1·4 11-Oxoreductase activity (pmol corticosterone formed/mg protein per h) with 500 nm 11-dehydrocorticosterone in the presence of 200 μm NADPH, was 187·7 ± 31·2. In situ hybridization studies of rat adrenal cortex and medulla using 35S-labelled antisense 11β-HSD1 cRNA probe revealed specific localization of 11β-HSD1 mRNA expression predominantly to cells at the corticomedullary junction, most likely within the inner cortex. In contrast, 11β-HSD2 mRNA was more abundant in cortex versus medulla, and was more uniformly distributed over the adrenal gland. Negligible staining was detected using control sense probes. Ingestion of the 11β-HSD inhibitor, glycyrrhizic acid (>100mg/kg body weight per day for 4 days) resulted in significant inhibition of adrenal NADP-dependent (98·0 ± 1·4 vs 42·5 ± 0·4) and NAD-dependent (97·0 ± 9·0 vs 73·2 ± 6·7) 11β-dehydrogenase activity and 11-oxoreductase activity (187·7 ± 31·2 vs 67·7 ± 15·3). However, while levels of 11β-HSD1 mRNA were similarly reduced (0·85 ± 0·07 vs 0·50 ± 0·05 arbitrary units), those for 11β-HSD2 remained unchanged (0·44 ± 0·03 vs 0·38 ± 0·01). Levels of mRNA encoding the glucocorticoid-dependent enzyme phenylethanolamine N-methyltransferase which catalyses the conversion of noradrenaline to adrenaline, were also significantly reduced in those rats given glycyrrhizic acid (1·12 ± 0·04 vs 0·78 ± 0·04), while those for the glucocorticoid-independent enzyme tyrosine hydroxylase (1·9 kb), which catalyses the conversion of tyrosine to DOPA, were unchanged (0·64 ± 0·04 vs 0·61 ± 0·04). In conclusion, the rat adrenal gland expresses both 11β-HSD1 and 11β-HSD2 isoforms. 11β-HSDl gene expression is localized to the adrenal cortico-medullary junction, where it is ideally placed to regulate the supply of cortex-derived corticosterone to the medullary chromaffin cells. This, together with our in vivo studies, suggests that 11β-HSD1 may play an important role with respect to adrenocorticosteroid regulation of adrenaline biosynthesis. The role of 11β-HSD2 in the adrenal remains to be elucidated.

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Deng, Xinqi, Nan Jiang, Li Guo, Chunguo Wang, Jiaoyan Li, Xiaoci Liu, Bixiu Zhu, et al. "Protective Effects and Metabolic Regulatory Mechanisms of Shenyan Fangshuai Recipe on Chronic Kidney Disease in Rats." Evidence-Based Complementary and Alternative Medicine 2020 (August 25, 2020): 1–13. http://dx.doi.org/10.1155/2020/5603243.

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Background. Chronic kidney disease (CKD) is one of the major causes of renal damage. Shenyan Fangshuai Recipe (SFR), a modified prescription of traditional medicine in China, showed potent effects in alleviating edema, proteinuria, and hematuria of CKD in clinical practices. In this study, we aimed to investigate scientific evidence-based efficacy as well as metabolic regulations of SFR in CKD treatment. Materials and Methods. The effect of SFR on CKD was observed in a rat model which is established with oral administration of adenine-ethambutol mixture for 21 days. Further, metabolites in serum were detected and identified with ultra-performance liquid chromatography-high resolution mass spectrometry (UPLC-HRMS). Metabolomics study was performed using Ingenuity Pathway Analysis (IPA) software. Results. With H&E staining and Masson’s trichrome, the results showed that chronic kidney damage is significantly rescued with SFR treatment and recovered to an approximately normal condition. Along with 44 differential metabolites discovered, the regulation of SFR on CKD was enriched in glycine biosynthesis I, mitochondrial L-carnitine shuttle pathway, phosphatidylethanolamine biosynthesis III, sphingosine-1-phosphate signaling, L-serine degradation, folate transformations I, noradrenaline and adrenaline degradation, salvage pathways of pyrimidine ribonucleotides, cysteine biosynthesis III (Mammalia), glycine betaine degradation, and cysteine biosynthesis/homocysteine degradation. Further, TGFβ-1 and MMP-9 were observed playing roles in this regulatory process by performing immunohistochemical staining. Conclusion. SFR exerts potent effects of alleviating glomerular sclerosis and interstitial fibrosis in the kidney, mainly via integrated regulations on metabolism and production of homocysteine, L-carnitine, and epinephrine, as well as the expression of TGFβ-1. This study provides evidence for SFR’s protective effects on CKD and reveals the metabolic mechanism behind these benefits for the first time.

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Galan, Xavier, Julia Peinado-Onsurbe, Monique Q. Robert, Maria Soley, Miquel Llobera, and Ignasi Ramírez. "Acute regulation of hepatic lipase secretion by rat hepatocytes." Biochemistry and Cell Biology 80, no. 4 (August 1, 2002): 467–74. http://dx.doi.org/10.1139/o02-136.

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Hepatic lipase is involved in cholesterol uptake by the liver. Although it is known that catecholamines are responsible for the daily variation of enzyme activity, the mechanisms involved are poorly understood. Rat hepatocytes incubated with adrenaline or other Ca2+-mobilizing hormones were used as an experimental model. Adrenaline reduced in a similar proportion the secretion of both hepatic lipase and albumin. The effect of adrenaline disappeared completely in cells exposed to cycloheximide. Adrenaline decreased incorporation of [35S]Met into cellular and secreted proteins, but it affected neither degradation of [35S]Met-prelabeled proteins nor the abundance of total and specific (albumin, hepatic lipase, beta-actin) mRNA. Other Ca2+-mobilizing agents had the opposite effect on hepatic lipase secretion: it was decreased by vasopressin but was increased by epidermal growth factor. Vasopressin and epidermal growth factor had the opposite effect on [35S]Met incorporation into cellular and secreted proteins, but neither affected hepatic lipase mRNA. The acute effect of adrenaline, vasopressin, and epidermal growth factor on hepatic lipase secretion is the consequence of the effect of these hormones on protein synthesis and is therefore nonspecific.Key words: adrenaline, vasopressin, epidermal growth factor, albumin secretion.

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Khurana, Sandhya, Sujeenthar Tharmalingam, Alyssa Murray, and T. C. Tai. "Epigenetic regulation of phenylethanolamine N‐methyltransferase: implications for adrenaline biosynthesis." FASEB Journal 34, S1 (April 2020): 1. http://dx.doi.org/10.1096/fasebj.2020.34.s1.04160.

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Costa, Vera M., Luísa M. Ferreira, Paula S. Branco, Félix Carvalho, Maria L. Bastos, Rui A. Carvalho, Márcia Carvalho, and Fernando Remião. "Characterization of adrenaline and adrenaline-GSH adduct transport in freshly isolated rat cardiomyocytes." Toxicology Letters 180 (October 2008): S99. http://dx.doi.org/10.1016/j.toxlet.2008.06.405.

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Napolitano, Gaetana, Daniela Barone, Sergio Di Meo, and Paola Venditti. "Adrenaline induces mitochondrial biogenesis in rat liver." Journal of Bioenergetics and Biomembranes 50, no. 1 (December 14, 2017): 11–19. http://dx.doi.org/10.1007/s10863-017-9736-6.

