Relevant bibliographies by topics / OCTN2

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers

Academic literature on the topic 'OCTN2'

Author: Grafiati
Published: 4 June 2021
Last updated: 15 February 2022

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'OCTN2.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Journal articles on the topic "OCTN2"

1

Pochini, Lorena, Michele Galluccio, Mariafrancesca Scalise, Lara Console, and Cesare Indiveri. "OCTN: A Small Transporter Subfamily with Great Relevance to Human Pathophysiology, Drug Discovery, and Diagnostics." SLAS DISCOVERY: Advancing the Science of Drug Discovery 24, no. 2 (December 7, 2018): 89–110. http://dx.doi.org/10.1177/2472555218812821.

Full text
Abstract:
OCTN is a small subfamily of membrane transport proteins that belongs to the larger SLC22 family. Two of the three members of the subfamily, namely, OCTN2 and OCTN1, are present in humans. OCTN2 plays a crucial role in the absorption of carnitine from diet and in its distribution to tissues, as demonstrated by the occurrence of severe pathologies caused by malfunctioning or altered expression of this transporter. These findings suggest avoiding a strict vegetarian diet during pregnancy and in childhood. Other roles of OCTN2 are related to the traffic of carnitine derivatives in many tissues. The role of OCTN1 is still unclear, despite the identification of some substrates such as ergothioneine, acetylcholine, and choline. Plausibly, the transporter acts on the control of inflammation and oxidative stress, even though knockout mice do not display phenotypes. A clear role of both transporters has been revealed in drug interaction and delivery. The polyspecificity of the OCTNs is at the base of the interactions with drugs. Interestingly, OCTN2 has been recently exploited in the prodrug approach and in diagnostics. A promising application derives from the localization of OCTN2 in exosomes that represent a noninvasive diagnostic tool.
APA, Harvard, Vancouver, ISO, and other styles
2

Pochini, Lorena, Mariafrancesca Scalise, Michele Galluccio, and Cesare Indiveri. "OCTN Cation Transporters in Health and Disease." Journal of Biomolecular Screening 18, no. 8 (June 14, 2013): 851–67. http://dx.doi.org/10.1177/1087057113493006.

Full text
Abstract:
The three members of the organic cation transporter novel subfamily are known to be involved in interactions with xenobiotic compounds. These proteins are characterized by 12 transmembrane segments connected by nine short loops and two large hydrophilic loops. It has been recently pointed out that acetylcholine is a physiological substrate of OCTN1. Its transport could be involved in nonneuronal cholinergic functions. OCTN2 maintains the carnitine homeostasis, resulting from intestinal absorption, distribution to tissues, and renal excretion/reabsorption. OCTN3, identified only in mouse, mediates also carnitine transport. OCTN1 and OCTN2 are associated with several pathologies, such as inflammatory bowel disease, primary carnitine deficiency, diabetes, neurological disorders, and cancer, thus representing useful pharmacological targets. The function and interaction with drugs of OCTNs have been studied in intact cell systems and in proteoliposomes. The latter experimental model enables reduced interference from other transporters or enzyme pathways. Using proteoliposomes, the molecular bases of toxicity of some drugs have recently been revealed. Therefore, proteoliposomes represent a promising experimental tool suitable for large-scale molecular screening of interactions of OCTNs with chemicals regarding human health.
APA, Harvard, Vancouver, ISO, and other styles
3

Kobayashi, Daisuke, Ikumi Tamai, Yoshimichi Sai, Kazuhiro Yoshida, Tomohiko Wakayama, Yasuto Kido, Jun-ichi Nezu, Shoichi Iseki, and Akira Tsuji. "Transport of carnitine and acetylcarnitine by carnitine/organic cation transporter (OCTN) 2 and OCTN3 into epididymal spermatozoa." Reproduction 134, no. 5 (November 2007): 651–58. http://dx.doi.org/10.1530/rep-06-0173.

