Publication

The sinusoidal efflux of dibromosulfophthalein from rat liver is stimulated by albumin, ligandin and fatty acid binding protein but not by other dibromosulfophthalein binding proteins

Nijssen, HMJ., Pijning, T., Proost, JH., Meijer, DKF. & Groothuis, GMM., Jul-1994, In : Journal of Hepatology. 21, 1, p. 29-36 8 p.

Research output: Contribution to journalArticleAcademicpeer-review

APA

Nijssen, HMJ., Pijning, T., Proost, JH., Meijer, DKF., & Groothuis, GMM. (1994). The sinusoidal efflux of dibromosulfophthalein from rat liver is stimulated by albumin, ligandin and fatty acid binding protein but not by other dibromosulfophthalein binding proteins. Journal of Hepatology, 21(1), 29-36. https://doi.org/10.1016/S0168-8278(94)80133-9

Author

Nijssen, HMJ ; Pijning, T ; Proost, JH ; Meijer, DKF ; Groothuis, GMM. / The sinusoidal efflux of dibromosulfophthalein from rat liver is stimulated by albumin, ligandin and fatty acid binding protein but not by other dibromosulfophthalein binding proteins. In: Journal of Hepatology. 1994 ; Vol. 21, No. 1. pp. 29-36.

Harvard

Nijssen, HMJ, Pijning, T, Proost, JH, Meijer, DKF & Groothuis, GMM 1994, 'The sinusoidal efflux of dibromosulfophthalein from rat liver is stimulated by albumin, ligandin and fatty acid binding protein but not by other dibromosulfophthalein binding proteins', Journal of Hepatology, vol. 21, no. 1, pp. 29-36. https://doi.org/10.1016/S0168-8278(94)80133-9

Standard

The sinusoidal efflux of dibromosulfophthalein from rat liver is stimulated by albumin, ligandin and fatty acid binding protein but not by other dibromosulfophthalein binding proteins. / Nijssen, HMJ; Pijning, T; Proost, JH; Meijer, DKF; Groothuis, GMM.

In: Journal of Hepatology, Vol. 21, No. 1, 07.1994, p. 29-36.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Nijssen HMJ, Pijning T, Proost JH, Meijer DKF, Groothuis GMM. The sinusoidal efflux of dibromosulfophthalein from rat liver is stimulated by albumin, ligandin and fatty acid binding protein but not by other dibromosulfophthalein binding proteins. Journal of Hepatology. 1994 Jul;21(1):29-36. https://doi.org/10.1016/S0168-8278(94)80133-9


BibTeX

@article{0ea52e7bac2b457f80de8f51b1127f19,
title = "The sinusoidal efflux of dibromosulfophthalein from rat liver is stimulated by albumin, ligandin and fatty acid binding protein but not by other dibromosulfophthalein binding proteins",
abstract = "Organic anions can be excreted from the liver into the bile or back into the general circulation (sinusoidal efflux). It has previously been shown that the net sinusoidal efflux rate of dibromosulfophthalein from the perfused liver into the perfusate is the result of actual efflux from and reuptake into the liver, and can be strongly influenced by the presence of bovine serum albumin in the perfusion medium. The present study investigated whether the influence of albumin on the net sinusoidal efflux process is albumin-specific or whether other binding proteins could have a similar effect on the sinusoidal efflux. Using a single-pass liver perfusion technique and short-lasting (pulse) protein infusions, the stimulatory effect of a wide range of dibromosulfophthalein binding proteins on the sinusoidal efflux process were determined. These experiments showed that all the serum albumins tested as well as the liver cytosolic binding proteins fatty acid binding protein and ligandin (glutathione S-transferase) stimulated this process. The other proteins tested, bovine beta lactoglobulin-b, human gamma globulin and chicken egg lysozyme showed no stimulatory effect, despite relatively high equilibrium binding of dibromosulfophthalein. No clear-cut relationship was found between the equilibrium unbound ligand concentration as measured in perfusate and the stimulatory effect, suggesting absence of equilibrium binding in the sinusoids. Equilibrium binding of dibromosulfophthalein to chicken serum albumin and ligandin as well as the dissociation rate constants were determined in vitro with rapid filtration techniques. Pharmacokinetic modeling using a series compartment model showed that the stimulatory effect of these proteins could only be simulated accurately with higher values for both the association and dissociation rate constants compared with those determined in vitro, as was previously also found for bovine serum albumin. This may imply altered binding characteristics of the proteins during passage through the liver and/or a direct effect on the carrier-mediated efflux process. (C) Journal of Hepatology.",
keywords = "DIBROMOSULFOPHTHALEIN, PROTEIN STIMULATION, REUPTAKE, SINUSOIDAL SECRETION, HEPATIC-UPTAKE, ROSE-BENGAL, MEDIATED TRANSPORT, SERUM-ALBUMIN, CONFORMATIONAL CHANGE, BOUND SUBSTANCES, CELL-SURFACE, DISSOCIATION, RECEPTOR, BILIRUBIN",
author = "HMJ Nijssen and T Pijning and JH Proost and DKF Meijer and GMM Groothuis",
year = "1994",
month = jul,
doi = "10.1016/S0168-8278(94)80133-9",
language = "English",
volume = "21",
pages = "29--36",
journal = "Journal of Hepatology",
issn = "0168-8278",
publisher = "ELSEVIER SCIENCE BV",
number = "1",