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Nahar, Nurun, and Nargis Akhter. "Effect of carvedilol on adrenaline-induced changes in serum electrolytes in rat." Bangladesh Medical Research Council Bulletin 35, no. 3 (February 8, 2010): 105–9. http://dx.doi.org/10.3329/bmrcb.v35i3.4116.

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Circulating catecholamine that is increased in early phase of myocardial infarction alters serum electrolyte levels which might predispose to serious ventricular arrhythmias. In this study the effect of pretreatment of carvedilol on adrenaline-induced changes in the serum electrolytes (Mg2+, K+, Ca2+, Na+) was evaluated in rats. Adrenaline was administered at a dose of 2 mg/kg body weight subcutaneously 2 injections 24 hours apart and serum electrolytes were estimated at 12 hours, 24 hours and 7 days after the 2nd injection of adrenaline. Adrenaline administration initially caused hypomagnesemia, hypokalemia, hypocalcemia and hyponatremia, which were restored to normal spontaneously within 7 days. Pretreatment of carvedilol orally at a dose of 1 mg/kg body weight for 2 weeks significantly prevented initial reduction in serum electrolyte levels induced by adrenaline. It was concluded that prophylactic use of carvedilol might prevent the serious consequences of myocardial infarction as sudden cardiac death due to arrhythmia caused by electrolyte changes. Keywords: Adrenaline; Carvedilol; Electrolyte; RatOnline: 9 Feb 2010DOI: http://dx.doi.org/10.3329/bmrcb.v35i3.4116Bangladesh Med Res Counc Bull 2009; 35: 105-109

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GARCIA, Carolina, Tania C. PITHON-CURI, Maria DE LOURDES FIRMANO, Mariza PIRES DE MELO, Philip NEWSHOLME, and Rui CURI. "Effects of adrenaline on glucose and glutamine metabolism and superoxide production by rat neutrophils." Clinical Science 96, no. 6 (April 28, 1999): 549–55. http://dx.doi.org/10.1042/cs0960549.

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Despite the large body of information on the role of corticosteroids in regulating lymphocyte and phagocyte function, the role of the hormone adrenaline in immunoregulation is an under-investigated topic. The present study has addressed the effects of adrenaline on the rates of utilization and oxidation of glucose and glutamine, the phagocytic capacity and the rate of superoxide production by rat neutrophils. Incubation of rat neutrophils in the presence of 50 µM adrenaline caused a marked elevation in glucose metabolism, an effect that could be blocked by propranolol. Adrenaline caused a partial inhibition of glutamine utilization by neutrophils, an effect that was also blocked by propranolol. These effects of adrenaline could be mimicked by 100 µM dibutyryl cAMP. Phosphate-dependent glutaminase activity was significantly elevated in neutrophils incubated in the presence of 50 µM adrenaline or 100 µM dibutyryl cAMP for 1 h, whereas glutamine oxidation was significantly depressed (P < 0.05) under these conditions. The elevation in enzyme activity was only partially blocked by propranolol. The phagocytic activity of rat neutrophils was not altered by adrenaline in the presence of either glucose or glutamine. The rate of phorbol 12-myristate 13-acetate-induced superoxide production in the presence of glucose was potently reduced by the addition of 5 nM or 50 µM adrenaline. This effect could be mimicked by dibutyryl cAMP. However, when rat neutrophils were incubated in the presence of glutamine plus adrenaline (5 nM or 50 µM), the rate of superoxide production was only marginally reduced. These findings support the proposition that adrenaline may deviate the flux of glucose from the NADPH-producing pentose phosphate pathway, thus reducing substrate availability for the superoxide-generating NADPH oxidase. However, glutamine metabolism may still give rise to substantial quantities of NADPH from the glutaminolysis pathway. We postulate that glutamine metabolism may thus provide a protective mechanism against the inhibitory effect of adrenaline on superoxide production by neutrophils.

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Abe, Nozomu, Hiroaki Toyama, Yutaka Ejima, Kazutomo Saito, Tsutomu Tamada, Masanori Yamauchi, and Itsuro Kazama. "α1-Adrenergic Receptor Blockade by Prazosin Synergistically Stabilizes Rat Peritoneal Mast Cells." BioMed Research International 2020 (May 13, 2020): 1–12. http://dx.doi.org/10.1155/2020/3214186.

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Background. Adrenaline quickly inhibits the release of histamine from mast cells. Besides β2-adrenergic receptors, several in vitro studies also indicate the involvement of α-adrenergic receptors in the process of exocytosis. Since exocytosis in mast cells can be detected electrophysiologically by the changes in the membrane capacitance (Cm), its continuous monitoring in the presence of drugs would determine their mast cell-stabilizing properties. Methods. Employing the whole-cell patch-clamp technique in rat peritoneal mast cells, we examined the effects of adrenaline on the degranulation of mast cells and the increase in the Cm during exocytosis. We also examined the degranulation of mast cells in the presence or absence of α-adrenergic receptor agonists or antagonists. Results. Adrenaline dose-dependently suppressed the GTP-γ-S-induced increase in the Cm and inhibited the degranulation from mast cells, which was almost completely erased in the presence of butoxamine, a β2-adrenergic receptor antagonist. Among α-adrenergic receptor agonists or antagonists, high-dose prazosin, a selective α1-adrenergic receptor antagonist, significantly reduced the ratio of degranulating mast cells and suppressed the increase in the Cm. Additionally, prazosin augmented the inhibitory effects of adrenaline on the degranulation of mast cells. Conclusions. This study provided electrophysiological evidence for the first time that adrenaline dose-dependently inhibited the process of exocytosis, confirming its usefulness as a potent mast cell stabilizer. The pharmacological blockade of α1-adrenergic receptor by prazosin synergistically potentiated such mast cell-stabilizing property of adrenaline, which is primarily mediated by β2-adrenergic receptors.

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Sakata, S., and J. Iriuchijima. "Adrenomedullary origin of the hindquarter vasodilation during the transposition response of the rat." Canadian Journal of Physiology and Pharmacology 66, no. 1 (January 1, 1988): 18–21. http://dx.doi.org/10.1139/y88-003.

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Transposing a rat from the home cage to a new cage produces a cardiovascular response (transposition response) characterized by an increase in hindquarter blood flow with unchanged systemic arterial pressure. Arterial blood samples were collected from rats before and during this response for radioenzymatic assay of catecholamines. During the transposition response, the concentration of adrenaline and noradrenaline in plasma increased about six- and two-fold, respectively. Ablation of the adrenal medulla prevented these changes in plasma catecholamine concentration. Constant i.v. infusion of adrenaline, at rates producing a hindquarter flow approximately matching that observed during the transposition response, evoked an increase in plasma adrenaline concentration also approximately matching the increase observed during the transposition response. It is concluded that the increase in plasma adrenaline secreted from the adrenal medulla is the main cause of the increase in hindquarter blood flow in the transposition response.

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Brindle, N. P., and J. A. Ontko. "α-adrenergic suppression of very-low-density-lipoprotein triacylglycerol secretion by isolated rat hepatocytes." Biochemical Journal 250, no. 2 (March 1, 1988): 363–68. http://dx.doi.org/10.1042/bj2500363.

