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Fluorescent characteristics and pharmacokinetic profiles of the fluorescent probe BCECF in various tissues: the role of blood content

Fluorescent characteristics and pharmacokinetic profiles of the fluorescent probe BCECF in various tissues: the role of blood content. Devoisselle, J. M.; Soulie, S.; Mordon, S.; Maillols, H. (Lab. Technique Pharmaceutique Ind., U.F.R. Sci. Pharmaceutiques, Montpellier, Fr.). Photochemistry and Photobiology, 64(6), 906-910 (English) 1996 American Society for Photobiology.There are some reagents like 85138-49-4 is used in this study. CODEN: PHCBAP. ISSN: 0031-8655. DOCUMENT TYPE: Journal CA Section: 9 (Biochemical Methods) The purpose of this study was to investigate the in vitro and in vivo spectral characteristics of the fluorescent pH-sensitive probe bis-carboxyethylcarboxyfluorescein (BCECF) in different tissues and its fluorescence kinetics profiles. The in vivo study was performed on anesthetized adult Wistar rats. After i.v. administration (4.8 mg/kg), fluorescence spectra were recorded on the following tissues: skin, an isolated blood vessel and liver. Measurements performed in vitro on blood samples show modifications of the BCECF emission spectrum with a blue-shift (10 nm) and a low fluorescence emission. Blood content greatly influences the pH measurement by increasing the I (490 exc., 530 em.)/I(470exc., 530 em.) fluorescence ratio value (ratio of the fluorescence intensities at 530 nm following excitation at 470 nm and 490 nm) when the hematocrit is high. A 0.35 ratio difference is obsd. between a BCECF-buffered soln. and blood samples of 44% hematocrit. The emission spectra recorded on the skin are quite similar to the emission spectrum of BCECF in aq. soln. and are consistent with an extravascular localization of the dye a few minutes after injection. On the contrary, spectra recorded on the blood vessel and the liver are more similar than those recorded in vitro on high hematocrit solns. Kinetic profiles in skin, liver and isolated blood vessels compared to the clearance obtained by blood sampling provide information about tissue perfusion. Then the variation of in vivo spectra in different tissues may be taken into account to measure tissue pH with special regard to the blood content of the illuminated area and the time range in which the measurement is performed. .

The role of multidrug resistance protein 1 (MRP1) in transport of fluorescent anions across the human erythrocyte membrane

The role of multidrug resistance protein 1 (MRP1) in transport of fluorescent anions across the human erythrocyte membrane. Rychlik, B.; Balcerczyk, A.; Klimczak, A.; Bartosz, G. (Department of Molecular Biophysics, University of Lodz, Lodz 90-237, Pol.). Journal of Membrane Biology, 193(2), 79-90 (English) 2003 Springer-Verlag New York Inc. CODEN: JMBBBO.Several reagents with their cas registry numbers 85138-49-4 and 2321-07-5 are used here. ISSN: 0022-2631. DOCUMENT TYPE: Journal CA Section: 13 (Mammalian Biochemistry) Section cross-reference(s): 6, 9 We employed human red blood cells as a model system to check the affinity of MRP1 (Multidrug Resistance-assocd. Protein 1) towards fluorescein and a set of its carboxyl derivs.: 5/6-carboxyfluorescein (CF), 2',7'-bis-(2-carboxyethyl)-5/6-carboxyfluorescein (BCECF) and calcein (CAL). We found significant differences in the characteristics of transport of the dyes tested across the erythrocyte membrane. Fluorescein is transported mainly in a passive way, while active efflux systems at least partially contribute to the transport of the other compds. Inside-out vesicle studies revealed that active transport of calcein is masked by another, ATP-independent, transport activity. Inhibitor profiles of CF and BCECF transport are typical for substrates of org. anion transporters. BCECF is transported mainly via MRP1, as proven by the use of QCRL3, a monoclonal antibody known to specifically inhibit MRP1-mediated transport. Lack of effect of QCRL3 on CF uptake excludes the possibility of MRP1 being a transporter of this dye. No inhibition of CF accumulation by cGMP, thioguanine and 6-mercaptopurine suggests also that this fluorescent marker is not a substrate for MRP5, another ABC transporter identified in the human erythrocyte membrane. .