Functional analysis of [methyl-3H]choline uptake in glioblastoma cells: Influence of anti-cancer and central nervous system drugs

Taguchi, C.; Inazu, Masato; Saiki, Iwao; Yara, Miki; Hara, Naomi; Yamanaka, T.; Uchino, Haruto

doi:10.1016/j.bcp.2014.01.033

Cited by 26 publications

(31 citation statements)

References 37 publications

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“…Similar to the high-affinity choline transporter CHT1, CTL1 is selectively inhibited by the choline analogue hemicholinium-3 (CH-3), yet with a much lower sensitivity. In recent years, further choline uptake studies confirmed the expression and choline transporter function of CTL1/SLC44A1 in human lung alveolar cells, 28 mouse bone marrow-derived macrophages, 42 rat renal tubule epithelial cells, 30 human keratinocytes, 31 human brain microvascular endothelial cells, 14 rheumatoid arthritis synovial fibroblasts, 40 mouse muscle and liver cell lines, 32,33 and numerous cancer cell lines 26,28,[34][35][36][37][38][39]41 as summarized in Table 1.…”

Section: Slc44a Proteinsmentioning

confidence: 78%

Choline transport for phospholipid synthesis: An emerging role of choline transporter-like protein 1

Hedtke

Bakovic

2019

Exp Biol Med (Maywood)

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This review provides a summary of recent discoveries in choline transport and the proteins mediating it with a specific focus on the choline transporter-like proteins (CTL)/solute carriers 44 A (SLC44A) and their role in phospholipid metabolism. Since its initial cloning, particularly, the CTL1/SLC44A1 transporter has been investigated further and its ubiquitous expression characterized in various cells and tissues of mouse, rat, and human origin. We describe the role of this choline transporter both in the plasma membrane and in the mitochondria and summarize novel aspects of choline transport regulation in the muscle, nervous system, and cancer. Impact statement This review will provide a summary of recent advances in choline transport research and highlight important novel areas of focus in the field.

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Section: Slc44a Proteinsmentioning

confidence: 78%

Choline transport for phospholipid synthesis: An emerging role of choline transporter-like protein 1

Hedtke

Bakovic

2019

Exp Biol Med (Maywood)

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“…In addition, CTL2‐expressing Xenopus oocytes take up choline significantly more than the control oocytes, indicating that CTL2 is a functional choline transporter . Choline transport by CTL2 in the human glioblastoma cell line can be pH‐dependent . Recently, the knockdown of CTL5 significantly decreased choline transport in human lung cancer H82 cells, indicating the role of CTL5 in choline transport ; however, to our knowledge, there is no report about the transport characteristics of CTL5 for choline.…”

Section: Discussionmentioning

confidence: 95%

Membrane transport mechanisms of choline in human intestinal epithelial LS180 cells

Horie

Ishida

Watanabe

et al. 2014

Biopharm & Drug Disp

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The aim of the present study was to investigate the membrane transport mechanisms of choline using human intestinal epithelial LS180 cells. The mRNA of choline transporter-like proteins (CTLs) was expressed significantly in LS180 cells, and the rank order was CTL1 > CTL4 > CTL3 > CTL2 > CTL5. In contrast, the mRNA expression of other choline transporters, organic cation transporter (OCT) 1, OCT2 and high-affinity choline transporter 1 (CHT1), was considerably lower in LS180 cells. Five mm unlabelled choline, hemicolinium-3 and guanidine, but not tetraethylammonium, inhibited the cellular uptake of 100 µm choline in LS180 cells. The uptake of choline into LS180 cells was virtually Na(+)-independent. The uptake of choline was significantly decreased by acidification of the extracellular pH; however, it was not increased by alkalization of the extracellular pH. In addition, both acidification and alkalization of intracellular pH decreased the uptake of choline, indicating that the choline uptake in LS180 cells is not stimulated by the outward H(+) gradient. On the other hand, the uptake of choline was decreased by membrane depolarization along with increasing extracellular K(+) concentration. In addition, the Na(+)-independent uptake of choline was saturable, and the Km value was estimated to be 108 µm. These findings suggest that the uptake of choline into LS180 cells is membrane potential-dependent, but not outward H(+) gradient-dependent.

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“…The estimated size of human CTL1 based on the deduced amino acid sequences was 73.3 kDa for deglycosylated CTL1, which is very similar to the size of the JEG-3 cells described here. For CTL2, a major band of 50 kDa was similar to bands of 60 kDa observed in the human glioblastoma cell line A-172 and U-251MG cells [25]. Furthermore, we achieved the direct visualization of CTL1 and CTL2 proteins expressed in plasma membrane by immunocytochemical staining using CTL1 polyclonal antibody and CTL2 antiserum.…”

Section: ) [ 3 H]mentioning

confidence: 89%

Molecular and functional characterization of choline transporter in the human trophoblastic cell line JEG-3 cells

et al. 2015

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Functional analysis of [methyl-3H]choline uptake in glioblastoma cells: Influence of anti-cancer and central nervous system drugs

Cited by 26 publications

References 37 publications

Choline transport for phospholipid synthesis: An emerging role of choline transporter-like protein 1

Choline transport for phospholipid synthesis: An emerging role of choline transporter-like protein 1

Membrane transport mechanisms of choline in human intestinal epithelial LS180 cells

Molecular and functional characterization of choline transporter in the human trophoblastic cell line JEG-3 cells

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