Plasma protein binding of catecholamines, prazosin and propranolol in diabetes mellitus

Trovik, T.; Jaeger, Ragnhild; Jorde, Rolf; Ingebretsen, Ole C.; Sager, Georg

doi:10.1007/bf02333020

Cited by 15 publications

(8 citation statements)

References 16 publications

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“…This is in agreement with previous studies performed in humans (Zia et al, 1971;Danon and Sapira, 1972;Powis, 1975;Trovik et al, 1992) and in dogs (Teixeira et al, 1979).…”

Section: Discussionsupporting

confidence: 94%

“…If the CAs present in the erythrocytes are taken into account, then the percentage of binding of CAs to plasma proteins was even less (11%). Previous experiments (Zia et al, 1971;Danon and Sapira, 1972;May et al, 1974;Powis, 1975;Teixeira et al, 1979;Sager et al, 1987;Trovik et al, 1992) reported that the percentage of binding of CAs to plasma proteins varied from 14% to 50%. The results of these experiments were calculated as if all CAs were present only in the plasma.…”

Section: Discussionmentioning

confidence: 96%

“…Several authors found such a binding of CA or their derivatives. They used various techniques, such as equilibrium dialysis (Powis, 1975;Sager et al, 1987;Boomsma et al, 1991;Trovik et al, 1992), electrophoresis (Mirkin et al, 1966;Teixeira et al, 1979) and gel ¢ltration (Zia et al, 1971;Danon and Sapira, 1972;May et al, 1974;Powis, 1975;Teixeira et al, 1979). Although some authors could not ¢nd any interaction between CA and albumin (Bickel and Bovet, 1962;Mirkin et al, 1966), others reported the binding of A and NA to serum albumin (Danon and Sapira, 1972), a-or bglobulins (Mirkin et al, 1966;Teixeira et al, 1979), a-acid glycoprotein (Sager et al, 1987), lipoproteins and immunoglobulin M (Powis, 1975).…”

Section: Introductionmentioning

confidence: 95%

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Binding and Clearance of Radioactive Adrenaline and Noradrenaline in Sheep Blood

Kahlbacher²,

Patzl

et al. 2006

Vet Res Commun

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An understanding of the conditions influencing protein binding of catecholamines (CAs) is important in studying their metabolic effects. Unfortunately, reports on plasma protein binding of CAs are scarce, conflicting and mainly performed in vitro. The aim of our in vivo and in vitro studies was to investigate binding and clearance of radioactive adrenaline (epinephrine) ((3)H-A), noradrenaline (norepinephrine) ((3)H-NA) and their metabolites in sheep blood. The time course of the radioactivity in the blood after intravenous injection of (3)H-A and (3)H-NA (3.7 MBq each) in 4 sheep (2 of each sex; total of 8 administrations) was determined. Blood samples were taken from the jugular vein. The highest radioactivity was observed in the first sample (5 min) following injection. Radioactivity showed a biphasic disappearance. An initial stage, in which radioactivity decreased rapidly (within 1 h) after the injection, was followed by a slow stage, lasting for up to 1 month, until background levels were reached. In vitro results indicated that NA and A were present not only in plasma (70%) but also in the erythrocytes (30%; mainly bound to haemoglobin). Sephadex G-25 gel filtration revealed that from the plasma fraction about 15% was strongly bound to proteins (mainly albumin). These results demonstrate that previous experiments in this field have overestimated the percentage of CAs bound to plasma proteins, because binding to haemoglobin was previously not known. In the future, efforts should be made to characterize the adduct products of CAs and establish an assay to determine them in vivo. If this could be achieved, it would yield a valuable tool for measuring the stress experienced for a longer period.

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“…This is in agreement with previous studies performed in humans (Zia et al, 1971;Danon and Sapira, 1972;Powis, 1975;Trovik et al, 1992) and in dogs (Teixeira et al, 1979).…”

Section: Discussionsupporting

confidence: 94%

Section: Discussionmentioning

confidence: 96%

Section: Introductionmentioning

confidence: 95%

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Binding and Clearance of Radioactive Adrenaline and Noradrenaline in Sheep Blood

Kahlbacher²,

Patzl

et al. 2006

Vet Res Commun

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“…Uremic substance due to ARF condition has been shown to decrease the plasma protein binding of acidic drugs. 5) On the other hand, basic drugs such as propranorol binds mainly to an inflammatory protein in plasma, a 1 -acid glycoprotein, 22) which is induced by ARF condition. Since the physicochemical property of CsA is neutral, CsA rather distributes to lipid fractions in plasma with an oil/water partition rule.…”

Section: Discussionmentioning

confidence: 99%

Evaluation of Factors to Decrease Bioavailability of Cyclosporin A in Rats with Gentamicin-Induced Acute Renal Failure

