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1 ancer for the carnitine transporter SLC22A5 (OCTN2).
2 ort to 57.8 +/- 7.4 mM (p<0.01 versus normal OCTN2).
3 nsport to approximately 50% of the reference OCTN2.
4 TN1, which does not transport carnitine, and OCTN2.
5 nsfer in the sodium-dependent co-transporter OCTN2.
6 he Na+-dependent organic cation transporter, OCTN2.
7 pendent carnitine/organic cation transporter OCTN2.
8 with the substitution of residues 341-454 of OCTN2.
9 his structural feature did not interact with OCTN2.
10 the sodium-dependent carnitine cotransporter OCTN2.
11 and the organic cation transport function of OCTN2.
12 e similar for the P478L mutant and wild type OCTN2.
13                  These studies revealed that OCTN2, a gene recently shown to play a role in carnitine
14            Substitution of the C terminus of OCTN2 (amino acid residues 342-557) with the correspondi
15 ene for this condition maps to 5q31.2-32 and OCTN2, an organic cation/carnitine transporter, also map
16 transport of carnitine compared to wild-type OCTN2, and 37 variants (25%) severely reduced function t
17  that although loss-of-function mutations in OCTN2 are likely to be rare, common variants of OCTN2 fo
18  in the organic cation/carnitine transporter OCTN2 are responsible for primary carnitine deficiency.
19 influence on the two transport activities of OCTN2 as did the P478L mutation.
20 bits much higher concentrative capacity than OCTN2 because of its energization by transmembrane gradi
21 reviously unappreciated relationship between OCTN2, carnitine, and hepatic triglyceride production is
22  encoding the membrane carnitine transporter OCTN2, cause the rare metabolic disorder Carnitine Trans
23  nonconserved between OCTN1 and OCTN2 in the OCTN2 cDNA indicated that the R341A, L409W, L424Y, and T
24 ansfection of patient's fibroblasts with the OCTN2 cDNA partially restored carnitine transport.
25                 Studies with human OCTN2/rat OCTN2 chimeric transporters indicated that the carnitine
26 ues, we screened for genetic variants in the OCTN2 coding region by direct sequencing of the exons an
27 etarians, possibly because of reduced muscle OCTN2 content.
28 ransfer and identifies a novel domain of the OCTN2 cotransporter involved in transmembrane sodium/sol
29 e, and cefluprenam, which were recognized by OCTN2, did not interact with PEPT1 and PEPT2.
30 N2 are likely to be rare, common variants of OCTN2 found in healthy populations may contribute to var
31 specific variant effect prediction model for OCTN2 function.
32                            Sequencing of the OCTN2 gene revealed different mutations in two unrelated
33         Confocal microscopy studies using an OCTN2-GFP fusion protein showed that Phe17Leu had distin
34  two missense mutations, L352R and P478L, in OCTN2 have been identified as the cause for primary carn
35 of the exons and flanking intronic region of OCTN2 in a large sample (n = 276) of ethnically diverse
36           Here we test the causative role of OCTN2 in primary carnitine deficiency by searching for m
37 n of residues nonconserved between OCTN1 and OCTN2 in the OCTN2 cDNA indicated that the R341A, L409W,
38                                              OCTN2 is an organic cation/carnitine transporter that is
39        The interaction of cephaloridine with OCTN2 is competitive with respect to carnitine.
40                                     Although OCTN2 is fairly well studied in its relationship with SC
41            Novel organic cation transporter (OCTN2) is an organic cation/carnitine transporter, and t
42 scent protein (GFP)-tagged variants impaired OCTN2 localization to the plasma membrane of human embry
43 r understanding of the mechanisms leading to OCTN2 loss-of-function (LOF) and creating a protein-spec
44 epime, and cefluprenam were found to inhibit OCTN2-mediated carnitine transport.
45            Furthermore, the Na(+)-dependent, OCTN2-mediated cellular uptake of cephaloridine could be
46 e transporter [organic cation transporter 2 (OCTN2)] messenger RNA and protein expressions were 16% (
47 ese mutations decreased the levels of mature OCTN2 mRNA and resulted in nonfunctional transporters, c
48 d increase in carnitine transporter protein (OCTN2) mRNA expression (P<0.05).
49                   This transporter, known as OCTN2 (novel organic cation transporter 2), is expressed
50  found eight amino acid sequence variants of OCTN2, of which three (Phe17Leu, Leu144Phe, and Pro549Se
51 rier frequency of disease-causing alleles of OCTN2, or of more common functional polymorphisms in thi
52 ed functional differences from the reference OCTN2 (Phe17Leu, Tyr449Asp, Val481Phe; p < 0.05).
53                      These studies show that OCTN2 plays a crucial role in the pharmacokinetics and t
54                           Studies with human OCTN2/rat OCTN2 chimeric transporters indicated that the
55 itine transport by the introduction of these OCTN2 residues in the OCTN1 portion of CHIM-9.
56 essive disease resulting from defects in the OCTN2 (SLC22A5) gene, which encodes the high-affinity pl
57 n the same gene and one in an adjacent gene, OCTN2 (SLC22A5), was associated with CD.
58 mia, which is associated with an increase in OCTN2 transcription.
59 tudies indicate that multiple domains of the OCTN2 transporter are required for carnitine transport a
60                       Confocal microscopy of OCTN2 transporters tagged with green fluorescent protein
61 tion of several beta-lactam antibiotics with OCTN2 using human cell lines that express the transporte
62 in this study we generated a rich dataset of OCTN2 variant function and localization, revealed import
63 ed upon machine learning-based prediction of OCTN2 variant function to aid in variant interpretation
64 cterize the largest set to date (n = 150) of OCTN2 variants identified in diverse ancestral populatio
65 e interaction of cefoselis and cefepime with OCTN2 was largely Na(+)-independent.
66        The interaction of cephaloridine with OCTN2 was Na(+)-dependent, whereas the interaction of ce
67 ctam antibiotics that were not recognized by OCTN2 were good substrates for the H(+)-coupled peptide
68 r (CHIM-9) in which only residues 341-454 of OCTN2 were substituted by OCTN1 had markedly reduced car
69 ention of Phe17Leu, in contrast to reference OCTN2, which localized specifically to the plasma membra
70 rogressive substitution of the N terminus of OCTN2 with OCTN1 resulted in a decrease in carnitine tra
71  subcellular localization from the reference OCTN2, with diffuse cytoplasmic retention of Phe17Leu, i