The Experts below are selected from a list of 107133 Experts worldwide ranked by ideXlab platform
Takeshi Sugaya - One of the best experts on this subject based on the ideXlab platform.
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local production of Fatty acid binding Protein 4 in epicardial perivascular fat and macrophages is linked to coronary atherosclerosis
Arteriosclerosis Thrombosis and Vascular Biology, 2016Co-Authors: Masato Furuhashi, Tomohiro Mita, Takahiro Fuseya, Shutaro Ishimura, Yuki Watanabe, Kyoko Hoshina, Masaki Murata, Akina Omori, Megumi Matsumoto, Takeshi SugayaAbstract:Objective—Fatty acid–binding Protein 4 (FABP4) is expressed in adipocytes and macrophages, and elevated circulating FABP4 level is associated with obesity-mediated metabolic phenotype. We systematically investigated roles of FABP4 in the development of coronary artery atherosclerosis. Approach and Results—First, by immunohistochemical analyses, we found that FABP4 was expressed in macrophages within coronary atherosclerotic plaques and epicardial/perivascular fat in autopsy cases and macrophages within thrombi covering ruptured coronary plaques in thrombectomy samples from patients with acute myocardial infarction. Second, we confirmed that FABP4 was secreted from macrophages and adipocytes cultured in vitro. Third, we investigated the effect of exogenous FABP4 on macrophages and human coronary artery–derived smooth muscle cells and endothelial cells in vitro. Treatment of the cells with recombinant FABP4 significantly increased gene expression of inflammatory markers in a dose-dependent manner. Finally, ...
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renoprotective effect of renal liver type Fatty acid binding Protein and angiotensin ii type 1a receptor loss in renal injury caused by ras activation
American Journal of Physiology-renal Physiology, 2014Co-Authors: Daisuke Ichikawa, Seiko Hoshino, Atsuko Kamijoikemori, Kimie Katayama, Takeshi Sugaya, Yugo Shibagaki, Takashi Yasuda, Junko Igarashimigitaka, Kazuaki Hirata, Kenjiro KimuraAbstract:The aim of this study was to assess the renoprotective effect of renal human liver-type Fatty acid binding Protein (hL-FABP) and angiotensin II (ANG II) type 1A receptor (AT1a) loss in renal injury...
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urinary liver type Fatty acid binding Protein in septic shock effect of polymyxin b immobilized fiber hemoperfusion
Shock, 2009Co-Authors: Tsukasa Nakamura, Takeshi Sugaya, Hikaru KoideAbstract:ABSTRACTWe aimed to determine retrospectively whether urinary liver-type Fatty Acid-Binding Protein (L-FABP) levels are altered in patients with septic shock or severe sepsis without shock and whether polymyxin B-immobilized fiber (PMX-F) hemoperfusion affects these levels. Forty patients with septi
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liver Fatty acid binding Protein as a biomarker of acute kidney injury after cardiac surgery
Kidney International, 2008Co-Authors: Didier Portilla, Takeshi Sugaya, Catherine L Dent, Kiran Nagothu, I Kundi, Page C Moore, Eisei Noiri, Prasad DevarajanAbstract:Acute kidney injury (AKI) is a major complication of cardiac bypass surgery. We examined whether levels of liver Fatty Acid-Binding Protein (L-FABP) can be an early biomarker for ischemic injury by measuring this Protein in the urine of 40 pediatric patients prior to and following cardiopulmonary bypass surgery. AKI was defined as a 50% increase in the serum creatinine from baseline, which was normally not seen until 24–72 h after surgery. Enzyme-linked immunosorbent assay analysis showed increased L-FABP levels (factored for creatinine excretion) of about 94- and 45-fold at 4 and 12 h, respectively, following surgery in the 21 patients who developed AKI with western blot analysis, confirming L-FABP identity. Univariate logistic regression analyses showed that both bypass time and urinary L-FABP were significant independent risk indicators for AKI. After excluding bypass time from the model and using a stepwise multivariate logistic regression analysis, urinary L-FABP levels at 4 h after surgery were an independent risk indicator with the area under the receiver-operating characteristic curve 0.810, sensitivity 0.714, and specificity 0.684 for a 24-fold increase in urinary L-FABP. Our study shows that urinary L-FABP levels represent a sensitive and predictive early biomarker of AKI after cardiac surgery.