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The effect of adrenaline on triacylglycerol synthesis and secretion was examined in isolated rat hepatocytes. Cells were incubated with 0.5 mM-[1-14C]oleate, and the accumulation of triacylglycerol and [14C]triacylglycerol was measured in the incubation medium. Triacylglycerol appearing in the medium was present in a form with properties similar to very-low-density lipoproteins. Triacylglycerol, [14C]triacylglycerol and [14C]phospholipid contents of hepatocytes were also determined. Addition of 10 microM-(-)adrenaline decreased accumulation of glycerolipid in the incubation medium and also decreased cellular [14C]phospholipid content. Prazosin abolished these effects, whereas propranolol did not. The hormone did not affect cellular triacylglycerol content or rates of incorporation of [1-14C]oleate into cell triacylglycerol. The effect of adrenaline on the removal of newly secreted triacylglycerol and the secretion of synthesized glycerolipid was also examined. The catecholamine did not affect rates of removal of newly secreted triacylglycerol. Adrenaline did inhibit the secretion of pre-synthesized lipid by the cells, as assessed by the appearance of radiolabelled triacylglycerol from hepatocytes that had been preincubated with [1,2,3-3H]-glycerol. Adrenaline did not affect rates of fatty acid uptake by hepatocytes, but did stimulate oxidation of [1-14C]oleate, principally to 14CO2.

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Donsmark, Morten, Jozef Langfort, Cecilia Holm, Thorkil Ploug, and Henrik Galbo. "Regulation and role of hormone-sensitive lipase in rat skeletal muscle." Proceedings of the Nutrition Society 63, no. 2 (May 2004): 309–14. http://dx.doi.org/10.1079/pns2004359.

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Intramyocellular triacylglycerol (TG) is an important energy store, and the energy content of this depot is higher than the energy content of the muscle glycogen depot. It has recently been shown that the mobilization of fatty acids from this TG pool may be regulated by the neutral lipase hormone-sensitive lipase (HSL). This enzyme is known to be rate limiting for intracellular TG hydrolysis in adipose tissue. The presence of HSL has been demonstrated in all muscle fibre types by Western blotting of muscle fibres isolated by collagenase treatment or after freeze-drying. The content of HSL varies between fibre types, being higher in oxidative fibres than in glycolytic fibres. When analysed under conditions optimal for“ HSL, neutral lipase activity in muscle can be stimulated by adrenaline as well as by contractions. These increases are abolished by the presence of anti-HSL antibody during analysis. Moreover, immunoprecipitation with affinity-purified anti-HSL antibody causes similar reductions in muscle HSL protein concentration and in measured neutral lipase responses to contractions. The immunoreactive HSL in muscle is stimulated by adrenaline via β-adrenergic activation of cAMP-dependent protein kinase (PKA). From findings in adipocytes it is likely that PKA phosphorylates HSL at residues Ser563, Ser659and Ser660. Contraction probably also enhances muscle HSL activity by phosphorylation, because the contraction-induced increase in HSL activity is elevated by the protein phosphatase inhibitor okadaic acid and reversed by alkaline phosphatase. A novel signalling pathway in muscle by which HSL activity may be stimulated by protein kinase C (PKC) via extracellular signal-regulated kinase (ERK) has been demonstrated. In contrast to previous findings in adipocytes, in muscle the activation of ERK is not necessary for stimulation of HSL by adrenaline. However, contraction-induced HSL activation is mediated by PKC, at least partly via the ERK pathway. In fat cells ERK is known to phosphorylate HSL at Ser600. Hence, phosphorylation of different sites may explain the finding that in muscle the effects of contractions and adrenaline on HSL activity are partially additive. In line with the view that the two stimuli act by different mechanisms, training increases contraction-mediated HSL activation but diminishes adrenaline-mediated HSL activation in muscle. In conclusion, HSL is present in skeletal muscle and can be activated by phosphorylation in response to both adrenaline and muscle contractions. Training increases contraction-mediated HSL activation, but decreases adrenaline-mediated HSL activation in muscle.

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Block, K. P., B. W. Heywood, M. G. Buse, and A. E. Harper. "Activation of rat liver branched-chain 2-oxo acid dehydrogenase in vivo by glucagon and adrenaline." Biochemical Journal 232, no. 2 (December 1, 1985): 593–97. http://dx.doi.org/10.1042/bj2320593.

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The activity of liver branched-chain 2-oxo acid dehydrogenase complex was measured in rats fed on low-protein diets and given adrenaline, glucagon, insulin or dibutyryl cyclic AMP in vivo. Administration of glucagon or adrenaline (200 micrograms/100 g body wt.) resulted in a 4-fold increase in the percentage of active complex. As with glucagon and adrenaline, treatment of rats with cyclic AMP (5 mg/100 g body wt.) resulted in marked activation of branched-chain 2-oxo acid dehydrogenase. Insulin administration (1 unit/100 g body wt.) also resulted in activation of enzyme; however, these effects were less than those observed with glucagon and adrenaline. In contrast with the results obtained with low-protein-fed rats, administration of adrenaline (200 micrograms/100 g body wt.) to rats fed with an adequate amount of protein resulted in only a modest (14%) increase in the activity of the complex. The extent to which these hormones activate branched-chain 2-oxo acid dehydrogenase appears to be correlated with their ability to stimulate amino acid uptake into liver.

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Gardemann, A., H. Beck, and K. Jungermann. "Differential control of glycogenolysis and flow by arterial and portal acetylcholine in perfused rat liver." Biochemical Journal 271, no. 3 (November 1, 1990): 599–604. http://dx.doi.org/10.1042/bj2710599.

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The effects of acetylcholine on glucose and lactate balance and on perfusion flow were studied in isolated rat livers perfused simultaneously via the hepatic artery (100 mmHg, 25-35% of flow) and the portal vein (10 mmHg, 75-65% of flow) with a Krebs-Henseleit bicarbonate buffer containing 5 mM-glucose, 2 mM-lactate and 0.2 mM-pyruvate. Arterial acetylcholine (10 microM sinusoidal concentration) caused an increase in glucose and lactate output and a slight decrease in arterial and portal flow. These effects were accompanied by an output of noradrenaline and adrenaline into the hepatic vein. Portal acetylcholine elicited only minor increases in glucose and lactate output, a slight decrease in portal flow and a small increase in arterial flow, and no noradrenaline and adrenaline release. The metabolic and haemodynamic effects of arterial acetylcholine and the output of noradrenaline and adrenaline were strongly inhibited by the muscarinic antagonist atropine (10 microM). The acetylcholine-dependent alterations of metabolism and the output of noradrenaline were not influenced by the alpha 1-blocker prazosin (5 microM), whereas the output of adrenaline was increased. The acetylcholine-dependent metabolic alterations were not inhibited by the beta 2-antagonist butoxamine (10 microM), although the overflow of noradrenaline was nearly completely blocked and the output of adrenaline was slightly decreased. These results allow the conclusion that arterial, but not portal, acetylcholine caused sympathomimetic metabolic effects, without noradrenaline or adrenaline being involved in signal transduction.

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Koh, Ho-Jin, Michael F. Hirshman, Huamei He, Yangfeng Li, Yasuko Manabe, James A. Balschi, and Laurie J. Goodyear. "Adrenaline is a critical mediator of acute exercise-induced AMP-activated protein kinase activation in adipocytes." Biochemical Journal 403, no. 3 (April 12, 2007): 473–81. http://dx.doi.org/10.1042/bj20061479.

