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Brain transporters

Leptin is a cytokine produced and secreted by adipose tissue in proportion to the body fat content [3]. Mice and humans lacking leptin or its receptor develop a severe hyperphagia and a dramatic degree of obesity which is considerably more pronounced than that of the NDRKO mouse. Thus, leptin is the key adiposity signal in rodents and humans. Leptin secretion appears to reflect the metabolic status of the adipocyte rather than the sheer size of triglyceride deposits, and leptin levels may transiently be dissociated from total body fat. Nonetheless, over the course of a day with unrestricted food supply, plasma leptin levels reliably reflect the amount of total body fat. Local administration of leptin into the brain results in reduced food intake. The vast majority of patients with obesity have elevated serum levels of leptin. Thus, it is believed that the polygenic obesity is due to leptin resistance rather than to inadequate leptin secretion, or to a reduced blood/brain transport of the cytokine. [Pg.209]

Drion N, Lemaire M, Lefauconnier JM, Scherrmann JM. Role of P-glyco-protein in the blood-brain transport of colchicine and vinblastine. J Neurochem 1996 67 1688-1693. [Pg.334]

Kandimalla KK, Donovan MD, Carrier (2003) Mediated transport of chlorpheniramine and chlorcyclizine across bovine olfactory mucosa Implications on nose-to-brain transport. J Pharm Sci 94 613-624. [Pg.130]

Basak SC, Gute BD, Drewes LR (1996) Predicting blood-brain transport of drugs a computational approach. Pharm Res 13 775-778. [Pg.554]

The interest of glycosyl phosphoric acid triester moieties (9.43) as brain transport vectors is seemingly not limited to AZT and analogues. Indeed,... [Pg.576]

Membrane transporter proteins (MDR or ABC transporter proteins) such as p-glycoprotein are crucially important in the process of excretion and also in absorption and distribution and elimination of chemicals from cells. These transport organic anions or cations and neutral compounds across membranes, pump unwanted chemicals out of cells such as in gut, placenta, and brain, transport chemicals into bile from liver cells, and facilitate excretion from the kidney. [Pg.72]

Ilium, L. 2004. Is nose-to-brain transport of drugs in man a reality. J Pharm Pharmacol 56 3. [Pg.372]

Melethil SK Mechanism of blood-brain transport of aluminum in rats University of Missouri Kansas National Institute of Environmental Health Sciences... [Pg.168]

The pharmacological effect of L-dopa is affected by diet (362). The off period in Parkinsonian patients treated with L-dopa is a clinical problem, since the efficacy of the drug suddenly fails. Because of the inverse relationship between the plasma levels of large neutral amino acid (LNAA) and the clinical performance of Parkinsonian patients (362) and the fact that the transcellular transport of L-leucine is inhibited by L-dopa (363) across primary cultured bovine brain capillary endothelial cells, the off period may be attributed to the membrane transport of L-dopa via LNAAT at the BBB. In addition to L-dopa, baclofen and melphalan are suggested to be taken up into the brain via amino acid transporter (363,364), and thereby, their brain transport might be also affected by the plasma concentration of large neutral amino acids. [Pg.175]

The BBB model system of RBE4 cells (Roux et al. 1994) is used in many publications to study brain transport (carnitine Mroczkowska et al. 2000 P-glycoprotein and Mrpl Begley et al. 1996 and Regina et al. 1998) as well as drag metabolising enzyme activities (Chat et al. 1998). [Pg.529]

Patrini C, Reggiani C, LaforenzaU, and Hindi G (1988) Blood-brain transport of thiamine monophosphate in the rat a kinetic study invivo. Journal of Neurochemistry 50,90-3. [Pg.446]

Disruption was the first BBB function noted to be perturbed in neuroimmune disease. Hov ever, the review above makes it clear that an increase in the BBB permeability can be induced for specific agents by increasing their blood-to-brain transport rate or inhibiting their brain-to-blood efflux rate. [Pg.33]

Figure 47.5. Effect of HRP modification with Pluronic block copolymer on transport across the BBB in an in vitro and in vivo models. A HRP conjugated with Pluronic P85 via the biodegradable bond B confocal microphotograph of BBMEC monolayers treated with rhodamine-labeled HRP and Pluronic-HRP for 2h C blood-to-brain transport of HRP and Pluronic-HRP in mice. Figure 47.5. Effect of HRP modification with Pluronic block copolymer on transport across the BBB in an in vitro and in vivo models. A HRP conjugated with Pluronic P85 via the biodegradable bond B confocal microphotograph of BBMEC monolayers treated with rhodamine-labeled HRP and Pluronic-HRP for 2h C blood-to-brain transport of HRP and Pluronic-HRP in mice.
Basak, S.C., Gute, B.D. and Drewes, L.R. (1996). Predicting Blood-Brain Transport of Drugs A Computational Approach. Pharm.Res., 13,775-778. [Pg.535]