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urinary excretion of liver type Fatty acid binding Protein in contrast medium induced nephropathy
American Journal of Kidney Diseases, 2006Co-Authors: Tsukasa Nakamura, Takeshi Sugaya, Koichi Node, Yoshihiko Ueda, Hikaru KoideAbstract:Background: Administration of contrast agents can cause a decrease in renal function and, occasionally, end-stage renal disease. Liver-type Fatty acid–binding Protein (L-FABP) is an intracellular carrier Protein of free Fatty acids that is expressed in proximal tubules of the human kidney. Whether urinary excretion of L-FABP can predict the occurrence of contrast medium–induced nephropathy was studied. Methods: Sixty-six patients (46 men, 20 women; mean age, 60.0 years) undergoing nonemergency coronary angiography or intervention at 1 of our institutions who had a serum creatinine (Cr) level greater than 1.2 mg/dL (>106 μmol/L) and less than 2.5 mg/dL ( 44 μmol/L) or a relative increase of more than 25% at 2 to 5 days after the procedure. Results: Contrast medium–induced nephropathy occurred in 13 of 66 patients (19.7%). Before angiography, urinary L-FABP levels were significantly greater in these 13 patients (contrast medium–induced nephropathy group; 18.5 ± 12.8 μg/g Cr; range, 5.8 to 33.6 μg/g Cr) than in the remaining 53 patients (non–contrast medium–induced nephropathy group; 7.4 ± 4.4 μg/g Cr; range, 2.8 to 13.8 μg/g Cr; P P P P Conclusion: Urinary L-FABP level can serve clinically as a predictive marker for contrast medium–induced nephropathy.
Patrizia Falabella - One of the best experts on this subject based on the ideXlab platform.
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aphidius ervi teratocytes release enolase and Fatty acid binding Protein through exosomal vesicles
Frontiers in Physiology, 2019Co-Authors: Rosanna Salvia, Annalisa Grimaldi, Rossana Girardello, Carmen Scieuzo, Andrea Scala, Heiko Vogel, Sabino Aurelio Bufo, Patrizia FalabellaAbstract:: The molecular bases of the host-parasitoid interactions in the biological system Acyrthosiphon pisum (Harris) (Homoptera, Aphididae) and Aphidius ervi (Haliday) (Hymenoptera, Braconidae) have been elucidated allowing the identification of a gamma-glutamyl transpeptidase, the active component of maternal venom secretion, and teratocytes, the embryonic parasitic factors responsible for host physiology regulation after parasitization. Teratocytes, cells deriving from the dissociation of the serosa, the parasitoid embryonic membrane, are responsible for extra-oral digestion of host tissues in order to provide a suitable nutritional environment for the development of parasitoid larvae. Teratocytes rapidly grow in size without undergoing any cell division, synthesize, and release in the host hemolymph two Proteins: a Fatty acid binding Protein (Ae-FABP) and an enolase (Ae-ENO). Ae-FABP is involved in transport of Fatty acids deriving from host tissues to the parasitoid larva. Ae-ENO is an extracellular glycolytic enzyme that functions as a plasminogen like receptor inducing its activation to plasmin. Both Ae-FABP and Ae-ENO lack their signal peptides, and they are released in the extracellular environment through an unknown secretion pathway. Here, we investigated the unconventional mechanism by which teratocytes release Ae-FABP and Ae-ENO in the extracellular space. Our results, obtained using immunogold staining coupled with TEM and western blot analyses, show that these two Proteins are localized in vesicles released by teratocytes. The specific dimension of these vesicles and the immunodetection of ALIX and HSP70, two exosome markers, strongly support the hypothesis that these vesicles are exosomes.
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a novel Fatty acid binding Protein produced by teratocytes of the aphid parasitoid aphidius ervi
Insect Molecular Biology, 2005Co-Authors: Patrizia Falabella, A Tranfaglia, L Riviello, Paola Varricchio, Franco Graziani, Giuseppe Perugino, P Caccialupi, Massimiliano Rossi, C Malva, Marco MoracciAbstract:: Aphidius ervi is an endophagous braconid, parasitoid of the pea aphid, Acyrthosiphon pisum. A. ervi teratocytes, deriving from the dissociation of the embryonic serosa, synthesize and release two major Proteins into the host haemocoel. The gene of one of these Proteins has been cloned and characterized. This gene codes for a 15.8 kDa Protein belonging to the Fatty acid binding Protein (FABP) family, named Ae-FABP (A. ervi-FABP). It is abundantly present in the host haemolymph when the parasitoid larva attains its maximum growth rate. The recombinant Ae-FABP binds to Fatty acids in vitro, showing a high affinity to C14-C18 saturated Fatty acids and to oleic and arachidonic acid. The possible nutritional role for the parasitoid larva of Ae-FABP is discussed.