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Exercise increases AMPK (AMP-activated protein kinase) activity in human and rat adipocytes, but the underlying molecular mechanisms and functional consequences of this activation are not known. Since adrenaline (epinephrine) concentrations increase with exercise, in the present study we hypothesized that adrenaline activates AMPK in adipocytes. We show that a single bout of exercise increases AMPKα1 and α2 activities and ACC (acetyl-CoA carboxylase) Ser79 phosphorylation in rat adipocytes. Similarly to exercise, adrenaline treatment in vivo increased AMPK activities and ACC phosphorylation. Pre-treatment of rats with the β-blocker propranolol fully blocked exercise-induced AMPK activation. Increased AMPK activity with exercise and adrenaline treatment in vivo was accompanied by an increased AMP/ATP ratio. Adrenaline incubation of isolated adipocytes also increased the AMP/ATP ratio and AMPK activities, an effect blocked by propranolol. Adrenaline incubation increased lipolysis in isolated adipocytes, and Compound C, an AMPK inhibitor, attenuated this effect. Finally, a potential role for AMPK in the decreased adiposity associated with chronic exercise was suggested by marked increases in AMPKα1 and α2 activities in adipocytes from rats trained for 6 weeks. In conclusion, both acute and chronic exercise are significant regulators of AMPK activity in rat adipocytes. Our findings suggest that adrenaline plays a critical role in exercise-stimulated AMPKα1 and α2 activities in adipocytes, and that AMPK can function in the regulation of lipolysis.

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Inglis, G. C., C. J. Kenyon, J. A. M. Hannah, J. M. C. Connell, and S. G. Ball. "Does dopamine regulate aldosterone secretion in the rat?" Clinical Science 73, no. 1 (July 1, 1987): 93–97. http://dx.doi.org/10.1042/cs0730093.

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1. This study investigated the role of dopamine in the control of adrenal steroidogenesis. Adrenaline, noradrenaline and dopamine have been measured in plasma and in the adrenal zona glomerulosa and medulla of rats fed low, normal and high sodium diets and in zona glomerulosa tissue of rats with adrenal regeneration hypertension (ARH). 2. Adrenal concentrations (means ± se) of adrenaline, noradrenaline and dopamine in rats fed a normal diet were 1471 ± 335, 527 ± 75 and 51 ± 12 nmol/g in the medulla, and 66 ± 17, 18 ± 9 and 6 ± 1 nmol/g in the zona glomerulosa. The dopamine content of the zona glomerulosa was greater than could be accounted for by simple contamination from the medullary catecholamines and is commensurate with that of tissue with dopaminergic innervation. 3. Adrenal noradrenaline and adrenaline concentrations and plasma catecholamine and corticosterone concentrations were not affected by dietary sodium intake. Plasma aldosterone concentrations were > 3030.4, 339.8 ± 41.5 and 55.2 ± 11.0 pmol/l in rats fed low, normal and high sodium diets respectively. 4. Five weeks after right adrenalectomy and nephrectomy and left adrenal enucleation, ARH rat systolic blood pressure had increased by 47 mmHg. In the regenerated gland, the concentrations of noradrenaline and adrenaline were negligible but dopamine was present in amounts similar to that of a normal adrenal cortex. 5. Dopamine is present in the adrenal zona glomerulosa in significant amounts but does not decrease when dietary sodium intake is reduced and is not inversely related to aldosterone secretion. These observations are compatible with findings in vivo which indicate that dopamine inhibits aldosterone secretion by an extra-adrenal process involving increased clearance of the major aldosterone trophin angiotensin II.

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Oyekan, A. O., and J. H. Botting. "The Influence of Adrenaline on Gender Difference in Adenosine Diphosphate-Induced Aggregation of Platelets in the Rat." Thrombosis and Haemostasis 60, no. 03 (1988): 481–85. http://dx.doi.org/10.1055/s-0038-1646995.

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SummaryThe role of adrenaline on the inhibitory effects of physiological levels of oestradiol on ADP-induced intravascular aggregation has been studied. Platelets from pro-oestrous female rats aggregated less than those from dioestrous and male rats. Following adrenalectomy, there was no longer any difference(s) in the aggregability of the platelets to ADP in any of the rats. Adrenaline infusion (20 mg kg−1 hr−1) restored platelet aggregation to preadrenalectomy levels in pro-oestrous rate. Measurement of spontaneous fibrinolytic activity of the plasma showed highest value in pro-oestrous rats. Adrenalectomy reduced, while adrenaline infusion increased the fibrinolytic activity. The results suggest that the inhibitory effects of oestradiol on intravascular aggregation are dependent on endogenous adrenaline possibly working through the fibrinolytic pathway.

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Pelto-Huikko, M., T. Salminen, and A. Hervonen. "Localization of enkephalins in adrenaline cells and the nerves innervating adrenaline cells in rat adrenal medulla." Histochemistry 82, no. 4 (1985): 377–83. http://dx.doi.org/10.1007/bf00494067.

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Layland, J., I. S. Young, and J. D. Altringham. "The effects of adrenaline on the work- and power-generating capacity of rat papillary muscle in vitro." Journal of Experimental Biology 200, no. 3 (February 1, 1997): 503–9. http://dx.doi.org/10.1242/jeb.200.3.503.

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The work loop technique was used to examine the effects of adrenaline on the mechanics of cardiac muscle contraction in vitro. The length for maximum active force (Lmax) and net work production (Lopt) for rat papillary muscles was determined under control conditions (without adrenaline). The concentration of adrenaline producing the maximum inotropic effect was determined. This concentration was used in the remainder of the experiments. Sinusoidal strain cycles about Lopt were performed over a physiologically relevant range of cycle frequencies (4-11 Hz). Maximum work and the frequency for maximum work increased from 1.91 J kg-1 at 3 Hz in controls to 2.97 J kg-1 at 6 Hz with adrenaline. Similarly, maximum power output and the frequency for maximum power output (fopt) increased from 8.62 W kg-1 at 6 Hz in controls to 19.95 W kg-1 at 8 Hz with adrenaline. We suggest that the power-frequency relationship, derived using the work loop technique, represents a useful index with which to assess the effects of pharmacological interventions on cardiac muscle contractility.

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23

Bertrand, G., M. Nenquin, and J. C. Henquin. "Comparison of the inhibition of insulin release by activation of adenosine and α2-adrenergic receptors in rat β-cells." Biochemical Journal 259, no. 1 (April 1, 1989): 223–28. http://dx.doi.org/10.1042/bj2590223.

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Rat islets were used to compare the mechanisms whereby adenosine and adrenaline inhibit insulin release. Adenosine (1 microM-2.5 mM) and its analogue N6(-)-phenylisopropyladenosine (L-PIA) (1 nM-10 microM) caused a concentration-dependent but incomplete (45-60%) inhibition of glucose-stimulated release. L-PIA was more potent than D-PIA [the N6(+) analogue], but much less than adrenaline, which caused nearly complete inhibition (85% at 0.1 microM). 8-Phenyltheophylline prevented the inhibitory effect of L-PIA and 50 microM-adenosine, but not that of 500 microM-adenosine or of adrenaline. In contrast, yohimbine selectively prevented the inhibition by adrenaline. Adenosine and L-PIA thus appear to exert their effects by activating membrane A1 receptors, whereas adrenaline acts on alpha 2-adrenergic receptors. Adenosine, L-PIA and adrenaline slightly inhibited 45Ca2+ efflux, 86Rb+ efflux and 45Ca2+ influx in glucose-stimulated islets. The inhibition of insulin release by adenosine or L-PIA was totally prevented by dibutyryl cyclic AMP, but was only attenuated when adenylate cyclase was activated by forskolin or when protein kinase C was stimulated by a phorbol ester. Adrenaline, on the other hand, inhibited release under these conditions. It is concluded that inhibition of adenylate cyclase, rather than direct changes in membrane K+ and Ca2+ permeabilities, underlies the inhibition of insulin release induced by activation of A1-receptors. The more complete inhibition mediated by alpha 2-adrenergic receptors appears to result from a second mechanism not triggered by adenosine.