In addition to the above uptake transporters that predominately express in the intestine, uptake transporters that function in other tissues also express in the intestine. For example, brain transporter OATP1A2, hepatic transporter OATP1B1, and OATP1B3 have been detected in human intestine [51]. In the intestine, OATP1A2 is localized on the apical membrane, and is the key uptake transporter for fexofenadine [51] and levofloxacin [12]. OATP1A2 was reported to be natively expressed in... [Pg.367]

Figure 3.2. Potential mechanisms for drug movement across the blood-brain barrier. Routes of passage include passive diffusion through the brain capillary endothelial cells (A) utilization of inwardly directed (i.e. towards brain) transport or carrier systems expressed on brain capillary endothelial cells (B) utilization of outwardly directed (i.e. towards blood) efflux transport systems (C) or inclusion in various endocytic vesicular transport processes occurring within the brain capillary endothelial cells (D). Figure 3.2. Potential mechanisms for drug movement across the blood-brain barrier. Routes of passage include passive diffusion through the brain capillary endothelial cells (A) utilization of inwardly directed (i.e. towards brain) transport or carrier systems expressed on brain capillary endothelial cells (B) utilization of outwardly directed (i.e. towards blood) efflux transport systems (C) or inclusion in various endocytic vesicular transport processes occurring within the brain capillary endothelial cells (D).
Clinical evaluation in treatment of AIDS L. Wet-terberg et al, ibid. 159. Chromatographic purification of [n-Aia J peptide T amide, a metabolically stable and more potent analog of peptide T T. R. Burke, M. Knight, J. Chromatog. 411, 431 ( 987). Blood to brain transport of the amide in mice C. M. Barrera et al, Brain Res. Bull 19, 629 (1987). Brief review of dehate over effectiveness of peptide T D. M. Barnes, Science 237, 128 (1987). [Pg.1134]

Drewes, L. R., and A. K. Singh. 1987. Cerebral metabolism and blood brain transport toxicity of organophosphorus compounds. Govt. Rep. Announce. Index (U.S.) 88(22), Abstr. No. 856, p. 413 cited in Chem. Abstr. CA III(l) 2296k. [Pg.687]

Vyas, T.K., A. Shahiwala, and M.M. Amiji. 2008. Improved oral bioavailabiUty and brain transport of saquinavir upon administration in novel nanoemulsion formulations. Int. J. Pharm. 347(l-2) 93-101. [Pg.528]

Gross, P. M., Teasdale, G. M., Graham, D. I., Angerson, W. J., and Harper, A. M., 1982, Intra-arterial histamine increases blood-brain transport in rats. Am. J. Physiol. 243 H307-H317. [Pg.208]

Cheng Q et al (2008) Brain transport of neurotoxin-I with PLA nanoparticles through intranasal administration in rats a microdialysis study. Biopharm Drug Dispos 29 431... [Pg.84]


See other pages where Brain transporters is mentioned: [Pg.255]    [Pg.516]    [Pg.578]    [Pg.338]    [Pg.32]    [Pg.33]    [Pg.32]    [Pg.33]    [Pg.487]    [Pg.902]    [Pg.223]   
See also in sourсe #XX -- [ Pg.416 , Pg.417 , Pg.420 ]

See also in sourсe #XX -- [ Pg.416 , Pg.417 , Pg.420 ]

See also in sourсe #XX -- [ Pg.416 , Pg.417 , Pg.420 ]

See also in sourсe #XX -- [ Pg.416 , Pg.417 , Pg.420 ]




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Active efflux transporters blood-brain barrier

Blood brain barrier drug efflux transport systems role

Blood brain barrier transport across

Blood brain barrier transporters

Blood-brain barrier active transport

Blood-brain barrier carrier-mediated transport

Blood-brain barrier nutrient transport across

Blood-brain barrier specialized transport systems

Blood-brain barrier transmembrane transport

Blood-brain barrier transport mechanisms

Blood-brain barrier transport proteins expression

Blood-brain barrier transport vectors

Brain astrocytic glutamate transporters

Brain transport systems

Brain vesicular glutamate transporters

Carrier-mediated transporters blood-brain barrier

Cytokine blood-brain barrier transport

Glucose transporters blood-brain barrier

Glutamate transporters and their role in brain

Immune cells blood-brain barrier transport

Interleukin blood-brain barrier transport

Leptin, blood-brain barrier transport

Morphine, blood-brain barrier transport

Opiate , blood-brain barrier transport

Opioid transportation from blood-brain

Receptor-mediated transporters blood-brain barrier

Transport Mechanisms Across the Blood-Brain Barrier

Transport at the Blood-Brain Barrier

Transport blood-brain barrier

Viruses blood-brain barrier transport

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