}

RIS

TY - JOUR

T1 - The sinusoidal efflux of dibromosulfophthalein from rat liver is stimulated by albumin, ligandin and fatty acid binding protein but not by other dibromosulfophthalein binding proteins

AU - Nijssen, HMJ

AU - Pijning, T

AU - Proost, JH

AU - Meijer, DKF

AU - Groothuis, GMM

PY - 1994/7

Y1 - 1994/7

N2 - Organic anions can be excreted from the liver into the bile or back into the general circulation (sinusoidal efflux). It has previously been shown that the net sinusoidal efflux rate of dibromosulfophthalein from the perfused liver into the perfusate is the result of actual efflux from and reuptake into the liver, and can be strongly influenced by the presence of bovine serum albumin in the perfusion medium. The present study investigated whether the influence of albumin on the net sinusoidal efflux process is albumin-specific or whether other binding proteins could have a similar effect on the sinusoidal efflux. Using a single-pass liver perfusion technique and short-lasting (pulse) protein infusions, the stimulatory effect of a wide range of dibromosulfophthalein binding proteins on the sinusoidal efflux process were determined. These experiments showed that all the serum albumins tested as well as the liver cytosolic binding proteins fatty acid binding protein and ligandin (glutathione S-transferase) stimulated this process. The other proteins tested, bovine beta lactoglobulin-b, human gamma globulin and chicken egg lysozyme showed no stimulatory effect, despite relatively high equilibrium binding of dibromosulfophthalein. No clear-cut relationship was found between the equilibrium unbound ligand concentration as measured in perfusate and the stimulatory effect, suggesting absence of equilibrium binding in the sinusoids. Equilibrium binding of dibromosulfophthalein to chicken serum albumin and ligandin as well as the dissociation rate constants were determined in vitro with rapid filtration techniques. Pharmacokinetic modeling using a series compartment model showed that the stimulatory effect of these proteins could only be simulated accurately with higher values for both the association and dissociation rate constants compared with those determined in vitro, as was previously also found for bovine serum albumin. This may imply altered binding characteristics of the proteins during passage through the liver and/or a direct effect on the carrier-mediated efflux process. (C) Journal of Hepatology.

AB - Organic anions can be excreted from the liver into the bile or back into the general circulation (sinusoidal efflux). It has previously been shown that the net sinusoidal efflux rate of dibromosulfophthalein from the perfused liver into the perfusate is the result of actual efflux from and reuptake into the liver, and can be strongly influenced by the presence of bovine serum albumin in the perfusion medium. The present study investigated whether the influence of albumin on the net sinusoidal efflux process is albumin-specific or whether other binding proteins could have a similar effect on the sinusoidal efflux. Using a single-pass liver perfusion technique and short-lasting (pulse) protein infusions, the stimulatory effect of a wide range of dibromosulfophthalein binding proteins on the sinusoidal efflux process were determined. These experiments showed that all the serum albumins tested as well as the liver cytosolic binding proteins fatty acid binding protein and ligandin (glutathione S-transferase) stimulated this process. The other proteins tested, bovine beta lactoglobulin-b, human gamma globulin and chicken egg lysozyme showed no stimulatory effect, despite relatively high equilibrium binding of dibromosulfophthalein. No clear-cut relationship was found between the equilibrium unbound ligand concentration as measured in perfusate and the stimulatory effect, suggesting absence of equilibrium binding in the sinusoids. Equilibrium binding of dibromosulfophthalein to chicken serum albumin and ligandin as well as the dissociation rate constants were determined in vitro with rapid filtration techniques. Pharmacokinetic modeling using a series compartment model showed that the stimulatory effect of these proteins could only be simulated accurately with higher values for both the association and dissociation rate constants compared with those determined in vitro, as was previously also found for bovine serum albumin. This may imply altered binding characteristics of the proteins during passage through the liver and/or a direct effect on the carrier-mediated efflux process. (C) Journal of Hepatology.

KW - DIBROMOSULFOPHTHALEIN

KW - PROTEIN STIMULATION

KW - REUPTAKE

KW - SINUSOIDAL SECRETION

KW - HEPATIC-UPTAKE

KW - ROSE-BENGAL

KW - MEDIATED TRANSPORT

KW - SERUM-ALBUMIN

KW - CONFORMATIONAL CHANGE

KW - BOUND SUBSTANCES

KW - CELL-SURFACE

KW - DISSOCIATION

KW - RECEPTOR

KW - BILIRUBIN

U2 - 10.1016/S0168-8278(94)80133-9

DO - 10.1016/S0168-8278(94)80133-9

M3 - Article

C2 - 7525696

VL - 21

SP - 29

EP - 36

JO - Journal of Hepatology

JF - Journal of Hepatology

SN - 0168-8278

IS - 1

ER -

ID: 6391245