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24

Helman, J., G. S. Roth, and B. J. Baum. "Adrenergic-agonist-induced Ca2+ fluxes in rat parotid cells are not Na+-dependent." Biochemical Journal 230, no. 2 (September 1, 1985): 313–20. http://dx.doi.org/10.1042/bj2300313.

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We investigated the hypothesis that extracellular Na+ is required for the rapid mobilization of Ca2+ by rat parotid cells after adrenergic stimulation. When Na+ salts in the media were osmotically replaced with either choline chloride (+atropine) or sucrose, efflux of 45Ca2+ from preloaded cells, caused by 10 microM-(-)-adrenaline, was unchanged. Similarly adrenaline stimulated 45Ca2+ uptake into cells under nonsteady-state conditions in the presence or absence of Na+. Monensin, a Na+ ionophore, was able to elicit a modest increase in 45Ca2+ efflux, compared with controls. Studies of net 45Ca2+ flux, performed under near-steady-state conditions, showed that adrenaline caused net 45Ca2+ accumulation, whereas monensin caused net 45Ca2+ release. The effect of monensin required the presence of Na+ in the incubation medium. Both 1 mM-LaCl3 and 0.1 mM-D-600 prevented adrenaline-stimulated 45Ca2+ uptake into cells, but had no effect on monensin-induced changes. We conclude that (1) the rapid mobilization of Ca2+ by adrenergic agonists seen in rat parotid cells does not require a Na+out greater than Na+in gradient and (2) the nature of the monensin effect is quite different from the adrenergic-agonist-induced response.

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25

Ainscow, Edward K., and Martin D. Brand. "The responses of rat hepatocytes to glucagon and adrenaline." European Journal of Biochemistry 265, no. 3 (December 25, 2001): 1043–55. http://dx.doi.org/10.1046/j.1432-1327.1999.00820.x.

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FRANCH, Jesper, Rune ASLESEN, and Jørgen JENSEN. "Regulation of glycogen synthesis in rat skeletal muscle after glycogen-depleting contractile activity: effects of adrenaline on glycogen synthesis and activation of glycogen synthase and glycogen phosphorylase." Biochemical Journal 344, no. 1 (November 8, 1999): 231–35. http://dx.doi.org/10.1042/bj3440231.

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We investigated the effects of insulin and adrenaline on the rate of glycogen synthesis in skeletal muscles after electrical stimulation in vitro. The contractile activity decreased the glycogen concentration by 62%. After contractile activity, the glycogen stores were fully replenished at a constant and high rate for 3 h when 10 m-i.u./ml insulin was present. In the absence of insulin, only 65% of the initial glycogen stores was replenished. Adrenaline decreased insulin-stimulated glycogen synthesis. Surprisingly, adrenaline did not inhibit glycogen synthesis stimulated by glycogen-depleting contractile activity. In agreement with this, the fractional activity of glycogen synthase was high when adrenaline was present after exercise, whereas adrenaline decreased the fractional activity of glycogen synthase to a low level during stimulation with insulin. Furthermore, adrenaline activated glycogen phosphorylase almost completely during stimulation with insulin, whereas a much lower activation of glycogen phosphorylase was observed after contractile activity. Thus adrenaline does not inhibit contraction-stimulated glycogen synthesis.

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27

Pal, Palash Kumar, Swaimanti Sarkar, Sanatan Mishra, Sreya Chattopadhyay, Aindrila Chattopadhyay, and Debasish Bandyopadhyay. "Amelioration of adrenaline induced oxidative gastrointestinal damages in rat by melatonin through SIRT1-NFκB and PGC1α-AMPKα cascades." Melatonin Research 3, no. 4 (October 9, 2020): 482–502. http://dx.doi.org/10.32794/mr11250074.

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Adrenaline at high pharmacological doses may lead to oxidative damages in diverse organs including gut. In this study, we attempt to elucidate the potentially protective effects of melatonin on gastrointestinal (GI) tissue damages induced by adrenaline. Rats were injected (s.c.) with different doses (0.125, 0.25 and 0.50 mg/kg) of adrenaline bitartrate (AD) for 15 days with or without melatonin (2.5, 5 and 10 mg/kg; orally). The results showed that adrenaline caused massive histological and ultra-structural GI injuries and melatonin (20 mg/kg) effectively protected these injuries. The protective mechanisms are related to the antioxidant and anti-inflammatory activities of melatonin indicated by increased glutathione levels and antioxidant enzymes as well as decreased oxidative stress markers and pro-inflammatory cytokines in GI tissues. The signal pathways of melatonin include up-regulating expression of Nrf2, SIRT1 and Bcl2, while down-regulating NFκB, TNFα and Bax. Melatonin also targeted mitochondrial energy homeostasis and biogenesis by up-regulating expression of PGC1α, AMPKα and SOD2 and reduced leakage of cytochrome c. The SIRT1-NFκB and PGC1α-AMPKα signal transduction pathways seem to play the central roles involving in melatonin’s protective effects on gastric damages induced by the high doses of adrenaline.

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NORTHEMANN, WOLFGANG, MICHAEL HEISIG, DIETER KUNZ, JOACHIM BAUER, MANFRED BIRMELIN, THUY-ANH TRAN-THI, KARL DECKER, and PETER C. HEINRICH. "Biosynthesis of rat α2-macroglobulin." Biochemical Society Transactions 13, no. 2 (April 1, 1985): 285–88. http://dx.doi.org/10.1042/bst0130285.

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29

Sanin, V. V., A. I. Yakovets, K. V. Rozova, Yu P. Korkach, Yu V. Goshovska, I. V. Shargorodska, and S. O. Rykov. "EFFECT OF N-ACETYLCARNOSINE CONTAINED EYE DROP ON CATECHOLAMINE-INDUCED MORPHOFUNCTIONAL DAMAGE IN RAT RETINA." Fiziolohichnyĭ zhurnal 66, no. 4 (August 20, 2020): 64–71. http://dx.doi.org/10.15407/fz66.04.064.

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The effects of N-acetylcarnosine (NAC)-contained eye drop ‘Clarastil’ on a model of adrenaline-induced high intraocular pressure (IOP) in Wistar rats were studied. The retina ultrastructure and markers of oxidative stress have been studied. NAC was found to have no significant effect on edema in the retinal ultrastructure, did not reduce endothelial thickening and histogemic barrier, and accordingly did not affect the value of IOP after prolonged adrenaline administration. However, the introduction of the eye drop prevented the swelling of the mitochondria, the formation of vacuolated crystals and probably stimulated energy production as a compensatory mechanism under conditions of hypercatecholemia. In addition, NAC significantly reduced adrenaline-induced overproduction of reactive oxygen species and lipid peroxidation products in eye tissues, indicating its antioxidant effect.

