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Journal articles on the topic 'Cell uptake'

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Published: 4 June 2021
Last updated: 10 March 2023

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1

Taher, Muhammad, Fadzilah Adibah Abdul Majid, and Mohamad Roji Sarmidi. "The Effect of Cinnamtannin B1 on Cell Proliferation and Glucose Uptake of 3T3-L1 Cells." Natural Product Communications 2, no. 1 (January 2007): 1934578X0700200. http://dx.doi.org/10.1177/1934578x0700200112.

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The effects of cinnamtannin B1 on cell proliferation and glucose uptake of 3T3-L1 cells were examined. Cinnamtannin B1 promoted cell proliferation of 3T3-L1 adipocytes at a concentration range between 0.11-0.17 mM. The effect of cinnamtannin B1 on cellular 2-deoxy-D-[1-3H] glucose uptake in differentiated 3T3-L1 adipocytes, following treatment with a 0.11 mM concentration of cinnamtannin B1 for 15, 30 and 60 minutes, was an increase in the glucose uptake from a basal value to 702.0, 1111.0 and 2226.0 cpm, respectively (p<0.005). The comparable glucose uptakes with insulin treatment were 660.0, 1039.0 and 2135.0 cpm, respectively. Wortmannin and cytochalasin B were found to inhibit cinnamtannin B1-stimulated glucose uptake, but sodium orthovanadate increased the glucose uptake.
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2

Xu, Hengyi, Zoraida P. Aguilar, Hua Wei, and Andrew Wang. "Cell Uptake of Nanoparticles." ECS Transactions 25, no. 31 (December 17, 2019): 9–17. http://dx.doi.org/10.1149/1.3327198.

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3

Yanagawa, N., and O. D. Jo. "Intracellular acidification inhibits opposum kidney cell phosphate uptake." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 272, no. 6 (June 1, 1997): R1904—R1911. http://dx.doi.org/10.1152/ajpregu.1997.272.6.r1904.

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The aim of our study is to examine the effect of intracellular pH (pHi) on inorganic phosphate (Pi) uptake by a proximal tubular cell line, the opposum kidney (OK) cells. The OK cell pHi (7.48 +/- 0.02; n = 12) was altered to levels between 6.5 and 8.5 by the high-K+ nigericin method, and cell uptakes were measured at 7.5 extracellular pH. It was found that pHi acidification suppressed Pi uptake with a decrease in maximal reaction rate, whereas alkalinization had no significant effect. Other Na(+)-dependent transport systems for glucose and amino acid were not affected by these pHi changes. The inhibition of cell Pi uptake by pHi acidification was not prevented by protein synthesis inhibitors (actinomycin D or cycloheximide) or by Na+/H+ exchange inhibitor [5-(N-ethyl-N-isopropyl)-amiloride]. pHi acidification caused a significant decrease in cellular adenosine 3',5'-cyclic monophosphate (cAMP) content, and cAMP-dependent protein kinase inhibitor (H-89) also did not prevent inhibition of cell Pi uptake by pHi acidification. However, pHi acidification stimulated protein kinase C (PKC) activity and inhibition of PKC by PKC inhibitors (bisindolylmaleimide, calphostin C, or staurosporine) or prolonged exposure to phorbol ester abrogated the inhibitory effect of pHi acidification on cell Pi uptake. In summary, these studies showed that pHi acidification inhibits Pi uptake in OK cells, probably through PKC activation. These effects of pHi acidification may thus contribute to increase acid excretion in systemic acidosis.
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4

Fujita, Yosuke, Tomoki Nagakura, Hiroyuki Uchino, Masato Inazu, and Tsuyoshi Yamanaka. "Functional Expression of Choline Transporters in Human Neural Stem Cells and Its Link to Cell Proliferation, Cell Viability, and Neurite Outgrowth." Cells 10, no. 2 (February 20, 2021): 453. http://dx.doi.org/10.3390/cells10020453.