Full text
Abstract:
Carnitine and acetylcarnitine are important for the acquisition of motility and maturation of spermatozoa in the epididymis. In this study, we examined the involvement of carnitine/organic cation transporter (OCTN) in carnitine and acetylcarnitine transport in epididymal spermatozoa of mice. Uptake of both compounds by epididymal spermatozoa was time-dependent and partially Na+-dependent. Kinetic analyses revealed the presence of a high-affinity transport system in the spermatozoa, withKmvalues of 23.6 and 6.57 μM for carnitine and acetylcarnitine respectively in the presence of Na+. Expression of OCTN2 and OCTN3 in epididymal spermatozoa was confirmed by immunofluorescence analysis. The involvement of these two transporters in carnitine and acetylcarnitine transport was supported by a selective inhibition study. We conclude that both Na+-dependent and -independent carnitine transporters, OCTN2 and OCTN3, mediate the supply of carnitine and acetylcarnitine to epididymal spermatozoa in mice.
APA, Harvard, Vancouver, ISO, and other styles
4

Burckhardt, Gerhard, and Natascha A. Wolff. "Structure of renal organic anion and cation transporters." American Journal of Physiology-Renal Physiology 278, no. 6 (June 1, 2000): F853—F866. http://dx.doi.org/10.1152/ajprenal.2000.278.6.f853.

Full text
Abstract:
Here we review the structural and functional properties of organic anion transporters (OAT1, OAT2, OAT3) and organic cation transporters (OCTN1, OCTN2, OCT1, OCT2, OCT3), some of which are involved in renal proximal tubular organic anion and cation secretion. These transporters share a predicted 12-transmembrane domain (TMD) structure with a large extracellular loop between TMD1 and TMD2, carrying potential N-glycosylation sites. Conserved amino acid motifs revealed a relationship to the sugar transporter family within the major facilitator superfamily. Following heterologous expression, most OATs transported the model anion p-aminohippurate (PAH). OAT1, but not OAT2, exhibited PAH-α-ketoglutarate exchange. OCT1–3 transported the model cations tetraethylammonium (TEA), N1-methylnicotinamide, and 1-methyl-4-phenylpyridinium. OCTNs exhibited transport of TEA and/or preferably the zwitterionic carnitine. Substrate substitution as well as cis-inhibition experiments demonstrated polyspecificity of the OATs, OCTs, and OCTN1. On the basis of comparison of the structurally closely related OATs and OCTs, it may be possible to delineate the binding sites for organic anions and cations in future experiments.
APA, Harvard, Vancouver, ISO, and other styles
5

Koch, Alexander, Bettina König, Sebastian Luci, Gabriele I. Stangl, and Klaus Eder. "Dietary oxidised fat up regulates the expression of organic cation transporters in liver and small intestine and alters carnitine concentrations in liver, muscle and plasma of rats." British Journal of Nutrition 98, no. 5 (November 2007): 882–89. http://dx.doi.org/10.1017/s000711450775691x.

Full text
Abstract:
It has been shown that treatment of rats with clofibrate, a synthetic agonist of PPARα, increases mRNA concentration of organic cation transporters (OCTN)-1 and -2 and concentration of carnitine in the liver. Since oxidised fats have been demonstrated in rats to activate hepatic PPARα, we tested the hypothesis that they also up regulate OCTN. Eighteen rats were orally administered either sunflower-seed oil (control group) or an oxidised fat prepared by heating sunflower-seed oil, for 6 d. Rats administered the oxidised fat had higher mRNA concentrations of typical PPARα target genes such as acyl-CoA oxidase, cytochrome P450 4A1 and carnitine palmitoyltransferases-1A and -2 in liver and small intestine than control rats (P < 0·05). Furthermore, rats treated with oxidised fat had higher hepatic mRNA concentrations of OCTN1 (1·5-fold) and OCTN2 (3·1-fold), a higher carnitine concentration in the liver and lower carnitine concentrations in plasma, gastrocnemius and heart muscle than control rats (P < 0·05). Moreover, rats administered oxidised fat had a higher mRNA concentration of OCTN2 in small intestine (2·4-fold; P < 0·05) than control rats. In conclusion, the present study shows that an oxidised fat causes an up regulation of OCTN in the liver and small intestine. An increased hepatic carnitine concentration in rats treated with the oxidised fat is probably at least in part due to an increased uptake of carnitine into the liver which in turn leads to reduced plasma and muscle carnitine concentrations. The present study supports the hypothesis that nutrients acting as PPARα agonists influence whole-body carnitine homeostasis.
APA, Harvard, Vancouver, ISO, and other styles
6

Karimian Pour, Navaz, Eliza R. McColl, and Micheline Piquette-Miller. "Impact of Viral Inflammation on the Expression of Renal Drug Transporters in Pregnant Rats." Pharmaceutics 11, no. 12 (November 22, 2019): 624. http://dx.doi.org/10.3390/pharmaceutics11120624.