M J Scanlon - One of the best experts on this subject based on the ideXlab platform.
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Fatty acid binding Protein 5 facilitates the blood brain barrier transport of docosahexaenoic acid
Molecular Pharmaceutics, 2015Co-Authors: Yijun Pan, M J Scanlon, Christopher J H Porter, Yuji Owada, Yui Yamamoto, Joseph A NicolazzoAbstract:The brain has a limited ability to synthesize the essential polyunsaturated Fatty acid (PUFA) docosahexaenoic acid (DHA) from its omega-3 Fatty acid precursors. Therefore, to maintain brain concentrations of this PUFA at physiological levels, plasma-derived DHA must be transported across the blood–brain barrier (BBB). While DHA is able to partition into the luminal membrane of brain endothelial cells, its low aqueous solubility likely limits its cytosolic transfer to the abluminal membrane, necessitating the requirement of an intracellular carrier Protein to facilitate trafficking of this PUFA across the BBB. As the intracellular carrier Protein Fatty Acid-Binding Protein 5 (FABP5) is expressed at the human BBB, the current study assessed the putative role of FABP5 in the brain endothelial cell uptake and BBB transport of DHA in vitro and in vivo, respectively. hFAPB5 was recombinantly expressed and purified from Escherichia coli C41(DE3) cells and the binding affinity of DHA to hFABP5 assessed using isot...
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probing the fibrate binding specificity of rat liver Fatty acid binding Protein
Journal of Medicinal Chemistry, 2009Co-Authors: Sara Chuang, Tony Velkov, James Horne, Christopher J H Porter, Jerome Wielens, David K Chalmers, M J ScanlonAbstract:Liver-Fatty acid binding Protein (L-FABP) is found in high levels in enterocytes and is involved in cytosolic solubilization of Fatty acids. In addition, L-FABP has been shown to bind endogenous and exogenous lipophilic compounds, suggesting that it may also play a role in modulating their absorption and disposition within enterocytes. Previously, we have described binding of L-FABP to a range of drugs, including a series of fibrates. In the present study, we have generated structural models of L-FABP-fibrate complexes and undertaken thermodynamic analysis of the binding of fibrates containing either a carboxylic acid or ester functionality. Analysis of the current data reveals that both the location and the energetics of binding are different for fibrates that contain a carboxylate compared to those that do not. As such, the data presented in this study suggest potential mechanisms that underpin molecular recognition and dictate specificity in the interaction between fibrates and L-FABP.
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characterization of the drug binding specificity of rat liver Fatty acid binding Protein
Journal of Medicinal Chemistry, 2008Co-Authors: Sara Chuang, Tony Velkov, James Horne, Christopher J H Porter, M J ScanlonAbstract:Liver-Fatty acid binding Protein (L-FABP) is found in high levels in enterocytes and is involved in the cytosolic solubilization of Fatty acids during fat absorption. In the current studies, the interaction of L-FABP with a range of lipophilic drugs has been evaluated to explore the potential for L-FABP to provide an analogous function during the absorption of lipophilic drugs. Binding affinity for L-FABP was assessed by displacement of a fluorescent marker, 1-anilinonaphthalene-8-sulfonic acid (ANS), and the binding site location was determined via nuclear magnetic resonance chemical shift perturbation studies. It was found that the majority of drugs bound to L-FABP at two sites, with the internal site generally having a higher affinity for the compounds tested. Furthermore, in contrast to the interaction of L-FABP with Fatty acids, it was demonstrated that a terminal carboxylate is not required for specific binding of lipophilic drugs at the internal site of L-FABP.