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Choline and choline metabolites are essential for all cellular functions. They have also been reported to be crucial for neural development. In this work, we studied the functional characteristics of the choline uptake system in human neural stem cells (hNSCs). Additionally, we investigated the effect of extracellular choline uptake inhibition on the cellular activities in hNSCs. We found that the mRNAs and proteins of choline transporter-like protein 1 (CTL1) and CTL2 were expressed at high levels. Immunostaining showed that CTL1 and CTL2 were localized in the cell membrane and partly in the mitochondria, respectively. The uptake of extracellular choline was saturable and performed by a single uptake mechanism, which was Na+-independent and pH-dependent. We conclude that CTL1 is responsible for extracellular choline uptake, and CTL2 may uptake choline in the mitochondria and be involved in DNA methylation via choline oxidation. Extracellular choline uptake inhibition caused intracellular choline deficiency in hNSCs, which suppressed cell proliferation, cell viability, and neurite outgrowth. Our findings contribute to the understanding of the role of choline in neural development as well as the pathogenesis of various neurological diseases caused by choline deficiency or choline uptake impairment.
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5

Chen, Ran, Tatsiana A. Ratnikova, Matthew B. Stone, Sijie Lin, Mercy Lard, George Huang, JoAn S. Hudson, and Pu Chun Ke. "Cell uptake: Small 5/2010." Small 6, no. 5 (March 8, 2010): NA. http://dx.doi.org/10.1002/smll.201090015.

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6

Emoto, Akiko, Fumihiko Ushigome, Noriko Koyabu, Hiroshi Kajiya, Koji Okabe, Shoji Satoh, Kiyomi Tsukimori, Hitoo Nakano, Hisakazu Ohtani, and Yasufumi Sawada. "H+-linked transport of salicylic acid, an NSAID, in the human trophoblast cell line BeWo." American Journal of Physiology-Cell Physiology 282, no. 5 (May 1, 2002): C1064—C1075. http://dx.doi.org/10.1152/ajpcell.00179.2001.

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We investigated the transport of salicylic acid and l-lactic acid across the placenta using the human trophoblast cell line BeWo. We performed uptake experiments and measured the change in intracellular pH (pHi). The uptakes of [14C]salicylic acid andl-[14C]lactic acid were temperature- and extracellular pH-dependent and saturable at higher concentrations. Both uptakes were also reduced by FCCP, nigericin, and NaN3. Various nonsteroidal anti-inflammatory drugs (NSAIDs) strongly inhibited the uptake of l-[14C]lactic acid. Salicylic acid and ibuprofen noncompetitively inhibited the uptake ofl-[14C]lactic acid. α-Cyano-4-hydroxycinnamate (CHC), a monocarboxylate transporter inhibitor, suppressed the uptake ofl-[14C]lactic acid but not that of [14C]salicylic acid. CHC also suppressed the decrease of pHi induced by l-lactic acid but had little effect on that induced by salicylic acid or diclofenac. These results suggest that NSAIDs are potent inhibitors of lactate transporters, although they are transported mainly by a transport system distinct from that for l-lactic acid.
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7

Delpire, E., and S. R. Gullans. "Cell volume and K+ transport during differentiation of mouse erythroleukemia cells." American Journal of Physiology-Cell Physiology 266, no. 2 (February 1, 1994): C515—C523. http://dx.doi.org/10.1152/ajpcell.1994.266.2.c515.

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In the present study, we evaluated the changes in cell volume, water content, and K+ transport in mouse erythroleukemia (MEL) cells during the transition from proerythroblast to young reticulocyte. When MEL cells were exposed to 1.8% dimethyl sulfoxide (DMSO) for a maximum of 7 days, they synthesized hemoglobin and reduced their volume by 66% while maintaining their water content. The total protein content decreased by 50%. We therefore concluded that the volume reduction was due to a loss of cellular material, water, and osmolytes. To evaluate the changes in pump and leak pathways, we performed 86Rb uptakes in the presence or absence of selected inhibitors. In undifferentiated cells, the uptake was mainly represented by the Na-K-2Cl cotransport (51%) and by the Na(+)-K+ pump (34%). A small portion of the uptake was mediated by barium- and quinidine-sensitive K+ channels (8%) and by the furosemide-sensitive K-Cl cotransporter (5%). After 4 days in DMSO, the 86Rb uptake was reduced by 57%, mainly due to a substantial (90%) decrease in Na-K-2Cl cotransport activity. The Na(+)-independent K-Cl cotransport activity also dramatically decreased by a factor of 10. In contrast, the Na(+)-K+ pump activity did not change after 4 days in DMSO. These results demonstrate a marked reduction in the activities of inorganic ion cotransport systems as red blood cells differentiate to reticulocytes. Our study also demonstrates that a strong correlation exists between cell volume reduction and a decrease in the main inward leak pathway for K+: the Na-K-2Cl cotransporter.
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8