Full text
Abstract:
Inflammation impacts the expression and function of drug transporters at term-gestation; however, the impact of inflammation on the expression of drug transporters at mid-gestation is largely unknown. Since renal drug transporters play a key role in the clearance of many drugs prescribed during pregnancy, our objective was to study the impact of the viral mimetic poly I:C on the expression of renal transporters in pregnant rats at mid-gestation. Poly I:C (10 mg/kg) or saline was administered intraperitoneally to pregnant Sprague–Dawley rats on gestational day 14. Expression of renal transporters was measured at 6, 24, and 48 h by qRT-PCR and Western blot. The mRNA levels of Mdr1a, Mrp4, Oct2, Octn1, Octn2, Mate1, Oat1-3, Urat1, Oatp4c1, Ent1, and Pept2 were significantly lower in the poly I:C group at 6 h. At 24 h, only the mRNA levels of Oct2, Oatp4c1, and Ent1 were decreased compared to saline. Poly I:C significantly decreased protein expression of Urat1 at 24 h, and P-gp, Oct2, Mate1, Oat1, Oat3 at 48 h,. Poly I:C imposed significant reductions in the expression of several key renal transporters at mid-gestation in pregnant rats. Thus, viral infection may impact renal excretion of drug transporter substrates, potentially leading to drug–disease interactions.
APA, Harvard, Vancouver, ISO, and other styles
7

Srinivas, Sonne R., Puttur D. Prasad, Nagavedi S. Umapathy, Vadivel Ganapathy, and Prem S. Shekhawat. "Transport of butyryl-l-carnitine, a potential prodrug, via the carnitine transporter OCTN2 and the amino acid transporter ATB0,+." American Journal of Physiology-Gastrointestinal and Liver Physiology 293, no. 5 (November 2007): G1046—G1053. http://dx.doi.org/10.1152/ajpgi.00233.2007.

Full text
Abstract:
l-Carnitine is absorbed in the intestinal tract via the carnitine transporter OCTN2 and the amino acid transporter ATB0,+. Loss-of-function mutations in OCTN2 may be associated with inflammatory bowel disease (IBD), suggesting a role for carnitine in intestinal/colonic health. In contrast, ATB0,+ is upregulated in bowel inflammation. Butyrate, a bacterial fermentation product, is beneficial for prevention/treatment of ulcerative colitis. Butyryl-l-carnitine (BC), a butyrate ester of carnitine, may have potential for treatment of gut inflammation, since BC would supply both butyrate and carnitine. We examined the transport of BC via ATB0,+ to determine if this transporter could serve as a delivery system for BC. We also examined the transport of BC via OCTN2. Studies were done with cloned ATB0,+ and OCTN2 in heterologous expression systems. BC inhibited ATB0,+-mediated glycine transport in mammalian cells (IC50, 4.6 ± 0.7 mM). In Xenopus laevis oocytes expressing human ATB0,+, BC induced Na+-dependent inward currents under voltage-clamp conditions. The currents were saturable with a K0.5 of 1.4 ± 0.1 mM. Na+ activation kinetics of BC-induced currents suggested involvement of two Na+ per transport cycle. BC also inhibited OCTN2-mediated carnitine uptake (IC50, 1.5 ± 0.3 μM). Transport of BC via OCTN2 is electrogenic, as evidenced from BC-induced inward currents. These currents were Na+ dependent and saturable ( K0.5, 0.40 ± 0.02 μM). We conclude that ATB0,+ is a low-affinity/high-capacity transporter for BC, whereas OCTN2 is a high-affinity/low-capacity transporter. ATB0,+ may mediate intestinal absorption of BC when OCTN2 is defective.
APA, Harvard, Vancouver, ISO, and other styles
8

Sayed-Ahmed, Mohamed M., Meshan Lafi Aldelemy, Mohamed M. Hafez, and Othman A. Al-Shabanah. "Inhibition of Gene Expression of Organic Cation/Carnitine Transporter and Antioxidant Enzymes in Oxazaphosphorines-Induced Acute Cardiomyopathic Rat Models." Oxidative Medicine and Cellular Longevity 2012 (2012): 1–13. http://dx.doi.org/10.1155/2012/452902.

