Search PubMed⌕ Search

Biomedical subjects

Z Zuo

Publications and source records attributed to Z Zuo.

36 records · Page 2Linked to original sources
PubMed1997

Population-based study of glutathione S-transferase mu gene deletion in adult glioma cases and controls.

Gene deletion at the glutathione S-transferase mu locus (GSTM1) has previously been associated with increased risk for environmentally-induced cancers (e.g. smoking-related lung cancer). In the present study we examined the hypothesis that GSTM1 deletion is a risk factor for malignant brain tumors in adults. We compared the prevalence of the GSTM1 homozygous deletion polymorphism in 158 Caucasian adults with gliomas with 157 controls. Cases and controls were drawn from a large population-based case-control study of brain cancers in six San Francisco Bay area counties. Overall, the prevalence of the GSTM1 deletion was similar in cases (83/158; 53%) and controls (78/157; 50%). Among brain tumor cases, analysis of variance modeling indicated a significant interaction of GSTM1 genotype and gender associated with age at diagnosis (P = 0.02). This effect was due to the fact that women with GSTM1 deletion were younger on average at diagnosis than women who were GSTM1 positive (43.9 years versus 52.4 years, respectively). Age at diagnosis among men was similar for those who were GSTM1 deleted and GSTM1 positive (49.4 years and 47.2 years, respectively). The younger age at diagnosis of GSTM1 null female cases compared with GSTM1 positive cases was observed in astrocytoma as well as the higher grade tumors (e.g. glioblastoma multiforme). There was no association of GSTM1 deletion with age or gender in controls. These studies suggest that among female cases, GSTM1 deletion may be associated with earlier age at onset. Confirmation of these findings could provide important clues to gene-environment interactions in the etiology of malignant brain tumors.

Adult↗
PubMed1997

Inhalational anesthetics up-regulate constitutive and lipopolysaccharide-induced inducible nitric oxide synthase expression and activity.

Nitric oxide (NO) is an important biological messenger involved in the regulation of blood vessel tone, neurotransmission, inflammatory responses, and host defenses. Inhalational anesthetics have been shown to inhibit the function of the NO signaling pathway in a variety of tissues. In addition, acute inhibition of the NO signaling pathway significantly reduced the required alveolar concentration of halothane or isoflurane for anesthesia, which suggests a role for the NO signaling pathway in mechanisms of anesthesia and consciousness. We now report that inhalational anesthetics affect gene expression of nitric oxide synthases (NOS) (EC 1.14.13.39), the enzymes that synthesize NO from L-arginine. Both halothane and isoflurane, at clinically relevant concentrations, significantly up-regulate the mRNA, protein, and activity level of NOS in lipopolysaccharide-treated macrophages (inducible NOS; type II NOS), and bovine pulmonary endothelial cells (endothelial constitutive NOS; type III NOS). This is a novel interaction between inhalational anesthetics and the NO signaling pathway and has wide-ranging implications for both clinical medicine and experimental biology.

Anesthetics, Inhalation↗
PubMed1997

[Spinal segment distribution of neural innervation related houhai acupoint--studied by CB-HRP tracing method focused on observation of the dendrites of spinal motor neurons].

The spinal segment distribution of neural innervation related Houhai acupoint in rats has been investigted by using horseradish peroxidase conjugated cholera toxin B subunit (CB-HRP) tracing technique. Spinal motoneurons (Mn) in L6-S1 were labeled retrogradely by CB-HRP, and their features have been characterized: 1) their marginal plexus of the dendrites radially projected to the lateral and/or anterior funiculus and their distal portions forming subpial dendritic plexus; 2) the medial dendrites ran along the ventral margin of the gray commissure and their distal portions surrounded the central canal' forming a subependymal dendritic plexus. Both of them are Golgi-phobic. Some distal branches of dendrites penetrated to the contralateral gray matter. The dendritic arbors of the labeled motoneurons in the group of electro-acupuncture or group of acupoint-inoculation with sheep red blood cells contracted in comparison with that in the normal control group. The primary sensory transganglionic labeled fibers and preterminal fibers revealed by CB-HRP in the dorsal horn and dorsal commissural nucleus of the spinal cord (L5-S2) converged and overlaped with the dendrites of retrogradely labeled motoneurons. The results indicated there is a reflect circuit of afferent-integration-efferent neuro-network in the spinal cord related Houhai acupoint. The Mns retrogradely labeled by CB-HRP in the L6-S1 segments might be involved in Houhai acupuncture.