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examination of the role of intestinal Fatty acid binding Protein in drug absorption using a parallel artificial membrane permeability assay
Chemistry & Biology, 2007Co-Authors: Tony Velkov, James Horne, Aisha Laguerre, Eric Dale Jones, M J Scanlon, Christopher J H PorterAbstract:Transcellular diffusion across the absorptive epithelial cells (enterocytes) of the small intestine is the main route of absorption for most orally administered drugs. The process by which lipophilic compounds transverse the aqueous environment of the cytoplasm, however, remains poorly defined. In the present study, we have identified a structurally diverse group of lipophilic drugs that display low micromolar binding affinities for a cytosolic lipid-binding Protein—intestinal Fatty Acid-Binding Protein (I-FABP). Binding to I-FABP significantly enhanced the transport of lipophilic drug molecules across a model membrane, and the degree of transport enhancement was related to both drug lipophilicity and I-FABP binding affinity. These data suggest that intracellular lipid-binding Proteins such as I-FABP may enhance the membrane transport of lipophilic xenobiotics and facilitate drug access to the enterocyte cytoplasm and cytoplasmic organelles.
Judith Storch - One of the best experts on this subject based on the ideXlab platform.
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liver Fatty acid binding Protein binds monoacylglycerol in vitro and in mouse liver cytosol
Journal of Biological Chemistry, 2013Co-Authors: William S Lagakos, Xudong Guan, Luciana Rodriguez Sawicki, Betina Corsico, Sarala Kodukula, Kaeko Murota, Ruth E Stark, Judith StorchAbstract:Liver Fatty Acid-Binding Protein (LFABP; FABP1) is expressed both in liver and intestinal mucosa. Mice null for LFABP were recently shown to have altered metabolism of not only Fatty acids but also monoacylglycerol, the two major products of dietary triacylglycerol hydrolysis (Lagakos, W. S., Gajda, A. M., Agellon, L., Binas, B., Choi, V., Mandap, B., Russnak, T., Zhou, Y. X., and Storch, J. (2011) Am. J. Physiol. Gastrointest. Liver Physiol. 300, G803–G814). Nevertheless, the binding and transport of monoacylglycerol (MG) by LFABP are uncertain, with conflicting reports in the literature as to whether this single chain amphiphile is in fact bound by LFABP. In the present studies, gel filtration chromatography of liver cytosol from LFABP−/− mice shows the absence of the low molecular weight peak of radiolabeled monoolein present in the fractions that contain LFABP in cytosol from wild type mice, indicating that LFABP binds sn-2 MG in vivo. Furthermore, solution-state NMR spectroscopy demonstrates two molecules of sn-2 monoolein bound in the LFABP binding pocket in positions similar to those found for oleate binding. Equilibrium binding affinities are ∼2-fold lower for MG compared with Fatty acid. Finally, kinetic studies examining the transfer of a fluorescent MG analog show that the rate of transfer of MG is 7-fold faster from LFABP to phospholipid membranes than from membranes to membranes and occurs by an aqueous diffusion mechanism. These results provide strong support for monoacylglycerol as a physiological ligand for LFABP and further suggest that LFABP functions in the efficient intracellular transport of MG. Background: The intracellular carrier Protein(s) for monoacylglycerols (MGs) is unknown. Results: Using chromatography and NMR and fluorescence spectroscopy, we show that liver Fatty Acid-Binding Protein (LFABP) is a binding Protein for MG and promotes rapid MG transfer to membranes. Conclusion: LFABP binds MG in vitro and in liver cytosol. Significance: LFABP may transport MG, a metabolic intermediate and signaling molecule, in liver and intestinal cytosol.