Full text
Abstract:
It is well documented that high therapeutic doses of oxazaphosphorines, cyclophosphamide (CP) and ifosfamide (IFO), are associated with cardiomyopathy. This study investigated whether oxazaphosphorines alter the expression of organic cation/carnitine transporter (OCTN2) and antioxidant genes and if so, whether these alterations contribute to CP and IFO-induced cardiotoxicity. Adult male Wistar albino rats were assigned to one of six treatment groups namely, control, L carnitine, CP, IFO, CP plus L carnitine and IFO plus L carnitine. In cardiac and kidney tissues, CP and IFO significantly decreased mRNA and protein expression of OCTN2. Oxazaphosphorines significantly increased serum acyl-carnitine/free carnitine ratio and urinary carnitine excretion and significantly decreased total carnitine in cardiac tissues. Interestingly, carnitine supplementation completely reversed the biochemical and gene expression changes-induced by oxazaphosphorines to the control values, except OCTN2 expression remained inhibited by IFO. Data from this study suggest that: (1) Oxazaphosphorines decreased myocardial carnitine content following the inhibition of OCTN2 mRNA and protein expression in cardiac tissues. (2) Oxazaphosphorine therapy increased urinary loss of carnitine secondary to the inhibition of OCTN2 mRNA and protein expression in proximal tubules of the kidney. (3) Carnitine supplementation attenuates CP but not IFO-induced inhibition of OCTN2 mRNA and protein expression in heart and kidney tissues.
APA, Harvard, Vancouver, ISO, and other styles
9

Shekhawat, Prem S., Han-Soo Yang, Michael J. Bennett, Alva Lee Carter, Dietrich Matern, Ikumi Tamai, and Vadivel Ganapathy. "Carnitine Content and Expression of Mitochondrial β-Oxidation Enzymes in Placentas of Wild-Type (OCTN2+/+) and OCTN2 Null (OCTN2−/−) Mice." Pediatric Research 56, no. 3 (September 2004): 323–28. http://dx.doi.org/10.1203/01.pdr.0000134252.02876.55.

Full text
APA, Harvard, Vancouver, ISO, and other styles
10

Elimrani, Ihsan, Karim Lahjouji, Ernest Seidman, Marie-Josée Roy, Grant A. Mitchell, and Ijaz Qureshi. "Expression and localization of organic cation/carnitine transporter OCTN2 in Caco-2 cells." American Journal of Physiology-Gastrointestinal and Liver Physiology 284, no. 5 (May 1, 2003): G863—G871. http://dx.doi.org/10.1152/ajpgi.00220.2002.

Full text
Abstract:
l-Carnitine is derived both from dietary sources and biosynthesis. Dietary carnitine is absorbed in the small intestine and then distributed to other organs. Previous studies using Caco-2 cells demonstrated that the transport ofl-carnitine in the intestine involves a carrier-mediated system. The purpose of this study was to determine whether the uptake of l-carnitine in Caco-2 cells is mediated by the recently identified organic cation/carnitine transporter (OCTN2). Kinetics ofl-[3H]carnitine uptake were investigated with or without specific inhibitors. l-Carnitine uptake in mature cells was sodium dependent and linear with time. K m and Vmax values for saturable uptake were 14.07 ± 1.70 μM and 26.3 ± 0.80 pmol · mg protein−1 · 6 min−1, respectively. l-carnitine uptake was inhibited ( P < 0.05–0.01) by valproate and other organic cations. Anti-OCTN2 antibodies recognized a protein in the brush-border membrane (BBM) of Caco-2 cells with an apparent molecular mass of 60 kDa. The OCTN2 expression was confirmed by double immunostaining. Our results demonstrate that l-carnitine uptake in differentiated Caco-2 cells is primarily mediated by OCTN2, located on the BBM.
APA, Harvard, Vancouver, ISO, and other styles
More sources

Dissertations / Theses on the topic "OCTN2"