Shibata¹,

Inoue²,

Fukumoto³

et al. 2004

Biological & Pharmaceutical Bulletin

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Focusing on the disposition of cyclosporin A (CsA) in the liver and intestine, effects of gentamicin-induced acute renal failure (ARF) on the decreased oral bioavailability of CsA were evaluated in rats. The area under the CsA concentration-time curve (AUC) in ARF rats after oral administration (5 mg/kg) significantly decreased by 43% as compared to the control, while the apparent oral clearance significantly increased by 76% of the control. The portal AUC of CsA in ARF rats with bile flow decreased by 67% as compared to the control rats. Without bile flow, the portal AUC of CsA in control rats decreased by 50% as compared to those with bile flow, whereas ARF rats without bile flow showed no notable change as compared to those with bile flow. The AUC of CsA mono-oxidative metabolite via CYP3A (M-OH) in ARF rats after oral or intravenous administration increased significantly by 84% or 241%, respectively, while there was no difference in the portal M-OH between control and ARF rats, suggesting that the elimination of M-OH was prolonged because of nephrotoxicity. Although the exsorption clearance of CsA from the blood circulation to the intestine after intravenous administration to ARF rats decreased significantly as compared to the control; and basolateral-to-apical transport of CsA through Caco-2 monolayers was significantly retarded in the presence of uremic toxins, there was no significant change in the total body clearance of CsA between ARF and control rats. Moreover, there were no effects of uremic toxins on the protein binding of CsA in plasma. These observations suggest that hepatic or intestinal CYP3A and P-glycoproteine (P-gp) are not likely to be concerned with lowering the oral bioavailability of CsA, and that bile function under the ARF condition induced by gentamicin is responsible for a marked decrease in the fraction absorbed of CsA in the small intestine.

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“…Protein binding in GDM is of interest not just because there is a paucity of information concerned with it but because there are reports of changes to this parameter in other forms of diabetes (Ruiz-Cabello and Erill, 1984;Trovik et al, 1992;Arredondo et al, 1999). For example, it has been demonstrated that the plasma protein binding of itraconazole in patients with type 1 and type 2 diabetes is significantly less than in healthy volunteers (Arredondo et al, 1999).…”

mentioning

confidence: 97%

Impact of Hyperlipidemia on Plasma Protein Binding and Hepatic Drug Transporter and Metabolic Enzyme Regulation in a Rat Model of Gestational Diabetes

Anger¹,

Piquette-Miller²

2010

J Pharmacol Exp Ther

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It is currently unknown whether gestational diabetes mellitus (GDM), a prevalent obstetrical complication, compounds the changes in drug disposition that occur naturally in pregnancy. Hyperlipidemia occurs in GDM. Using a rat model of GDM, we determined whether excess lipids compete with drugs for plasma protein binding. Because lipids activate nuclear receptors that regulate drug transporters and metabolic enzymes, we used proteome analysis to determine whether hyperlipidemia indirectly leads to the dysregulation of these proteins in the liver. GDM was induced on gestational day 6 (GD6) via streptozotocin injection. Controls received either vehicle alone or streptozotocin with subsequent insulin treatment. Liver and plasma were collected on GD20. Glyburide and saquinavir protein binding was determined by ultrafiltration, and an established solvent method was used for plasma delipidation. Proteomics analysis was performed by using isobaric tags for relative and absolute quantitation methodology with membrane-enriched hepatic protein samples. Relative to controls, GDM rat plasma contained more cholesterol and triglycerides. Plasma protein binding of glyburide and saquinavir was decreased in GDM. Delipidation normalized protein binding in GDM plasma. Proteins linked to lipid metabolism were strongly affected in the GDM proteomics data set, with prohyperlipidemic and antihyperlipidemic changes observed, and formed networks that implicated several nuclear receptors. Up-regulation of drug transporters and metabolic enzymes was observed (e.g., multidrug resistance 1/2, CYP2A1, CYP2B9, and CYP2D3). In this study, GDM-induced hyperlipidemia decreased protein binding and was associated with drug transporter and metabolic enzyme up-regulation in the liver. Both of these findings could change drug disposition in affected pregnancies, compounding changes associated with pregnancy itself.

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Plasma protein binding of catecholamines, prazosin and propranolol in diabetes mellitus

Cited by 15 publications

References 16 publications

Binding and Clearance of Radioactive Adrenaline and Noradrenaline in Sheep Blood

Binding and Clearance of Radioactive Adrenaline and Noradrenaline in Sheep Blood

Evaluation of Factors to Decrease Bioavailability of Cyclosporin A in Rats with Gentamicin-Induced Acute Renal Failure

Impact of Hyperlipidemia on Plasma Protein Binding and Hepatic Drug Transporter and Metabolic Enzyme Regulation in a Rat Model of Gestational Diabetes

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