Acupuncture Points↗
PubMed1996

Halothane and isoflurane dose-dependently inhibit the cyclic GMP increase caused by N-methyl-D-aspartate in rat cerebellum: novel localization and quantitation by in vitro autoradiography.

Using a novel technique combining immunohistochemistry and in vitro quantitative autoradiography, we were able simultaneously to localize and quantitate cyclic guanosine 3',5'-monophosphate (cGMP)-immunoreactive binding in adult rat cerebellum. The cGMP-immunoreactive binding was predominantly detected in the molecular layer of the cerebellum under both basal and N-methyl-D-aspartate-stimulated conditions. N-Methyl-D-aspartate significantly increased the cGMP binding density in the molecular layer. This increased cGMP level was dose-dependently and significantly inhibited by the inhalational anesthetics halothane and isoflurane. This increased cGMP level was also significantly inhibited by L-NG-nitroarginine methyl ester, an inhibitor of nitric oxide synthases. L-Arginine, the substrate of nitric oxide synthase, reversed the inhibition by L-NG-nitroarginine methyl ester on the cGMP increase. This novel combination of immunohistochemistry and quantitative autoradiography may be used to localize and quantitate simultaneously cGMP or other substances in animal tissues. Our data also confirm that nitric oxide is involved in the stimulation of cGMP formation by N-methyl-D-aspartate. Halothane and isoflurane inhibit the nitric oxide-guanylyl cyclase signaling pathway activated by the excitatory amino acid N-methyl-D-aspartate in the brain, which may be a component of the mechanisms by which these two inhalational anesthetics produce their anesthetic effects.

Anesthetics, General↗
PubMed1996

Halothane and isoflurane inhibit vasodilation due to constitutive but not inducible nitric oxide synthase. Implications for the site of anesthetic inhibition of the nitric oxide/guanylyl cyclase signaling pathway.

BACKGROUND: Inhalational anesthetics inhibit the nitric oxide-guanylyl cyclase signaling pathway, but the site of this inhibition is not yet clear. This study was designed to test the hypothesis that receptor activation or downstream signaling events leading to nitric oxide synthase activation are important sites for this inhibition by comparing the effect of anesthetics on vasodilation caused by the calcium-dependent constitutive endothelial nitric oxide synthase versus the calcium-independent inducible nitric oxide synthase. METHODS: Endothelium-intact or -denuded rat thoracic aorta rings preincubated with or without lipopolysaccharide were mounted for isometric tension measurement, constricted with phenylephrine, then relaxed with methacholine in the presence or absence of halothane (1-3%) or isoflurane (1-3%). The cyclic guanosine 3,5-monophosphate content in the endothelium-denuded rings preincubated with or without lipopolysaccharide in the presence or absence of 3% halothane or 3% isoflurane was quantified by radioimmunoassay. The activity of partially purified inducible nitric oxide synthase from activated mouse macrophage was assayed in the presence or absence of halothane (1-4%) or isoflurane (1-5%) by the conversion of 3H-L-arginine to 3H-L-citrulline. RESULTS: Halothane and isoflurane inhibited methacholine-stimulated, nitric oxide-mediated vasorelaxation in endothelium-intact aortic rings. Neither halothane nor isoflurane affected the vasorelaxation caused by basal endothelial nitric oxide synthase or inducible nitric oxide synthase activity. Neither anesthetic altered the cyclic guanosine 3,5-monophosphate increase caused by inducible nitric oxide synthase in the lipopolysaccharide-treated rings. CONCLUSIONS: The results demonstrated that halothane and isoflurane inhibit only receptor/calcium-activated nitric oxide synthase action and that direct inhibition of nitric oxide synthase, soluble guanylyl cyclase, or an interaction with nitric oxide are not responsible for anesthetic inhibition of endothelium-dependent vasorelaxation.

Anesthetics, Inhalation↗
PubMed1996

Decreased gonadotropin-releasing hormone neurosecretory response to glutamate agonists in middle-aged female rats on proestrus afternoon: a possible role in reproductive aging?