1

Kwok, Bruce Chia-Wah. "Characterization on OCTN1 and OCTN2 in the human mammary gland." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2001. http://www.collectionscanada.ca/obj/s4/f2/dsk3/ftp04/MQ63172.pdf.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Ott, Klaus. "Untersuchung von Polymorphismen mit möglicher funktioneller Relevanz in den Genen der organischen Kationentransporter OCTN1 und OCTN2 bei chronisch-entzündlichen Darmerkrankungen." Diss., lmu, 2009. http://nbn-resolving.de/urn:nbn:de:bvb:19-97970.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Bonitz, Karina [Verfasser]. "Bedeutung des Carnitin-Transporters OCTN2 für die Entwicklung einer Herzinsuffizienz und eines akuten Myokardinfarktes. / Karina Bonitz." Greifswald : Universitätsbibliothek Greifswald, 2016. http://d-nb.info/1082001880/34.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Grigat, Silke. "Analyse der Substratspezifität des Carnitin-Transporters SLC22A5 (OCTN2) von Mensch, Ratte und Huhn mittels LC-MS/MS /." Köln, 2008. http://opac.nebis.ch/cgi-bin/showAbstract.pl?sys=000253974.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Pagels, Stefanie [Verfasser], Peter [Akademischer Betreuer] Meisel, Gabriele [Akademischer Betreuer] Jedlitschky, Peter [Gutachter] Meisel, and Thomas [Gutachter] Hoffmann. "Untersuchungen zur Assoziation zwischen genetischen Varianten von OCTN1 und OCTN2 und Parodontitis: Ergebnisse aus der Bevölkerungsstudie Study of Health in Pomerania (SHIP-0) / Stefanie Pagels ; Gutachter: Peter Meisel, Thomas Hoffmann ; Peter Meisel, Gabriele Jedlitschky." Greifswald : Universität Greifswald, 2019. http://d-nb.info/1200547764/34.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Rödin, Mattias. "Characterization of the Carnitine Transporter, OCTN2: Functional Impact of Mutations and Its Role in COVID-19 Treatment Related Drug-Drug Interactions." Thesis, Uppsala universitet, Institutionen för farmaceutisk biovetenskap, 2020. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-416447.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

Yamamoto, Priscila Akemi. "Impacto dos polimorfismos genéticos de OCT2 e OCTN1 na disposição cinética da gabapentina em pacientes com dor crônica /." Araraquara, 2018. http://hdl.handle.net/11449/154376.

Full text
Abstract:
Orientador: Natália Valadares de Moraes
Banca: Rosângela Gonçalves Peccinini
Banca: Fabíola Dach
Resumo: A gabapentina (GAB) é um anticonvulsivante indicado para o tratamento de epilepsia e dor crônica. Possui cinética não linear relacionada a saturação do processo de absorção, não é metabolizada e é eliminada principalmente por excreção renal. Estudos sugerem a atividade dos transportadores de cátions orgânicos (OCT2 e OCTN1) na secreção renal da GAB. O objetivo do estudo foi investigar a influência dos polimorfismos genéticos de OCT2 e OCTN1 e outras possíveis covariáveis na disposição cinética da GAB em pacientes tratados com doses múltiplas. Os métodos de cromatografia líquida de alta eficiência com detecção por ultravioleta (CLAE-UV) para determinação da concentração de GAB no plasma e na urina foram desenvolvidos e validados segundo a RDC nº 27/2012 da ANVISA. Foi utilizado como agente derivatizante o 1-flúor-2,4-dinitrobenzeno, e como padrão interno o anlodipino. Os métodos apresentaram linearidade na faixa de 200-14.000 ng/mL de plasma e 2-120 µg/mL de urina. Foram investigados 66 participantes (35 mulheres e 31 homens), com idade média de 54 anos e com dor crônica tratados com GAB por pelo menos 7 dias. Os participantes foram genotipados como GG (n=58) e GT (n=8) para o polimorfismo SLC22A2 c.808G>T e CC (n=31), CT (n= 27) e TT (n=8) para o polimorfismo SLC22A4 c.1507C>T. As concentrações plasmáticas mínima de GAB no estado de equilíbrio variaram de 402,0 a 11.937,9 ng/mL durante tratamento com doses diárias que variaram de 600 a 3.600 mg. A idade e a taxa de filtração ... (Resumo completo, clicar acesso eletrônico abaixo)
Abstract: Gabapentin (GAB) is an anticonvulsant indicated for the treatment of epilepsy and chronic pain. It has nonlinear kinetics due to the saturation of absorption process, is not metabolized and is mainly eliminated by renal excretion. Studies suggest the activity of organic cation transporters (OCT2 and OCTN1) in the renal excretion of GAB. The aim of this study is to investigate the influence of genetic polymorphisms of OCT2 and OCTN1 and other possible covariates on the kinetic disposition of GAB in patients treated with multiple doses. High performance liquid chromatography with ultraviolet detection (HPLC-UV) methods for the determination of GAB plasma and urine concentration were developed and validated according to RDC nº 27/2012 of ANVISA. 1-fluoro-2,4-dinitrobenzene was used as derivatization agent, and amlodipine as internal standard. The methods showed linearity in the range of 20014,000 ng/mL of plasma and 2-120 µg/mL of urine. Sixty-six participants (35 women and 31 men), with mean age of 54 years and with chronic pain treated with GAB for at least 7 days were investigated. They were genotyped as GG (n=58) and GT (n=8) for SLC22A2 c.808G>T polymorphism and as CC (n=31), CT (n=27) and TT (n=8) for SLC22A4 c.1507C>T polymorphism. GAB steady-state minimum plasma concentrations ranged from 402.0 to 11,937.9 ng/mL during the treatment with daily doses ranging from 600 to 3,600 mg. Age and estimated glomerular filtrate rate showed significant correlation with the plasma concentration of GAB/daily dose ratio. Other variables (gender, body weight and body mass index) were not correlated. The estimated glomerular filtration rate and daily dose were found as significant covariates to predict GAB minimum plasma concentration at steady-state, explained 68% of plasma concentration variability. The population pharmacokinetics showed... (Complete abstract click electronic access below)
Mestre
APA, Harvard, Vancouver, ISO, and other styles
8