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30

Pal, Palash Kumar, Bharati Bhattacharjee, Arnab Kumar Ghosh, Aindrila Chattopadhyay, and Debasish Bandyopadhyay. "Adrenaline induced disruption of endogenous melatoninergic system, antioxidant and inflammatory responses in the gastrointestinal tissues of male Wistar rat: an in vitro study." Melatonin Research 1, no. 1 (December 3, 2018): 109–31. http://dx.doi.org/10.32794/mr11250007.

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The current study aimed to demonstrate the potentially adverse effects of adrenaline, an endogenous stressor, on the melatonergic system, oxidative status, antioxidative responses and inflammatory markers in different parts of gastrointestinal tract of Wistar rat. These included stomach, duodenum and colon and they were incubated with different concentrations (2.5, 5.0 and 10.0 µg/mL) of adrenaline for 1h, respectively. The levels of melatonin, gene expressions of arylalkylamine N-acetyltransferase (AANAT) and melatonin receptor 1 (MT1) as well as other stress-induced parameters including NF-kB expression, levels of cAMP, calcium, malondialdehyde, protein carbonyl content, reduced glutathione, nitrate, superoxide dismutase, catalase, glutathione peroxidase and glutathione S-transferase, tumour necrosis factor-α, IL-1β, IL6 and IL10 were systemically measured in these tissues. An adrenaline dose-dependent decrease in level of melatonin, AANAT, MT1 and NF-kB in these tissues were observed. In contrast, the profound increases in the levels of cAMP, calcium and all oxidative stress markers, inflammatory cytokines (except IL10), and activities of antioxidant enzymes (except superoxide dismutase) were observed after adrenaline treatment. A maximum effect was found in tissues treated with 5 µg/mL of adrenaline. The Correlation studies between melatonin level and other parameters (any two at a time) indicated a potentially physiological interplay between adrenaline stress and melatonin tissue levels. Collectively, the results provided the novel data on the adverse effects of adrenaline on the endogenous melatonergic system, antioxidant and inflammatory responses in the gastrointestinal tissues of rats.

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31

Poggioli, J., J. P. Mauger, and M. Claret. "Effect of cyclic AMP-dependent hormones and Ca2+-mobilizing hormones on the Ca2+ influx and polyphosphoinositide metabolism in isolated rat hepatocytes." Biochemical Journal 235, no. 3 (May 1, 1986): 663–69. http://dx.doi.org/10.1042/bj2350663.

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The effect of the interaction between the Ca2+-mobilizing hormone adrenaline, used as alpha-adrenergic agonist, and cyclic AMP-dependent hormones, including beta-adrenergic agonists and glucagon, on the initial 45Ca2+ uptake rate and polyphosphoinositide metabolism were investigated in isolated rat hepatocytes. Each hormone alone increased the initial 45Ca2+ uptake rate. When adrenaline was added without inhibitor, it induced a rise in the initial 45Ca2+ uptake rate larger than the sum of the rises elicited by its alpha and beta components singly. Similarly, when adrenaline was used as an alpha-agonist and added together with glucagon, it enhanced the initial 45Ca2+ uptake rate synergistically. Kinetic analysis of the initial 45Ca2+ uptake rate measured at different Ca2+ concentrations suggested that the increased influx elicited by the combination of adrenaline as alpha-adrenergic agonist and glucagon reflects an activation of the rate of Ca2+ transport via a homogeneous population of Ca2+ channels or carriers. Dose-response curves for the alpha-adrenergic action of adrenaline or glucagon applied in the presence of increasing doses of glucagon or adrenaline showed that each hormone increases the maximal response to the other without affecting its ED50. Measurement of polyphosphoinositide hydrolysis and of the inositol phosphates formed in the presence of adrenaline or vasopressin and/or glucagon showed that Ca2+-mobilizing hormones and glucagon had no synergistic effects on inositol 1,4,5-trisphosphate production. It is therefore proposed that the synergistic action of glucagon and Ca2+-mobilizing hormones on Ca2+ influx occurs at a step that takes place close to the Ca2+ channels or carriers themselves. The Ca2+ gating involved might be mainly controlled by two products, one of them arising from the polyphosphoinositide metabolism, and the other from the increase in internal cyclic AMP.

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32

Wlllerth, M., and J. A. Thornhill. "The effects of endogenous opioids on tension development of isolated, electrically stimulated rat atria." Canadian Journal of Physiology and Pharmacology 65, no. 6 (June 1, 1987): 1227–33. http://dx.doi.org/10.1139/y87-194.

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The possible inotropic effects of all three classes of endogenous opioids were tested alone or in combination with noradrenaline, adrenaline, or carbachol on electrically stimulated atria isolated from male Sprague–Dawley rats. Noradrenaline (6.0 and 12 μM) and adrenaline (4.0 and 8.0 μM) injections caused marked but transient (5 min) dose-related increases in atrial tension compared with preinjection control values, whereas carbachol (0.14 and 1.4 μM) caused a more potent and prolonged (over 15 min) dose-related decrease in atrial tension development. Adrenal enkephalins (0.3–4.0 μM) of methionine enkephalin, leucine enkephalin, Met-enkephalin-Arg6-Phe7, and Met-enkephalin-Arg6-Gly7-Leu8, β-endorphin (0.2–2.0 μM), or dynorphin A(1–13) (0.2–2.0 μM) did not change atrial tension for a 15-min postadministration test period. In addition, these opioids did not affect the positive inotropic effects of noradrenaline (12 μM) or adrenaline (8.0 μM) or the negative inotropic actions of carbachol (1.4 μM) when the same doses of noradrenaline, adrenaline, or carbachol were given alone. These data indicate that endogenous opioids given in micromolar concentrations tested did not affect atrial tension development of electrically stimulated rat atria. Comparing these data with those of past literature, it is suggested that circulating endogenous opioids probably do not have any direct effects on the rat myocardium to affect myocardial contractility.

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33

Kilgour, E., and R. G. Vernon. "Catecholamine activation of pyruvate dehydrogenase in white adipose tissue of the rat in vivo." Biochemical Journal 241, no. 2 (January 15, 1987): 415–19. http://dx.doi.org/10.1042/bj2410415.

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Intraperitoneal injections of noradrenaline or adrenaline into rats increased the proportion of pyruvate dehydrogenase in the active state in white adipose tissue; this effect of catecholamines was also apparent in streptozotocin-diabetic rats, showing that it was not due to an increase in serum insulin concentration. The catecholamine-induced increase in pyruvate dehydrogenase of white adipose tissue in vivo was completely blocked by prior injection of either the beta-antagonist propranolol or the alpha 1-antagonist prazosin. Cervical dislocation of conscious rats increased pyruvate dehydrogenase activity of white adipose tissue, which was prevented by prior injection of propranolol. Adrenaline (30 nM) activated pyruvate dehydrogenase in white adipocytes in vitro; the maximum effect of adrenaline required activation of both alpha 1- and beta-receptors. The results show that catecholamines activate pyruvate dehydrogenase of white adipose tissue both in vivo and in vitro and that this effect is mediated by a combination of alpha 1- and beta-adrenergic receptors.

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34

Jensen, Kjell Briseid, and Reidar Bredo Sund. "The Inhibitory Action of Adrenaline on the Isolated Rat Uterus." Acta Pharmacologica et Toxicologica 17, no. 2 (March 13, 2009): 173–81. http://dx.doi.org/10.1111/j.1600-0773.1960.tb01241.x.