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solution state molecular structure of apo and oleate liganded liver Fatty acid binding Protein
Biochemistry, 2007Co-Authors: Xiaomin Yang, Judith Storch, Sarala Kodukula, Hsin Wang, Rima Estephan, Fouad Francis, Ruth E StarkAbstract:Rat liver Fatty Acid-Binding Protein (LFABP) is distinctive among intracellular lipid-binding Proteins (iLBPs): more than one molecule of long-chain Fatty acid and a variety of diverse ligands can be bound within its large cavity, and in vitro lipid transfer to model membranes follows a mechanism that is diffusion-controlled rather than mediated by Protein-membrane collisions. Because the apoProtein has proven resistant to crystallization, nuclear magnetic resonance spectroscopy offers a unique route to functionally informative comparisons of molecular structure and dynamics for LFABP in free (apo) and liganded (holo) forms. We report herein the solution-state structures determined for apo-LFABP at pH 6.0 and for holoProtein liganded to two oleates at pH 7.0, as well as the structure of the complex including locations of the ligands. 1H, 13C, and 15N resonance assignments revealed very similar types and locations of secondary structural elements for apo- and holo-LFABP as judged from chemical shift indices. The solution-state tertiary structures of the Proteins were derived with the CNS/ARIA computational protocol, using distance and angular restraints based on 1H-1H nuclear Overhauser effects (NOEs), hydrogen-bonding networks, 3J(HNHA) coupling constants, intermolecular NOEs, and residual dipolar (NH) couplings. The holo-LFABP solution-state conformation is in substantial agreement with a previously reported X-ray structure [Thompson, J., Winter, N., Terwey, D., Bratt, J., and Banaszak, L. (1997) The crystal structure of the liver Fatty Acid-Binding Protein. A complex with two bound oleates, J. Biol. Chem. 272, 7140-7150], including the typical beta-barrel capped by a helix-turn-helix portal. In the solution state, the internally bound oleate has the expected U-shaped conformation and is tethered electrostatically, but the extended portal ligand can adopt a range of conformations based on the computationally refined structures, in contrast to the single conformation observed in the crystal structure. The apo-LFABP also has a well-defined beta-barrel structural motif typical of other members of the iLBP Protein family, but the portal region that is thought to facilitate ligand entry and exit exhibits conformational variability and an unusual "open cap" orientation with respect to the barrel. These structural results allow us to propose a model in which ligand binding to LFABP occurs through conformational fluctuations that adjust the helix-turn-helix motif to open or close the top of the beta-barrel, and solvent accessibility to the Protein cavity favors diffusion-controlled ligand transport.
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role of surface lysine residues of adipocyte Fatty acid binding Protein in Fatty acid transfer to phospholipid vesicles
Biochemistry, 2001Co-Authors: Hengling Liou, Judith StorchAbstract:The tertiary structure of murine adipocyte Fatty Acid-Binding Protein (AFABP) is a flattened 10-stranded β-barrel capped by a helix−turn−helix segment. This helical domain is hypothesized to behave as a “lid” or portal for ligand entry into and exit from the binding cavity. Previously, we demonstrated that anthroyloxy-labeled Fatty acid (AOFA) transfer from AFABP to phospholipid membranes occurs by a collisional process, in which ionic interactions between positively charged lysine residues on the Protein surface and negatively charged phospholipid headgroups are involved. In the present study, the role of specific lysine residues located in the portal and other regions of AFABP was directly examined using site-directed mutagenesis. The results showed that isoleucine replacement for lysine in the portal region, including the αI- and αII-helices and the β C-D turn, resulted in much slower 2-(9-anthroyloxy)palmitate (2AP) transfer rates to acidic membranes than those of native AFABP. An additive effect was ...
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role of portal region lysine residues in electrostatic interactions between heart Fatty acid binding Protein and phospholipid membranes
Biochemistry, 1996Co-Authors: Fiona M Herr, Jed Aronson, Judith StorchAbstract:The structure of heart Fatty acid binding Protein (HFABP) is a flattened β-barrel comprising 10 antiparallel β-sheets capped by two α-helical segments. The helical cap region is hypothesized to behave as a portal “lid” for the entry and release of ligand from the binding pocket. The transfer of Fatty acid from HFABP is thought to occur via effective collisional interactions with membranes, and these interactions are enhanced when transfer is to membranes of net negative charge, thus implying that specific basic residues on the surface of HFABP may govern the transfer process [Wootan, M. G., & Storch, J. (1994) J. Biol. Chem. 269, 10517−10523]. To directly examine the role of charged lysine residues on the HFABP surface in specific interactions with membranes, chemical modification and selective mutagenesis of HFABP were used. All surface lysine residues were neutralized by acetylation of recombinant HFABP with acetic anhydride. In addition, seven mutant HFABPs were generated that resulted in charge altera...
Christopher J H Porter - One of the best experts on this subject based on the ideXlab platform.