Before becoming acyclic, middle-aged rats display an attenuated LH surge and a decreased number of activated GnRH neurons. The present study examined whether the decreased activation of GnRH neurons in middle-aged rats could be due to defective glutamate neurosignaling in the hypothalamus. Arcuate nucleus/median eminence (ARC/ME) fragments were isolated from young (2-month-old) and middle-aged (9- to 11-month-old) rats at 1700 h on proestrus and incubated in vitro with or without the specific glutamate agonists, D,L-alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (1 mM), kainate (1 mM), and N-methyl-D-aspartate (NMDA; 50 mM). The results showed that basal GnRH release was similar in the two age groups. In contrast, stimulated GnRH release by D,L-alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid, kainate, and NMDA was significantly attenuated in middle-aged vs. young rats. KCl stimulation at the end of the experiments confirmed the viability of all ARC/ME fragments. Quantitative reverse transcriptase-PCR revealed that messenger RNA levels for the major NMDA receptor subunit (NMDAR1) were significantly lower in the preoptic area and ARC/ME of the middle-aged rat on proestrus afternoon. As a whole, these findings suggest that a defect in hypothalamic glutamate neurosignaling may be an important mechanism leading to age-related defects in LH secretion and acyclicity in female animals.

Aging↗
PubMed1995

Halothane, enflurane, and isoflurane do not affect the basal or agonist-stimulated activity of partially isolated soluble and particulate guanylyl cyclases of rat brain.

BACKGROUND: Evidence suggests that inhalational anesthetics interact with the nitric oxide-guanylyl cyclase signaling pathway in the central nervous system and that the inhibitation of this pathway in brain may result in an anesthetic, analgesic, or sedative effect. The mechanism of the effects inhalational anesthetics on this signaling pathway is not clear. This study attempted to determine whether inhalational anesthetics directly affect soluble or particulate guanylyl cyclase activity in a partially isolated enzyme system. METHODS: The effects of halothane (0.44-4.4%), enflurane (1.34-6.7%), and isoflurane (0.6-5.0%) on basal or stimulated soluble or particulate guanylyl cyclase activity were examined. Soluble guanylyl cyclase was isolated from whole rat brain and was stimulated by sodium nitroprusside or nitric oxide. Particulate guanylyl cyclase was isolated from rat olfactory bulb and was stimulated by rat atrial natriuretic peptide(1-28). Cyclic guanosine monophosphate content was measured by radiommunoassay. The concentrations of anesthetics in the incubation solution were confirmed by gas chromatography methods. RESULTS: None of the three anesthetics affected the activity of basal or stimulated soluble or particulate guanylyl cyclase at the concentrations examined in the current experimental conditions. CONCLUSIONS: These results suggest that halothane, enflurane, and isoflurane do not directly interact with soluble or particulate guanylyl cyclases of rat brain.

Animals↗
PubMed1995

Natriuretic peptide receptors in the fetal rat.

In vitro autoradiography of rat fetuses from embryonic days 12-19 (E12-E19) showed widespread high-affinity specific binding sites for natriuretic peptides. The sites on E16 somites avidly bound C-type natriuretic peptide [CNP-(1-22)] as well as C-ANP, a synthetic ligand that selects the C-type natriuretic peptide receptor (NPR-C). Most somitic binding sites had high affinity for atrial natriuretic peptide [ANP-(1-28)], confirming their resemblance to NPR-C. A few had a lower apparent affinity for ANP-(1-28), suggesting that they might be NPR-B. CNP-(1-22) was more powerful than ANP-(1-28) as an agonist of guanosine 3',5'-cyclic monophosphate production in somites, and ATP augmented the action of CNP-(1-22). These observations further suggest the presence of NPR-B. However, with cross-linking of 3-[125I]iodo-0-tyrosyl rat CNP-(1-22) to somitic membranes followed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, only a single 64-kDa binding protein was detected under reducing conditions. This is not consistent with intact approximately 120-kDa NPR-B. In vitro autoradiography of the binding of natriuretic peptides to E16 liver implied the presence of NPR-A and NPR-C-like receptors. Hepatic guanosine 3',5'-cyclic monophosphate production was most powerfully stimulated by ANP-(1-28), as expected for NPR-A. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis also identified NPR-A and NPR-C-like proteins in E16 hepatic membranes. Thus different NPRs are expressed by specific fetal tissues. This may be developmentally significant.