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35

Jensen, Kjell Briseid, and Anne Marie Venneröd. "Determination of Adrenaline on the Isolated Serotonin-Stimulated Rat Uterus." Acta Pharmacologica et Toxicologica 18, no. 1 (March 13, 2009): 80–88. http://dx.doi.org/10.1111/j.1600-0773.1961.tb00315.x.

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36

Bouryi, Vitali A., and David I. Lewis. "Adrenaline modulates multiple conductances in rat vagal motoneurones in vitro." Neuroreport 12, no. 8 (June 2001): 1709–13. http://dx.doi.org/10.1097/00001756-200106130-00038.

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37

Kujacic, Mirjana, Lars O. Hansson, and Arvid Carlsson. "Acute dopaminergic influence on plasma adrenaline levels in the rat." European Journal of Pharmacology 273, no. 3 (February 1995): 247–57. http://dx.doi.org/10.1016/0014-2999(94)00699-8.

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38

Quintana, I., M. Grau, F. Moreno, C. Soler, I. Ramírez, and M. Soley. "The early stimulation of glycolysis by epidermal growth factor in isolated rat hepatocytes is secondary to the glycogenolytic effect." Biochemical Journal 308, no. 3 (June 15, 1995): 889–94. http://dx.doi.org/10.1042/bj3080889.

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We have studied the relationship between the effect of epidermal growth factor (EGF) on glycogen metabolism and its effect on glycolysis, in rat hepatocyte suspensions. Although 10 nM glucagon or 10 microM adrenaline increased glycogen degradation by more than 120%, 10 nM EGF increased glycogenolysis by less than 20% in hepatocytes incubated in glucose-free medium. Both glucagon and adrenaline increased phosphorylase a activity by more than 130%; EGF increased this activity by about 30%. Under basal conditions, 65% of the glucosyl residues were released as free glucose and about 30% ended up as C3 molecules (lactate and pyruvate). Both glucagon and adrenaline decreased the proportion of glucosyl units that rendered glycolysis end-products (to 2% for glucagon and 6% for adrenaline) and increased the proportion that ended up as free glucose (to 94% and 88% of the glucosyl residues for glucagon and adrenaline respectively). EGF increased the production of both free glucose and lactate+pyruvate, but the proportion of glucosyl residues that ended up as free glucose or glycolysis end-products was unchanged. In glycogen-depleted hepatocytes incubated in the presence of 25 mM glucose, EGF affected neither glycogen deposition nor glycolysis. EGF increased cytosolic free Ca2+, and neomycin decreased both the Ca2+ signal and the glycogenolytic effect. In conclusion, our results indicate that the effect of EGF on glycolysis is secondary to the Ca(2+)-mediated stimulation of glycogenolysis in rat hepatocyte suspensions.

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39

Hildebrandt, E. F., D. B. Buxton, and M. S. Olson. "Acute regulation of the branched-chain 2-oxo acid dehydrogenase complex by adrenaline and glucagon in the perfused rat heart." Biochemical Journal 250, no. 3 (March 15, 1988): 835–41. http://dx.doi.org/10.1042/bj2500835.

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Rates of transamination and decarboxylation of [1-14C]leucine at a physiological concentration (0.1 mM) were measured in the perfused rat heart. In hearts from fasted rats, metabolic flux through the branched-chain 2-oxo acid dehydrogenase reaction was low initially, but increased gradually during the perfusion period. The increase in 14CO2 production was accompanied by an increase in the amount of active branched-chain 2-oxo acid dehydrogenase complex present in the tissue. In hearts from rats fed ad libitum, extractable branched-chain dehydrogenase activity was low initially, but increased rapidly during perfusion, and high rates of decarboxylation were attained within the first 10 min. Infusion of glucagon, adrenaline, isoprenaline, or adrenaline in the presence of phentolamine all produced rapid, transient, inhibition (40-50%) of the formation of 4-methyl-2-oxo[1-14C]pentanoate and 14CO2 within 1-2 min, but the specific radioactivity of 4-methyl-2-oxo[14C]pentanoate released into the perfusate remained constant. Glucagon and adrenaline infusion also resulted in transient decreases (16-24%) in the amount of active branched-chain 2-oxo acid dehydrogenase. In hearts from fasted animals, infusion for 10 min of adrenaline, phenylephrine, or adrenaline in the presence of propranolol, but not infusion of glucagon or isoprenaline, stimulated the rate of 14CO2 production 3-fold, and increased 2-fold the extractable branched-chain 2-oxo acid dehydrogenase activity. These results demonstrate that stimulation of glucagon or beta-adrenergic receptors in the perfused rat heart causes a transient inhibition of branched-chain amino acid metabolism, whereas alpha-adrenergic stimulation causes a slower, more sustained, enhancement of branched-chain amino acid metabolism. Both effects reflect interconversion of the branched-chain 2-oxo acid dehydrogenase complex between active and inactive forms. Also, these studies suggest that the concentration of branched-chain 2-oxo acid available for decarboxylation can be regulated by adrenaline and glucagon.

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40

Kuchmenko, O. B., D. M. Petukhov, I. N. Yevstratova, L. S. Mkhitaryan, and G. V. Donchenko. "Ефект попередників і модуляторів біосинтезу убіхінону на вміст і функціонування убіхінону та оксидативний статус у серці при введенні адреналіну." Visnyk of Dnipropetrovsk University. Biology, medicine 2, no. 1 (June 17, 2011): 68–74. http://dx.doi.org/10.15421/021111.

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Preventive and/or subsequent application of precursors and modulators complexes of ubiquinone biosynthesis under the adrenaline treatment reduces free-radical lipid and protein peroxidation intensity, but increases superoxide dismutase activity and improves activities of the mitochondrial electron-transport chain complexes. EPM and EPMD complexes can be effective anti-hypoxic remedies that promote normalization of the energy metabolism in ischemic heart.

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41

Burns, G., B. L. Brown, and P. R. M. Dobson. "Diurnal variation in the effect of potassium depolarization on vasoactive intestinal polypeptide release from rat hypothalamus: a possible role for adrenaline." Journal of Endocrinology 116, no. 3 (March 1988): 335–41. http://dx.doi.org/10.1677/joe.0.1160335.

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ABSTRACT We have previously reported a lack of effect of a depolarizing concentration of K+ on the release of vasoactive intestinal polypeptide (VIP) from the perifused rat hypothalamus, and suggested that this was due to the presence of an endogenous inhibitor of the release of VIP. In this study we report that the VIP response to K+ was restored if the hypothalami were obtained from animals killed during the dark phase of the light–dark cycle. Adrenaline blocked the K+-stimulated release of VIP when used at a concentration of 0·1 μmol/l; however, at a higher concentration (10 μmol/l) adrenaline stimulated the basal release of VIP. The use of specific receptor antagonists indicated that this dual effect of adrenaline was mediated through two distinct receptors, a stimulatory β-receptor and an inhibitory α2-receptor. The suggestion that adrenaline might be the endogenous inhibitor of the release of VIP, mediating the diurnal variation in the effect of K+, was supported by studies where 50 mmol K+/l was perifused concomitantly with an α2-antagonist, restoring the VIP response to K+ in light-phase hypothalami. In conclusion, adrenaline has a dual role in the control of VIP release and may function to inhibit the K+-stimulated release of VIP in our system. J. Endocr. (1988) 116, 335–341

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Higuchi, T., H. Negoro, and J. Arita. "Reduced responses of prolactin and catecholamine to stress in the lactating rat." Journal of Endocrinology 122, no. 2 (August 1989): 495–98. http://dx.doi.org/10.1677/joe.0.1220495.