CPK, Cheung. "T Cells, Endothelial Cell, Metabolism; A Therapeutic Target in Chronic Inflammation." Open Access Journal of Microbiology & Biotechnology 5, no. 2 (2020): 1–6. http://dx.doi.org/10.23880/oajmb-16000163.

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The role of metabolic reprogramming in the coordination of the immune response has gained increasing consideration in recent years. Indeed, it has become clear that changes in the metabolic status of immune cells can alter their functional properties. During inflammation, stimulated immune cells need to generate sufficient energy and biomolecules to support growth, proliferation and effector functions, including migration, cytotoxicity and production of cytokines. Thus, immune cells switch from oxidative phosphorylation to aerobic glycolysis, increasing their glucose uptake. A similar metabolic reprogramming has been described in endothelial cells which have the ability to interact with and modulate the function of immune cells and vice versa. Nonetheless, this complicated interplay between local environment, endothelial and immune cells metabolism, and immune functions remains incompletely understood. We analyze the metabolic reprogramming of endothelial and T cells during inflammation and we highlight some key components of this metabolic switch that can lead to the development of new therapeutics in chronic inflammatory disease.
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9

Becker, Christiane, Michael Hodenius, Gitta Blendinger, Antonio Sechi, Thomas Hieronymus, Detlef Müller-Schulte, Thomas Schmitz-Rode, and Martin Zenke. "Uptake of magnetic nanoparticles into cells for cell tracking." Journal of Magnetism and Magnetic Materials 311, no. 1 (April 2007): 234–37. http://dx.doi.org/10.1016/j.jmmm.2006.11.203.

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10

Tokita, N., and M. R. Raju. "Cell cycle-dependent adriamycin uptake in Chinese hamster cells." European Journal of Cancer and Clinical Oncology 21, no. 2 (February 1985): 243–47. http://dx.doi.org/10.1016/0277-5379(85)90179-8.

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11

Nakae, Susumu, Keisuke Oboki, and Hirohisa Saito. "Mast cells and T-cell expansion." Blood 111, no. 5 (March 1, 2008): 2497–98. http://dx.doi.org/10.1182/blood-2007-12-128330.

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IgE/antigen-FcϵRI crosslinking promotes antigen internalization and apoptosis in mouse mast cells. Dendritic cells uptake the apoptotic mast cells carrying internalized antigens, and thus can efficiently present the antigens to memory T cells.
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12

Eiríksdottir, E., H. Myrberg, M. Hansen, and U. Langel. "Cellular Uptake of Cell-Penetrating Peptides." Drug Design Reviews - Online 1, no. 2 (April 1, 2004): 161–73. http://dx.doi.org/10.2174/1567269043480636.

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13

Levin, P., T. Bistritzer, L. Hanukoglu, S. Max, and L. Roeder. "ACTH1-24Stimulates Muscle Cell Glucose Uptake." Hormone and Metabolic Research 22, no. 12 (December 1990): 608–11. http://dx.doi.org/10.1055/s-2007-1004984.

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14

Pistocchi, Rossella, Nello Bagni, and José A. Creus. "Polyamine Uptake in Carrot Cell Cultures." Plant Physiology 84, no. 2 (June 1, 1987): 374–80. http://dx.doi.org/10.1104/pp.84.2.374.

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15

Morita, Aryan, Felipe P. Perona Martinez, Mayeul Chipaux, Nicolas Jamot, Simon R. Hemelaar, Kiran J. van der Laan, and Romana Schirhagl. "Cell Uptake of Lipid‐Coated Diamond." Particle & Particle Systems Characterization 36, no. 8 (June 7, 2019): 1900116. http://dx.doi.org/10.1002/ppsc.201900116.

