Decrease of in vitro serum protein binding of salicylate in rheumatoid arthritis

Netter, Patrick; Monot, C.; Stalars, M. C.; Mur, J. M.; Royer, R; Fauré, G; Pourel, J; Martin, Jean‐Charles; Gaucher, A

doi:10.1007/bf03189613

Cited by 8 publications

(1 citation statement)

References 20 publications

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“…The results should be considered in parallel to the 121 well-known variation of the protein binding with the protein concentration. Thus, the protein binding is less in diseases associated with hypoalbuminaemia, such as rheumatoid arthritis (Netter et al 1984). In the same manner, the lower binding in synovial fluid compared with that in plasma was related to the difference in protein concentrations in these 2 liquids (Wanwimolruk et al 1983).…”

Section: Discussionmentioning

confidence: 97%

Protein Binding and Stereoselectivity of Nonsteroidal Anti-Inflammatory Drugs

Lapicque¹,

Muller²,

Payan³

et al. 1993

Clinical Pharmacokinetics

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Stereoselective binding of nonsteroidal anti-inflammatory drugs (NSAIDs) can be studied using various techniques. Thus the results obtained by different investigators may be poorly consistent and even contradictory. NSAIDs are bound stereoselectively to serum albumin to different degrees depending on the drug investigated (ibuprofen, indoprofen, carprofen, etodolac, ketoprofen and flurbiprofen). For other drugs, both enantiomers are bound to a similar extent (pirprofen, fenoprofen). This stereoselectivity could vary with experimental conditions, in particular with protein concentration (ketoprofen, etodolac), leading to individual differences. Finally, the stereoselectivity of protein binding and of pharmacokinetics can be compared: differences in binding between enantiomers can explain their differences in pharmacokinetics, once metabolic properties such as inversion have been taken into account.

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Section: Discussionmentioning

confidence: 97%

Protein Binding and Stereoselectivity of Nonsteroidal Anti-Inflammatory Drugs

Lapicque¹,

Muller²,

Payan³

et al. 1993

Clinical Pharmacokinetics

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Stereoselective binding of etodolac to human serum albumin

et al. 1992

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The protein binding of etodolac enantiomers was studied in vitro by equilibrium dialysis in human serum albumin (HSA) of various concentrations varying from 1 to 40 g/liter, by addition of each enantiomer at increasing concentrations. In the 1 g/liter solution, at the lowest drug levels, the (R)-form is more bound than its antipode, the contrary being observed at the highest drug levels. For higher albumin concentrations, S was bound in a larger extent than R. Using the displacement of specific markers of HSA sites I and II, studied by spectrofluorimetry, it was suggested that R and S are both bound to site I, while only S is strongly bound to site II.

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Stereoselective protein binding of ketoprofen: Effect of albumin concentration and of the biological system

Dubois

Lapicque

Abiteboul³

et al. 1993

Chirality

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Equilibrium dialysis was used to study in vitro the enantioselective binding of R, S, and racemic ketoprofen at physiological pH and temperature in human serum albumin (HSA) (1, 20, and 40 g/liter) and in plasma. The binding of enantiomers in a racemic mixture was studied to see the effect of each isomer on the other's interaction with the protein. The free fractions were determined by high-performance liquid chromatography. The binding of ketoprofen enantiomers to albumin was enantioselective, depending on both drug and protein concentrations. Enantioselectivity was observed in plasma too but was the opposite of that in HSA at 40 g/liter. The percentage of each isomer unbound was higher in the racemic mixture than with the isomer alone. The displacement of probes specific for HSA sites I and II, studied by spectrofluorimetry, suggests that all three preparations of ketoprofen are bound mainly to site I and secondarily to site II.

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Decrease of in vitro serum protein binding of salicylate in rheumatoid arthritis

Cited by 8 publications

References 20 publications

Protein Binding and Stereoselectivity of Nonsteroidal Anti-Inflammatory Drugs

Protein Binding and Stereoselectivity of Nonsteroidal Anti-Inflammatory Drugs

Stereoselective binding of etodolac to human serum albumin

Stereoselective protein binding of ketoprofen: Effect of albumin concentration and of the biological system

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