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ABSTRACT Prolactin, GH, TSH, adrenaline and noradrenaline responses to the stress of immobilization were compared between lactating and non-lactating dioestrous rats. The concentrations of GH in plasma were reduced to a similar degree by the immobilization of lactating and non-lactating rats, and TSH levels were unchanged in both groups. The increases in plasma concentrations of adrenaline and noradrenaline induced by stress were significantly smaller in lactating than in non-lactating rats. Immobilization caused a marked increase in prolactin levels in the plasma of non-lactating rats but no increase in lactating rats. These changes may help to save energy and maintain milk production during the period of lactation. Journal of Endocrinology (1989) 122, 495–498

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43

CLARK, Andrew D. H., Eugene J. BARRETT, Stephen RATTIGAN, Michelle G. WALLIS, and Michael G. CLARK. "Insulin stimulates laser Doppler signal by rat muscle in vivo, consistent with nutritive flow recruitment." Clinical Science 100, no. 3 (January 30, 2001): 283–90. http://dx.doi.org/10.1042/cs1000283.

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Insulin-mediated increases in limb blood flow are thought to enhance glucose uptake by skeletal muscle. Using the perfused rat hindlimb, we report that macro laser Doppler flowmetry (LDF) probes positioned on the surface of muscle detect changes in muscle capillary (nutritive) flow. With this as background, we examined the effects of insulin and adrenaline (epinephrine), which are both known to increase total leg blood flow, on the LDF signals from scanning and stationary probes on the muscle surface in vivo. The aim is to assess the relationship between capillary recruitment, total limb blood flow and glucose metabolism. Glucose infusion rate, femoral arterial blood flow (FBF) and muscle LDF, using either scanning or a stationary probe positioned over the biceps femoris muscle, were measured. With scanning LDF, animals received insulin (10 m-units·min-1·kg-1), adrenaline (0.125 µg·min-1·kg-1) or saline. By 1 h, insulin had increased the glucose infusion rate from 0 to 128 µmol·min-1·kg-1 and the scanning LDF had increased by 62±8% (P < 0.05), but FBF was unaffected. Adrenaline increased FBF by 49% at 15 min, but LDF was unchanged. With saline at 1 h, neither FBF nor LDF had changed. With the stationary LDF surface probe, insulin at 1 h had increased FBF by 47% (P < 0.05) and LDF by 47% (P < 0.05) relative to saline controls. Adrenaline increased FBF (39%), but LDF was unaltered. The stimulation of LDF by insulin is consistent with capillary recruitment (nutritive flow) as part of the action of this hormone in vivo. The recruitment may be independent of changes in total flow, as adrenaline, which also increased FBF, did not increase LDF. The time of onset suggests that LDF closely parallels glucose uptake. Thus, depending on probe design, measurement of muscle haemodynamic effects mediated by insulin in normally responsive and insulin-resistant patients should be possible.

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44

Kalén, A., E. L. Appelkvist, G. Dallner, Bertil Andersson, and Hans-Erik Åkerlund. "Biosynthesis of Ubiquinone in Rat Liver." Acta Chemica Scandinavica 41b (1987): 70–72. http://dx.doi.org/10.3891/acta.chem.scand.41b-0070.

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Appelkvist, Eeva-Liisa, Ole Hammerich, Vernon D. Parker, Bertil Andersson, and Hans-Erik Åkerlund. "Dolichol Biosynthesis in Rat Liver Peroxisomes." Acta Chemica Scandinavica 41b (1987): 73–75. http://dx.doi.org/10.3891/acta.chem.scand.41b-0073.

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McCOLL, K. E. L., F. M. BOND, G. G. THOMPSON, and M. R. MOORE. "Haem biosynthesis in the Gunn rat." Biochemical Society Transactions 14, no. 5 (October 1, 1986): 921–22. http://dx.doi.org/10.1042/bst0140921.

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47

Gomez-Sanchez, Celso E., Ming Yi Zhou, Eduardo N. Cozza, Hiroyuki Morita, Mark F. Foecking, and Elise P. Gomez-Sanchez. "Aldosterone Biosynthesis in the Rat Brain1." Endocrinology 138, no. 8 (August 1997): 3369–73. http://dx.doi.org/10.1210/endo.138.8.5326.

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48

Tekle, Michael, Magnus Bentinger, Tomas Nordman, Eeva-Liisa Appelkvist, Tadeusz Chojnacki, and Jerker M. Olsson. "Ubiquinone Biosynthesis in Rat Liver Peroxisomes." Biochemical and Biophysical Research Communications 291, no. 5 (March 2002): 1128–33. http://dx.doi.org/10.1006/bbrc.2002.6537.

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49

Tsuchiya, Yugo, Fiona C. Denison, Richard B. Heath, David Carling, and David Saggerson. "5′-AMP-activated protein kinase is inactivated by adrenergic signalling in adult cardiac myocytes." Bioscience Reports 32, no. 2 (November 21, 2011): 197–209. http://dx.doi.org/10.1042/bsr20110076.

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In adult rat cardiac myocytes adrenaline decreased AMPK (AMP-activated protein kinase) activity with a half-time of approximately 4 min, decreased phosphorylation of AMPK (α-Thr172) and decreased phosphorylation of ACC (acetyl-CoA carboxylase). Inactivation of AMPK by adrenaline was through both α1- and β-ARs (adrenergic receptors), but did not involve cAMP or calcium signalling, was not blocked by the PKC (protein kinase C) inhibitor BIM I (bisindoylmaleimide I), by the ERK (extracellular-signal-regulated kinase) cascade inhibitor U0126 or by PTX (pertussis toxin). Adrenaline caused no measurable change in LKB1 activity. Adrenaline decreased AMPK activity through a process that was distinct from AMPK inactivation in response to insulin or PMA. Neither adrenaline nor PMA altered the myocyte AMP:ATP ratio although the adrenaline effect was attenuated by oligomycin and by AICAR (5-amino-4-imidazolecarboxamide-1-β-D-ribofuranoside), agents that mimic ‘metabolic stress’. Inactivation of AMPK by adrenaline was abolished by 1 μM okadaic acid suggesting that activation of PP2A (phosphoprotein phosphatase 2A) might mediate the adrenaline effect. However, no change in PP2A activity was detected in myocyte extracts. Adrenaline increased phosphorylation of the AMPK β-subunit in vitro but there was no detectable change in vivo in phosphorylation of previously identified AMPK sites (β-Ser24, β-Ser108 or β-Ser182) suggesting that another site(s) is targeted.

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Mishra, Sanatan, Aindrila Chattopadhyay, Shamreen Naaz, Arnab K. Ghosh, Asish Ranjan Das, and Debasish Bandyopadhyay. "Oleic acid ameliorates adrenaline induced dysfunction of rat heart mitochondria by binding with adrenaline: An isothermal titration calorimetry study." Life Sciences 218 (February 2019): 96–111. http://dx.doi.org/10.1016/j.lfs.2018.12.035.

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Journal articles on the topic 'Biosynthesis of rat adrenaline'

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