Friedrich, Anne. "Studies of the expression and characterization of various transport systems at RBE4 cells, an in vitro model of the blood-brain barrier." Doctoral thesis, Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden, 2003. http://nbn-resolving.de/urn:nbn:de:swb:14-1060258657421-84155.

Full text
Abstract:
The purpose of this study was the investigation of several transport systems expressed at the BBB. The identification and functional characterization of such transport systems is essential to provide a basis for strategies to regulate drug disposition into the brain. Immortalized rat brain endothelial cells (RBE4 cells) have been used in this study as an in vitro model of the BBB. The present study has shown that the RBE4 cells are a suitable model of the BBB for transporter studies. These cells do express the amino acid transport systems L and y+, which are known to be present at the BBB. The uptake of L-tryptophan, a neutral amino acid transported by system L, exhibited a half saturation constant (Kt) of 31 µM and a maximal velocity rate (Vmax) of about 1 nmol/mg/min in RBE4 cells. The kinetic constants of the L-arginine uptake, representing system y+ transport activity, into RBE4 cells were determined with a Kt value of about 55 µM and a Vmax of 0.56 nmol/mg/min. Furthermore the expression of two sodium dependent transporters, the 5-HT transporter (SERT) and the organic cation/carnitine transporter OCTN2, was shown at the RBE4 cells. Uptake studies with radiolabeled 5-HT exhibited a saturable, sodium dependent transport at RBE4 cells with a Kt value of about 0.40 µM and a Vmax of about 52 fmol/mg/min. L-carnitine and TEA (tetraethylammonium) are known to be transported by the OCTN2 transporter. The uptake of L-carnitine into RBE4 cells was shown to be sodium dependent and saturable with a Kt value of 54 µM and a maximal velocity of about 3.6 pmol/mg/min. In contrast, the organic cation TEA follows a sodium independent uptake mechanism at RBE4 cells. Also a sodium independent choline uptake into the cells was discovered but the molecular identity remained unknown. This saturable choline transport exhibited a Kt value of about 22 µM and a maximal velocity of about 52 pmol/mg/min.
APA, Harvard, Vancouver, ISO, and other styles
9

Friedrich, Anne. "Studies of the expression and characterization of various transport systems at RBE4 cells, an in vitro model of the blood-brain barrier." Doctoral thesis, Technische Universität Dresden, 2002. https://tud.qucosa.de/id/qucosa%3A23820.

Full text
Abstract:
The purpose of this study was the investigation of several transport systems expressed at the BBB. The identification and functional characterization of such transport systems is essential to provide a basis for strategies to regulate drug disposition into the brain. Immortalized rat brain endothelial cells (RBE4 cells) have been used in this study as an in vitro model of the BBB. The present study has shown that the RBE4 cells are a suitable model of the BBB for transporter studies. These cells do express the amino acid transport systems L and y+, which are known to be present at the BBB. The uptake of L-tryptophan, a neutral amino acid transported by system L, exhibited a half saturation constant (Kt) of 31 µM and a maximal velocity rate (Vmax) of about 1 nmol/mg/min in RBE4 cells. The kinetic constants of the L-arginine uptake, representing system y+ transport activity, into RBE4 cells were determined with a Kt value of about 55 µM and a Vmax of 0.56 nmol/mg/min. Furthermore the expression of two sodium dependent transporters, the 5-HT transporter (SERT) and the organic cation/carnitine transporter OCTN2, was shown at the RBE4 cells. Uptake studies with radiolabeled 5-HT exhibited a saturable, sodium dependent transport at RBE4 cells with a Kt value of about 0.40 µM and a Vmax of about 52 fmol/mg/min. L-carnitine and TEA (tetraethylammonium) are known to be transported by the OCTN2 transporter. The uptake of L-carnitine into RBE4 cells was shown to be sodium dependent and saturable with a Kt value of 54 µM and a maximal velocity of about 3.6 pmol/mg/min. In contrast, the organic cation TEA follows a sodium independent uptake mechanism at RBE4 cells. Also a sodium independent choline uptake into the cells was discovered but the molecular identity remained unknown. This saturable choline transport exhibited a Kt value of about 22 µM and a maximal velocity of about 52 pmol/mg/min.
APA, Harvard, Vancouver, ISO, and other styles
10

