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4 edition of Characterization of OCTN1 and OCTN2 in the human mammary gland found in the catalog.

Characterization of OCTN1 and OCTN2 in the human mammary gland

Bruce Chia-Wah Kwok

Characterization of OCTN1 and OCTN2 in the human mammary gland

by Bruce Chia-Wah Kwok

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  • 35 Currently reading

Published by National Library of Canada in Ottawa .
Written in English


Edition Notes

Thesis (M.Sc.) -- University of Toronto, 2001.

SeriesCanadian theses = -- Theses canadiennes
The Physical Object
FormatMicroform
Pagination2 microfiches : negative.
ID Numbers
Open LibraryOL20835803M
ISBN 100612631729
OCLC/WorldCa52623265

Since solute carrier (SLC) and ATP-binding cassette (ABC) transporters play pivotal roles in the transport of both nutrients and drugs into breast milk, drug-nutrient transport interactions at the lactating mammary gland are possible. Our purpose was to characterize lactation stage-dependent changes in transporter expression in rat mammary gland and isolated mammary epithelial organoids (MEO Cited by: The translation ※ of basic science advances to tangible benefits in clinical practice remains a fundamental goal. OCTN2 is a physiologically important, high affinity sodium carnitine cotransporter and choline transporter-like protein CTL1 in human lung adenocarcinoma cell lines in e is an essential nutrient for cell survival and proliferation, however without a marked release of.

  (b) Multiple sequence alignment of OCTN2 with transmembrane domains from rat UST2r, human OCTN1, human OCT1, human OCT2, rat OCT1A, rat OCT2, rat OCT3, mouse OCT2, rabbit OCT1, pig OCT2 and fruit fly ORCT. Pro is shown in by: You can write a book review and share your experiences. Other readers will always be interested in your opinion of the books you've read. Whether you've loved the book or not, if you give your honest and detailed thoughts then people will find new books that are right for them.

Primary Carnitine Deficiency and SLC22A5. Initial release: August Last update: January Primary carnitine deficiency or carnitine uptake defect (CUD; OMIM#) is an autosomal recessive disorder of fatty acid oxidation due to defective OCTN2 (organic cation transporter novel 2 carnitine transporters). OCTN2 is encoded by the fifth member of the solute carrier family 22 of organic. SLC22A5 is a membrane transport protein associated with primary carnitine deficiency. This protein is involved in the active cellular uptake of carnitine. It acts a symporter, moving sodium ions and other organic cations across the membrane along with s: SLC22A5, CDSP, OCTN2, solute carrier .


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Characterization of OCTN1 and OCTN2 in the human mammary gland by Bruce Chia-Wah Kwok Download PDF EPUB FB2

In addition, we report the first demonstration of the subcellular localization of an in-frame fusion GFP-human high-affinity carnitine transporter OCTN2 protein in the plasma membrane by confocal.

OCTN1 is widely expressed in human tissues []. It also appears to have higher mRNA expression than OCTN2 in many tissues. It is located on the brush-border membrane (urine side) of proximal tubule cells and on the luminal (air) side of airway epithelial cells [4, 5]. Keywords: MATE1, P-gp, OCTN1, OCTN2, Immunohistochemistry, COPD, Human lung tissue, Drug transporters, Uptake, Efflux Background Inhaled administration is the main treatment route in chronic obstructive pulmonary disease (COPD), enabling high local drug concentrations, lower systemic exposure and consequently, less risk of side effects.

The Cited by: 8. 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 pl Cited by: 7. Inwe cloned novel human transporter OCTN1, which is an organic cation transporter. 3 The OCTN1 gene is located on chromosome 5q31 and encodes amino acid residues with 12 predicted transmembrane domains (TMDs).

3 Human OCTN1 is expressed ubiquitously, with strong expression in kidney, trachea, bone marrow, and fetal liver. 3 It Cited by: OCTN2 protein is detected in the alveolar epithelia of mammary gland, apparently at a sufficient level to supply carnitine to milk.

In mice, Octn1, 2 and 3 are all expressed in mammary gland. Their intracellular localization in mammary gland is not known; however, Octn1 is expressed mainly in blood vessel endothelium and secretory alveolar apical membrane, Octn2 in secretory alveoli, and Octn3 in.

A total of 15 case–control studies, containing 4, cases/5, controls for OCTN1 and 4, cases/5, controls for OCTN2 were included.

Overall, significant associations were found between OCTN1/2 polymorphisms and susceptibility of Crohn's disease for all genetic by: In mice, three isoforms, Octn1 (Slc22a4), Octn2 (Slc22a5) and Octn3 (Slc22a21), have been identified, while in humans there are two isoforms, OCTN1 (SLC22A4) and OCTN2 (SLC22A5) 2 - 4.