Animals↗
PubMed1995

Natriuretic peptide receptors are expressed during cerebral growth in the fetal rat.

Autoradiography of frozen sections of fetal rat brain shows that receptor-like binding sites for atrial and C-type natriuretic peptides (ANP and CNP) occur in the generative juxtaventricular zone of the telencephalon after the 12th embryonic day (E12). These sites avidly bind both ANP and CNP. They thus resemble the cloned NPR-C type of natriuretic peptide receptor. Covalent cross-linking of 3-[125I]iodo-O-tyrosyl CNP-(1-22) and 3-[125I]iodo-28-tyrosyl rat ANP-(1-28) to membrane proteins from E16 telencephala labels a single protein band on reducing sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis. The protein has high affinities for ANP and CNP and a molecular mass of 60-70 kDa under reducing conditions, consistent with reduced NPR-C. However, because the telencephalic protein has unusual physicochemical properties in SDS under nonreducing conditions it was not possible to assess whether this protein can form disulfide-bridged dimers like NPR-C. CNP-(1-22) was a full agonist and ANP-(1-28) was a partial agonist of guanosine 3',5'-cyclic monophosphate (cGMP) production by E16 telencephalon. C-ANP, a synthetic ligand of NPR-C, antagonized CNP-(1-22)-mediated cGMP production. The results imply that either the NPR-C-like telencephalic receptor modulates the level of cGMP or a guanylate cyclase-coupled receptor, such as the 120-kDa B-type NPR, for which CNP-(1-22) is a full agonist, is present at levels insufficient to be detected by autoradiography or protein labeling.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1995

Kinetics and products of OH radical addition to baicalin.

The reaction of OH radicals with baicalin was studied by pulse and gamma radiolysis in N2O-saturated aqueous solutions. The addition of an OH radical to baicalin produced an intermediate species that shows a maximum UV absorbance band at 420 nm and decays with a unimolecular rate constant of 1.25 x 10(4) s-1 and a bimolecular rate constant of 6.1 x 10(8) mol-1 dm3 s-1. Four major final products were obtained by gamma irradiation, and their structures were identified. Two of them (P1 and P2) are suggested to originate from the unimolecular reaction and the other two (P3 and P4) from the bimolecular reaction of the radicals.

Flavonoids↗
PubMed1994

Receptor proteins and biological effects of C-type natriuretic peptides in the renal glomerulus of the rat.

Binding studies on rat glomeruli using 125I-labeled Tyr0-C-type natriuretic peptide-(1-22) [125I-Tyr0-CNP-(1-22)] and 125I-labeled alpha-atrial natriuretic peptide (alpha-125I-ANP), and the unlabeled ligands CNP-(1-22), alpha-ANP, and des-Gln18,Ser19,Gly20,Leu21,Gly22-ANP-(4-2 3)-NH2 (C-ANP) suggest that receptor-like sites that bind both alpha-ANP and C-ANP fall into two categories, one with high [dissociation constant (Kd) approximately 10(-9)M] and one with low (Kd approximately 10(-5)M) affinity for CNP-(1-22). Covalent attachment of 125I-Tyr0-CNP-(1-22) and alpha-125I-ANP to these sites identifies two membrane proteins with corresponding properties. The first, which can be labeled by both radioligands, is a disulfide-bridged approximately 140-kDa protein that is reduced by dithiothreitol to approximately 67 kDa. This protein binds C-ANP and has Kd approximately 10(-10) M for CNP-(1-22). The second protein, which is labeled only by alpha-125I-ANP, also binds C-ANP, but has Kd approximately 10(-5)M for CNP-(1-22). This approximately 77-kDa protein may also have a disulfide-bridged, high-molecular-mass form of approximately 140 kDa in the absence of dithiothreitol. Studies of glomerular function show that alpha-125I-ANP is internalized whereas 125I-Tyr0-CNP-(1-22) is not. C-ANP abolishes the specific internalization of alpha-125I-ANP. CNP-(1-22) inhibits internalization of 400 pM alpha-125I-ANP weakly, only approximately 60% being inhibited by 10 microM CNP-(1-22). This implies that the approximately 77-kDa protein, with its low affinity for CNP-(1-22), mediates internalization. Furthermore, CNP-(1-22), as well as alpha-ANP and C-ANP, inhibits glomerular levels of adenosine 3',5'-cyclic monophosphate (cAMP), and CNP-(1-22) does so with a high affinity, which corresponds to its affinity for the approximately 67-kDa protein. The results suggest that the approximately 67-kDa receptor is distinct from the natriuretic peptide clearance receptor and may control cAMP levels.

Amino Acid Sequence↗
PubMed1994

[Ripening effect of mylis and tiluoan on the uterine cervix in pregnant rats].

Effect of Mylis and Tiluoan on cervical ripening and blood levels of estradiol and progesterone of pregnant rats were studied. Dehydroepiandrosterone (DHA) is the main component in both of the drugs. Pregnant rats groups were given the drugs on the 19th day of gestation at dosage of 10, 20 and 40 mg/kg respectively. The results indicated that both drugs at different dose were able to significantly decrease the cervical extensibility, to dilate the cervical OS, increase the cervical wet weight, and elevate the blood estradiol level, lower the progesterone concentration. It indicated that DHA enhances estradiol synthesis and suppresses progesterone secretion.

Animals↗
PubMed1993

C-type natriuretic peptide and atrial natriuretic peptide receptors of rat brain.

Natriuretic peptide receptors in rat brain were mapped by in vitro autoradiography using 125I-labeled [Tyr0]CNP-(1-22) to bind atrial natriuretic peptide receptor (ANPR)-B and ANPR-C receptors selectively, and 125I-labeled alpha-ANP to select ANPR-A and ANPR-C receptors. Des-[Gln18,Ser19,Gly20,Leu21,Gly22]ANP-(4- 23)-amide (C-ANP) was used for its selectivity for ANPR-C over ANPR-A. Specific binding of 125I-[Tyr0]CNP-(1-22) with a dissociation constant (Kd) approximately 1 nM occurred in olfactory bulb, cerebral cortex, lateral septal nucleus, choroid plexus, and arachnoid mater. This binding was abolished by C-type natriuretic peptide [CNP-(1-22)], alpha-ANP and C-ANP, and conformed to ANPR-C. 125I-alpha-ANP bound to all structures that bound 125I-[Tyr0]CNP-(1-22). This binding was also inhibited by both CNP-(1-22) and C-ANP, confirming the presence of ANPR-C-like binding sites. However, ANPR-C-like binding sites were heterogenous because only some had high affinities for 125I-[Tyr0]CNP-(1-22) and CNP-(1-22). 125I-alpha-ANP also bound sites without affinities for C-ANP or CNP-(1-22). These sites were consistent with ANPR-A. They occurred mainly on the olfactory bulb, the choroid plexus, and the subfornical organ. Guanosine 3',5'-cyclic monophosphate production was strongly stimulated by alpha-ANP but not by CNP-(1-22) in olfactory bulb. Neither ligand stimulated it in cortical tissue. Thus the natriuretic peptide binding sites of rat brain conformed to ANPR-A and to heterogenous ANPR-C-like sites. No ANPR-B were detected.

Animals↗
PubMed1992

Laser photolysis of cytosine, cytidine and dCMP in aqueous solution.

Laser photolysis of cytosine and cytosine derivatives (cytidine and 2'-deoxycytidine-5'-monophosphate) using acetone as a sensitizer have been carried out in aqueous solution using a KrF laser. The absorption spectra of triplet states of cytosine and cytosine derivatives have been observed for the first time. From detailed kinetic analyses, the reaction mechanisms including triplet-triplet excitation transfer, and intramolecular excitation transfer within the exciplex arising from the interaction of triplet acetone with cytosine and cytosine derivatives, have been suggested. Accordingly, a series of kinetic parameters have also been obtained.

Cytidine↗
PubMed1992

Renal receptors for atrial and C-type natriuretic peptides in the rat.