Fink, Matthias Alexander [Verfasser], Henry W. S. [Akademischer Betreuer] Schroeder, Sandra [Akademischer Betreuer] Bien-Möller, Henry W. S. [Gutachter] Schroeder, and Veit [Gutachter] Rohde. "Untersuchungen zur prognostischen Relevanz des L-Carnitin-Transporters OCTN2 im Glioblastoma multiforme mit in vitro-Charakterisierung seines zytoprotektiv wirksamen Substrats L-Carnitin in humanen Glioblastomzellen / Matthias Alexander Fink ; Gutachter: Henry W. S. Schroeder, Veit Rohde ; Henry W. S. Schroeder, Sandra Bien-Möller." Greifswald : Universität Greifswald, 2019. http://d-nb.info/119416272X/34.

Full text
APA, Harvard, Vancouver, ISO, and other styles
More sources

Books on the topic "OCTN2"

1

Kwok, Bruce Chia-Wah. Characterization of OCTN1 and OCTN2 in the human mammary gland. Ottawa: National Library of Canada, 2001.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
2

Pendleton, Don. Executioner Oct02. Gold Eagle, 2002.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
3

Deseo Oct02 Ppk12. Harlequin Books, 2002.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
4

Duets Oct02 Ppk6. Harlequin Books, 2002.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
5

Lewis, Carroll. Cooper's Corner Oct02. Simon & Schuster, 2002.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
6

Historical Oct02 Ppk8. Harlequin Books, 2002.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
7

Superromance Oct02 Ppk12. Harlequin Books, 2002.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
8

Continuities Oct02 Ppk6. Simon & Schuster, 2002.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
9

Desire Oct02 Ppk18. Silhouette Books, 2002.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
10

Blaze Oct02 Ppk4. Harlequin Books, 2002.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
More sources

Book chapters on the topic "OCTN2"

1

Slawik, Marc, Felix Beuschlein, Katrina Light, Roger Mulder, Gordon Dent, Mark G. Buckley, Stephen T. Holgate, et al. "OCTN2 Transporter Deficiency." In Encyclopedia of Molecular Mechanisms of Disease, 1511. Berlin, Heidelberg: Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-540-29676-8_7488.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

de Boer, L., L. A. J. Kluijtmans, and E. Morava. "Primary Carnitine (OCTN2) Deficiency Without Neonatal Carnitine Deficiency." In JIMD Reports, 39–40. Berlin, Heidelberg: Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/8904_2012_198.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Longo, Nicola, Cristina Amat Di San Filippo, and Marzia Pasquali. "The OCTN2 carnitine transporter and fatty acid oxidation." In Membrane Transporter Diseases, 161–74. Boston, MA: Springer US, 2003. http://dx.doi.org/10.1007/978-1-4419-9023-5_11.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Stocker, Sophie L., Arian Emami Riedmaier, Matthias Schwab, and Kathleen M. Giacomini. "OCT (SLC22A) and OCTN Family." In Pharmacogenomics of Human Drug Transporters, 171–208. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2013. http://dx.doi.org/10.1002/9781118353240.ch8.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Koepsell, Hermann. "Organic Cation and Zwitterion Transporters (OCTs, OCTNs)." In Drug Transporters, 7–24. Hoboken, NJ: John Wiley & Sons, Inc., 2014. http://dx.doi.org/10.1002/9781118705308.ch2.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Wang, Ying, and Nicole Behler. "In Vitro Characterization of Renal Transporters OAT1, OAT3, and OCT2." In Methods in Pharmacology and Toxicology, 417–29. Totowa, NJ: Humana Press, 2013. http://dx.doi.org/10.1007/978-1-62703-742-6_24.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

Enna, S. J., and David B. Bylund. "OCTN Organic Cation-Sodium Transporters." In xPharm: The Comprehensive Pharmacology Reference, 1. Elsevier, 2007. http://dx.doi.org/10.1016/b978-008055232-3.63803-6.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Koepsell, Hermann. "General Overview of Organic Cation Transporters in Brain." In Handbook of Experimental Pharmacology. Berlin, Heidelberg: Springer Berlin Heidelberg, 2021. http://dx.doi.org/10.1007/164_2021_449.