In humans, OCTN1 was discovered inand then OCTN2, the sodium ion‐dependent carnitine transporter, was founded in 2, by:   In particular, we hypothesized that the OCTN2 functional variants that showed decreased promoter activity could be associated with a more severe clinical course of CD, as well-known OCTN1 Cited by: 3.

OCTN2 also operates as a polyspecific Na+-independent organic cation transporter, and can transport substrates in both directions across the plasma membrane. OCTN2 was first cloned from human kidney and identified as the transporter responsible for systemic carnitine deficiency [3].

OCTN2 has a high degree of sequence homology with OCTN1 [4]. OCTN2, expressed also in the heart (see the subsection “OCTN2”), is inhibited by many cardiovascular drugs commonly used in human therapy, such as verapamil, spironolactone, and mildronate, for which a competitive mode of inhibition was observed.

92 OCTN2 and OCTN1 have been described to be responsible for oxaliplatin transport in embryonic Cited by:   To further evaluate their potential to impact on inhaled drug disposition, the localization of MATE1, P-gp, OCTN1 and OCTN2 were investigated in human lung.

METHODS: Transporter proteins were analysed by immunohistochemistry in lung tissue from Cited by: 8. OCTN1 Is a High-Affinity Carrier of Nucleoside Analogues Christina D.

Drenberg1, Alice A. Gibson1, Stanley B. Pounds2, The human embryonic kidney cell line HEK (Invitrogen), HeLa, and Chinese hamster ovary (CHO; ATCC) were obtained OAT2, OAT3, OCTN2, OCT1, OCT2, and OCT3 (Supplementary Fig.

S1D). Quantitative RT Cited by:   The full-length OCTN1, OCTN2, and OCTN3 cDNAs appeared to encode polypeptides of, and amino acids and h 86, and 78% similarities with human OCTN2 (9), respectively. The similarities with human OCTN1 w 73, and 67%, respectively (10).

OCTN1, OCTN2 and OCT6 are all cation and carnitine transporters. OCTN1 transport activity can be affected by both sodium and proton gradients, depending on the substrate transported.

OCTN2 also mediates both sodium-dependent and sodium-independent uptake, depending on the substrate (Koepsell et al., ). In addition to carnitine, TEA is also a substrate of both transporters and is frequently Cited by:   Human cells possess three high affinity (OCTN1/SLC22A4, OCTN2/SLC22A5 and hCT2/SLC22A16), as well as three low affinity (OCT1/SLC22A1, OCT2/SLC22A2 and OCT3/SLC22A3) L-carnitine transporters Cited by:   To evaluate the selectivity of OCTN1 for the transport of nucleoside analogues, we initially performed pharmacologic profiling of the NCI60 cell panel, which comprises 60 different human tumor cell lines, representing leukemia, melanoma, and cancers of the lung, colon, brain, ovary, breast, prostate, and by: The human gene coding SLC22A5 was cloned in [22,23] and the protein was named OCTN2 because of its similarity (%) to OCTN1/SLC22A4.

Overexpressed OCTN1 was shown to transport carnitine in a Na + -dependent manner [ 17, 33 ]; however, its activity was much lower in comparison with OCTN2 and OCTN3 [ 17 ].Author: Barbara Juraszek, Katarzyna A.

Nałęcz. For example, CYP1A1, 1B1, 2C, 2D6, 2E1 and 3A4/5 mRNA and/or protein are expressed in the mammary gland from human samples [60,61,62]. There, they may contribute to the clearance and bioactivation of their substrates, including carcinogens such as 7,dimethylbenz(a)anthracene [ 63 ].Cited by: 1.

Several transporters, of which pregabalin is a substrate (including OCT2 and OCTN1), have been identified in human mammary gland epithelia. The primary focus of our research program is the biochemical and molecular characterization of the organic cation/carnitine transporter family OCTN1, OCTN2 and OCTN3 and to increase understanding of their regulation and roles in maintaining intracellular carnitine homeostasis in brain, heart, muscle, testis and developing mammary gland.For the determination of mRNA expression levels of PPARα, cytochrome P A1 (CYP4A1), acyl–coenzyme A oxidase (ACO), liver-type carnitine palmitoyltransferase I (L-CPT I), fatty acid translocase (FAT/CD36), fatty acid transport protein (FATP), plasma membrane fatty acid binding protein (FABPpm), OCTN1, OCTN2, TMABA-DH, TMLD, and BBD, total RNA was isolated from rat livers and rat mammary Cited by: Glucose, fatty acids, and L-carnitine are important substrates that support mammary epithelial cell metabolism, biosynthetic capacity, and milk yield and composition.

Our study investigated the effects of LPS-induced inflammation on the expression of several glucose, fatty acid, and L-carnitine transporters in the lactating rat mammary gland at different lactation by: