Prednisolone Binding to Plasma Proteins in Domestic Species

Alvinerie, M.; Houin, Georges; Toutain, P. L.

doi:10.1002/jps.2600771107

Cited by 14 publications

(11 citation statements)

References 9 publications

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“…Furthermore, prednisolone does not exhibit extensive plasma protein binding in dogs (~50%-70% at the concentration tested in this study; Frey et al, 1980;Alvinerie et al, 1988), and the binding to albumin is nonspecific (Alvinerie et al, 1988 It is important to note that the effect of prednisolone on the protein binding of MPA may not necessarily be reflected by a higher concentration of unbound MPA in plasma in vivo and may be biologically irrelevant. An increase in the free fraction of the drug could be offset by the distribution of the MPA into tissues and by a faster elimination of the drug from the body.…”

Section: Discussionmentioning

confidence: 62%

Ex vivo binding of the immunosuppressant mycophenolic acid to dog and cat plasma proteins and the effect of co‐incubated dexamethasone and prednisolone

Morassi

Vélez

Slovak

et al. 2018

Vet Pharm & Therapeutics

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Mycophenolic acid (MPA) has been shown to be promising for the treatment of autoimmune diseases in dogs and cats. In humans, MPA is highly bound to plasma proteins (~97%). It has been recommended to monitor free drug plasma concentrations because the free MPA correlates with its immunosuppressive effect. However, it is unknown if MPA is highly bound to plasma proteins in dogs and cats. The objectives of this study were to determine the extent of plasma protein binding of MPA and evaluate the effect of prednisolone and dexamethasone on the extent of protein binding of MPA in dogs and cats. The extent of plasma protein binding of MPA was determined in plasma collected from clinically healthy adult cats (n = 13) and dogs (n = 14) by combining high-throughput dialysis and ultra-high-liquid chromatography. This study reveals that MPA is highly bound to plasma proteins (>90%) in dogs and cats, mean extent of binding of MPA at 15 μg/ml to plasma proteins being 96% (range, 95%-97%) and 92% (range, 90%-93%) for dogs and cats, respectively. In dog plasma, MPA is primarily bound to albumin. In vitro, prednisolone increased the unbound MPA in dogs (p < .01) but not in cats (p = .07) while dexamethasone had no effect on MPA plasma binding in either species (p > .05). Results of this study provide valuable information for designing future pharmacokinetic and pharmacodynamic studies and also therapeutic monitoring programs for dogs and cats.

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Section: Discussionmentioning

confidence: 62%

Ex vivo binding of the immunosuppressant mycophenolic acid to dog and cat plasma proteins and the effect of co‐incubated dexamethasone and prednisolone

Morassi

Vélez

Slovak

et al. 2018

Vet Pharm & Therapeutics

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“…Plasma protein binding is an important parameter in understanding the pharmacokinetics of a drug; for example changes in clearance, volume of distribution and elimination half-life have been related to interspecies variations in the concentration of unbound drug (Rocci et al., 1980;Alvinerie et al, 1988).…”

Section: Ohmentioning

confidence: 99%

Plasma protein binding of nitroxynil in several species

Alvinerie¹,

Floc'h

Galtier³

1991

Vet Pharm & Therapeutics

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The binding of nitroxynil to total plasma proteins of cows, sheep and rabbits was characterized using equilibrium dialysis. The data indicate clearly that nitroxynil was highly (97-98%) bound to plasma protein of each animal. This linear binding would be due to the particular power exerted by serum albumin. The results are in good agreement with known pharmacokinetic properties of nitroxynil in domestic species.

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“…Synthetic corticosteroids are largely bound to albumin, but prednisolone is also capable of binding with CBG (Alvinerie et al . ) and as a consequence cannot be used to conduct adrenal suppression tests in horses, as plasma cortisol concentrations decrease following i.v. administration of prednisolone due to the displacement of cortisol from CBG rather than as a consequence of adrenal suppression alone.…”

Section: Metabolism and Mechanism Of Actionmentioning

confidence: 99%

“…Free cortisol is the active moiety according to the free-hormone hypothesis (Ferguson et al 2009); however, it is also possible that CBG is able to interact with cell membranes and facilitate entry of cortisol into cells (Gayrard et al 1996). Synthetic corticosteroids are largely bound to albumin, but prednisolone is also capable of binding with CBG (Alvinerie et al 1988) and as a consequence cannot be used to conduct adrenal suppression tests in horses, as plasma cortisol concentrations decrease following i.v. administration of prednisolone due to the displacement of cortisol from CBG rather than as a consequence of adrenal suppression alone.…”

Section: Metabolismmentioning

confidence: 99%

Review of glucocorticoid therapy in horses. Part 1: Pharmacology

Cuming

Groover

Wooldridge

et al. 2016

Equine Veterinary Education

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Summary This article is the first in a three part review series examining glucocorticoid use in treatment of medical conditions and musculoskeletal disorders of the horse. This article provides a review of the structure and function of corticosteroids together with a summary of the available literature pertaining to the pharmacodynamics, pharmacokinetics and indications for use of, and adverse effects associated with, glucocorticoids currently available for use by equine veterinarians.

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Prednisolone Binding to Plasma Proteins in Domestic Species

Cited by 14 publications

References 9 publications

Ex vivo binding of the immunosuppressant mycophenolic acid to dog and cat plasma proteins and the effect of co‐incubated dexamethasone and prednisolone

Ex vivo binding of the immunosuppressant mycophenolic acid to dog and cat plasma proteins and the effect of co‐incubated dexamethasone and prednisolone

Plasma protein binding of nitroxynil in several species

Review of glucocorticoid therapy in horses. Part 1: Pharmacology

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