Full text
Abstract:
AbstractInhibitors of Na+/Cl− dependent high affinity transporters for norepinephrine (NE), serotonin (5-HT), and/or dopamine (DA) represent frequently used drugs for treatment of psychological disorders such as depression, anxiety, obsessive-compulsive disorder, attention deficit hyperactivity disorder, and addiction. These transporters remove NE, 5-HT, and/or DA after neuronal excitation from the interstitial space close to the synapses. Thereby they terminate transmission and modulate neuronal behavioral circuits. Therapeutic failure and undesired central nervous system side effects of these drugs have been partially assigned to neurotransmitter removal by low affinity transport. Cloning and functional characterization of the polyspecific organic cation transporters OCT1 (SLC22A1), OCT2 (SLC22A2), OCT3 (SLC22A3) and the plasma membrane monoamine transporter PMAT (SLC29A4) revealed that every single transporter mediates low affinity uptake of NE, 5-HT, and DA. Whereas the organic transporters are all located in the blood brain barrier, OCT2, OCT3, and PMAT are expressed in neurons or in neurons and astrocytes within brain areas that are involved in behavioral regulation. Areas of expression include the dorsal raphe, medullary motoric nuclei, hypothalamic nuclei, and/or the nucleus accumbens. Current knowledge of the transport of monoamine neurotransmitters by the organic cation transporters, their interactions with psychotropic drugs, and their locations in the brain is reported in detail. In addition, animal experiments including behavior tests in wildtype and knockout animals are reported in which the impact of OCT2, OCT3, and/or PMAT on regulation of salt intake, depression, mood control, locomotion, and/or stress effect on addiction is suggested.
APA, Harvard, Vancouver, ISO, and other styles
9

Gorboulev, Valentin, and Hermann Koepsell. "OCTN-2, Organic Cation-Sodium Transporter 2." In xPharm: The Comprehensive Pharmacology Reference, 1–3. Elsevier, 2007. http://dx.doi.org/10.1016/b978-008055232-3.60481-7.

Full text
APA, Harvard, Vancouver, ISO, and other styles
10

Betterton, Robert D., Thomas P. Davis, and Patrick T. Ronaldson. "Organic Cation Transporter (OCT/OCTN) Expression at Brain Barrier Sites: Focus on CNS Drug Delivery." In Handbook of Experimental Pharmacology. Berlin, Heidelberg: Springer Berlin Heidelberg, 2021. http://dx.doi.org/10.1007/164_2021_448.

Full text
APA, Harvard, Vancouver, ISO, and other styles

Conference papers on the topic "OCTN2"

1

Jong, Nancy N., Takeo Nakanishi, Johnson J. Liu, Ikumi Tamai, and Mark J. McKeage. "Abstract 4391: OCTN1- and OCTN2-mediated uptake of oxaliplatin in rat dorsal root ganglion neurons and HEK293 cells over-expressing OCTN1 or OCTN2." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-4391.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Hu, Chaoxin, Cynthia S. Lancaster, Ryan M. Franke, Kelly K. Filipski, and Alex Sparreboom. "Abstract 3529: Cisplatin-induced downregulation of OCTN2 affects carnitine (vitamin BT) wasting." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-3529.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Pabla, Navjotsingh, Jason A. Sprowl, Su Sien Ong, Alice A. Gibson, Guoqing Du, Wenwei Lin, Shuiying Hu, Lie Li, Taosheng Chen, and Alex Sparreboom. "Abstract 4415: Tyrosine phosphorylation is essential for OCT2 function and a target of inhibition by TKIs." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-4415.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Lancaster, Cynthia S., Ryan M. Franke, Kelly K. Filipski, Ashley M. Kosloske, and Alex Sparreboom. "Abstract 1522: Identification of pifithrin-α as a potent inhibitor of OCT2-mediated transport of cisplatin." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-1522.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Franke, Ryan M., Ashley M. Kosloske, Kelly K. Filipski, and Alex Sparreboom. "Abstract 1521: Influence of Oct1/Oct2-deficiency on cisplatin-induced changes in urinary N-acetyl-β-D-glucosaminidase." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-1521.

Full text
APA, Harvard, Vancouver, ISO, and other styles
You might also be interested in the extended bibliographies on the topic 'OCTN2' for particular source types:
Journal articles Dissertations / Theses Books
We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!

To the bibliography