Receptors for alpha-atrial natriuretic peptide (alpha-ANP) and C-type natriuretic peptide [CNP-(1-22)] were quantified in kidneys from adult Wistar rats by in vitro autoradiography. 125I-labeled alpha-ANP (100 pM) bound reversibly to glomeruli, outer medullary vasa recta, and inner medulla with an apparent dissociation constant (Kd) of 3-6 nM. The presence of 10 microM des-[Gln18,Ser19,Gly20,Leu21,Gly22]ANP-(4- 23) (C-ANP), a specific ligand of the ANPR-C subtype of alpha-ANP receptor, inhibited approximately 50% of the glomerular binding of 125I-alpha-ANP, and this moiety of glomerular binding was also inhibited by CNP-(1-22) with an apparent inhibitory constant (Ki) of 10.47 +/- 7.59 nM. C-ANP and CNP-(1-22) showed little affinity for the medullary binding sites of alpha-ANP. 125I-[Tyr0]CNP-(1-22) (110 pM) bound solely to glomeruli and was competitively displaced by increasing concentrations of [Tyr0]CNP-(1-22) with an apparent Kd of 1.42 +/- 0.48 nM. Binding of increasing concentrations (25 pM to 1 nM) of 125I-[Tyr0]CNP-(1-22) in the presence or absence of 1 microM [Tyr0]CNP-(1-22) also demonstrated a high affinity (Kd of 0.41 +/- 0.07 nM) for the glomerular binding of 125I-[Tyr0]CNP-(1-22). Bound 125I-[Tyr0]CNP-(1-22) could be displaced by excess alpha-ANP and excess CNP-(1-22), both with high affinities. The glomerular binding of 125I-[Tyr0]CNP-(1-22) was also prevented by 10 microM C-ANP. Guanosine 3',5'-cyclic monophosphate produced by isolated glomeruli was measured by radioimmunoassay.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMedDate not supplied

Flutamide-hydroxypropy-beta-chiyclodextrin complex: formulation, physical characterization, and absorption studies using the Caco-2 in vitro model.

PURPOSE: The objective of this research was to formulate flutamide (FLT) in hydroxypropyl-beta-cyclodextrin (HPbetaCyD), and to investigate FLT transcellular permeation from the complex using the Caco-2 monolayer in vitro model. METHODS: Classical solubility data were used to derive thermodynamic parameters which, together with Differential Scanning Calorimetry (DSC), (1)H-NMR and (19)F-NMR, were used to characterize and derive stability constants for the FLT-HPbetaCyD complex. The Caco-2 cell line was used to examine the role of HPbetaCyD on the passage of FLT across cell monolayers in vitro. RESULTS: The solubility of FLT in water (1.46 mmol/L) increased almost 170 times (to 243.45 mmol/L) in the presence of 50% (w/v) HPbetaCyD. Solubility data for FLT in aqueous HPbetaCyD were used to derive thermodynamic parameters (DeltaG degrees at 298 K = -3.48, DeltaH degrees = 2.85, DeltaS degrees at 298 K = 21.24). The solubility of FLT in HPbetaCyD increased proportionally with an increase in temperature. The FLT-HPbetaCyD complex had an A(L)-type (DSC) isotherm, consistent with a linear increase in FLT solubility and unchanged stoichiometry. The DSC of free FLT and HPbetaCyD showed endothermic peaks at 110 degrees C and 300 degrees C, respectively. FLT-HPbetaCyD did not display a free-FLT endothermic response, but exhibited broadening of the endothermic peak in the HPbetaCyD region. (19)F- and (1)H-NMR chemical shifts of FLT moved upfield as a function of its increased solubility in the presence of HPbetaCyD. The FLT-HPbetaCyD stability constant, K(s) (1:1) was estimated to be 356 M(-1 )and 357 M(-1), from thermodynamic and (19)F NMR data, respectively. The apical-to-basal permeability coefficient (P(eff) = 4.75 x 10(-5) cm.s(-1)) for FLT across Caco-2 cell monolayers at 37; C increased as HPbetaCyD concentrations were reduced, indicative of transepithelial passage via passive diffusion of available free FLT in solution. Studies in the presence and absence of Ca(2+ )ruled out a significant paracellular transport component. CONCLUSIONS: FLT-HPbetaCyD is a relatively stable, 1:1 inclusion complex. Formation of this complex substantially increases the water solubility of FLT, but HPbetaCyD, except in high dilution, reduces transcellular passage of FLT in the Caco-2 cell in vitro model.

2-Hydroxypropyl-beta-cyclodextrin↗