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Fatty acid binding Protein 5 facilitates the blood brain barrier transport of docosahexaenoic acid
Molecular Pharmaceutics, 2015Co-Authors: Yijun Pan, M J Scanlon, Christopher J H Porter, Yuji Owada, Yui Yamamoto, Joseph A NicolazzoAbstract:The brain has a limited ability to synthesize the essential polyunsaturated Fatty acid (PUFA) docosahexaenoic acid (DHA) from its omega-3 Fatty acid precursors. Therefore, to maintain brain concentrations of this PUFA at physiological levels, plasma-derived DHA must be transported across the blood–brain barrier (BBB). While DHA is able to partition into the luminal membrane of brain endothelial cells, its low aqueous solubility likely limits its cytosolic transfer to the abluminal membrane, necessitating the requirement of an intracellular carrier Protein to facilitate trafficking of this PUFA across the BBB. As the intracellular carrier Protein Fatty Acid-Binding Protein 5 (FABP5) is expressed at the human BBB, the current study assessed the putative role of FABP5 in the brain endothelial cell uptake and BBB transport of DHA in vitro and in vivo, respectively. hFAPB5 was recombinantly expressed and purified from Escherichia coli C41(DE3) cells and the binding affinity of DHA to hFABP5 assessed using isot...
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probing the fibrate binding specificity of rat liver Fatty acid binding Protein
Journal of Medicinal Chemistry, 2009Co-Authors: Sara Chuang, Tony Velkov, James Horne, Christopher J H Porter, Jerome Wielens, David K Chalmers, M J ScanlonAbstract:Liver-Fatty acid binding Protein (L-FABP) is found in high levels in enterocytes and is involved in cytosolic solubilization of Fatty acids. In addition, L-FABP has been shown to bind endogenous and exogenous lipophilic compounds, suggesting that it may also play a role in modulating their absorption and disposition within enterocytes. Previously, we have described binding of L-FABP to a range of drugs, including a series of fibrates. In the present study, we have generated structural models of L-FABP-fibrate complexes and undertaken thermodynamic analysis of the binding of fibrates containing either a carboxylic acid or ester functionality. Analysis of the current data reveals that both the location and the energetics of binding are different for fibrates that contain a carboxylate compared to those that do not. As such, the data presented in this study suggest potential mechanisms that underpin molecular recognition and dictate specificity in the interaction between fibrates and L-FABP.
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characterization of the drug binding specificity of rat liver Fatty acid binding Protein
Journal of Medicinal Chemistry, 2008Co-Authors: Sara Chuang, Tony Velkov, James Horne, Christopher J H Porter, M J ScanlonAbstract:Liver-Fatty acid binding Protein (L-FABP) is found in high levels in enterocytes and is involved in the cytosolic solubilization of Fatty acids during fat absorption. In the current studies, the interaction of L-FABP with a range of lipophilic drugs has been evaluated to explore the potential for L-FABP to provide an analogous function during the absorption of lipophilic drugs. Binding affinity for L-FABP was assessed by displacement of a fluorescent marker, 1-anilinonaphthalene-8-sulfonic acid (ANS), and the binding site location was determined via nuclear magnetic resonance chemical shift perturbation studies. It was found that the majority of drugs bound to L-FABP at two sites, with the internal site generally having a higher affinity for the compounds tested. Furthermore, in contrast to the interaction of L-FABP with Fatty acids, it was demonstrated that a terminal carboxylate is not required for specific binding of lipophilic drugs at the internal site of L-FABP.
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examination of the role of intestinal Fatty acid binding Protein in drug absorption using a parallel artificial membrane permeability assay
Chemistry & Biology, 2007Co-Authors: Tony Velkov, James Horne, Aisha Laguerre, Eric Dale Jones, M J Scanlon, Christopher J H PorterAbstract:Transcellular diffusion across the absorptive epithelial cells (enterocytes) of the small intestine is the main route of absorption for most orally administered drugs. The process by which lipophilic compounds transverse the aqueous environment of the cytoplasm, however, remains poorly defined. In the present study, we have identified a structurally diverse group of lipophilic drugs that display low micromolar binding affinities for a cytosolic lipid-binding Protein—intestinal Fatty Acid-Binding Protein (I-FABP). Binding to I-FABP significantly enhanced the transport of lipophilic drug molecules across a model membrane, and the degree of transport enhancement was related to both drug lipophilicity and I-FABP binding affinity. These data suggest that intracellular lipid-binding Proteins such as I-FABP may enhance the membrane transport of lipophilic xenobiotics and facilitate drug access to the enterocyte cytoplasm and cytoplasmic organelles.