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16

Yap, A. S., J. R. Bourke, and S. W. Manley. "Role of cell–cell contact in the preservation of differentiation and response to thyrotrophin in cultured porcine thyroid cells." Journal of Endocrinology 113, no. 2 (May 1987): 223—NP. http://dx.doi.org/10.1677/joe.0.1130223.

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ABSTRACT Cultured porcine thyroid cells did not reassociate into functional follicles in the presence of TSH unless the initial seeding density was adequate. At 0·2 × 106 cells/35 mm diameter culture dish the cells rapidly formed a monolayer even in the presence of TSH (128 μu./ml), and radioiodide uptake was not significantly increased compared with that in control cells. Seeding densities of 1–3 × 106 cells/dish resulted in cultures which responded to TSH with follicular development and increased radioiodide uptake. A cell-free membrane fraction of thyroid homogenate restored the ability of cultures seeded at low densities to respond to TSH with development of follicular morphology and increased radioiodide uptake. Delaying the addition of TSH by 48 h markedly reduced the stimulation of follicular development and radioiodide uptake of cultures. Addition of membrane fractions, or an alkali-soluble fraction of membranes, at zero time improved the responses to TSH added after a 48-h delay. It was concluded that maintenance of differentiation and of TSH-responsiveness in cultured thyroid cells was influenced by cell–cell contact. J. Endocr. (1987) 113, 223–229
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17

Moglia, Italo, Margarita Santiago, Simon Guerrero, Mónica Soler, Alvaro Olivera-Nappa, and Marcelo J. Kogan. "Enhanced Cellular Uptake of H-Chain Human Ferritin Containing Gold Nanoparticles." Pharmaceutics 13, no. 11 (November 19, 2021): 1966. http://dx.doi.org/10.3390/pharmaceutics13111966.

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Gold nanoparticles (AuNP) capped with biocompatible layers have functional optical, chemical, and biological properties as theranostic agents in biomedicine. The ferritin protein containing in situ synthesized AuNPs has been successfully used as an effective and completely biocompatible nanocarrier for AuNPs in human cell lines and animal experiments in vivo. Ferritin can be uptaken by different cell types through receptor-mediated endocytosis. Despite these advantages, few efforts have been made to evaluate the toxicity and cellular internalization of AuNP-containing ferritin nanocages. In this work, we study the potential of human heavy-chain (H) and light-chain (L) ferritin homopolymers as nanoreactors to synthesize AuNPs and their cytotoxicity and cellular uptake in different cell lines. The results show very low toxicity of ferritin-encapsulated AuNPs on different human cell lines and demonstrate that efficient cellular ferritin uptake depends on the specific H or L protein chains forming the ferritin protein cage and the presence or absence of metallic cargo. Cargo-devoid apoferritin is poorly internalized in all cell lines, and the highest ferritin uptake was achieved with AuNP-loaded H-ferritin homopolymers in transferrin-receptor-rich cell lines, showing more than seven times more uptake than apoferritin.
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18

Vorasubin, Nopawan, Quyen To Nguyen, Emilia Olson, Todd A. Aguilera, Tao Jiang, and Roger Y. Tsien. "Cell Penetrating Peptide Uptake by Human Tissue." Otolaryngology–Head and Neck Surgery 139, no. 2_suppl (August 2008): P35. http://dx.doi.org/10.1016/j.otohns.2008.05.116.

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Objective 1) Assess activatable cell penetrating peptide (ACPP) uptake by human tissue. 2) Compare ACPP uptake in normal and cancer tissue. Methods ACPPs are peptides that become activated for cellular uptake by cleavage in the presence of specific proteases. Fluorescently tagging ACPPs and designing a cleavage site recognized by proteases abundant in cancer allows for selective uptake and imaging. Cleavable ACPPs consist of L-amino acids linkers, while uncleavable linkers consist of corresponding D-isomers. To assess ACPP uptake by human tissue, we imaged freshly ressected surgical specimens following incubation with ACPP. Uptake was analyzed by measuring average fluorescent intensities (AFI) for histologically identified areas of cancer and normal tissue. Standardized uptake value (SUV) measurements, which represents fluorescence uptake per given tissue weight, and zymography were also performed. Results Average cancer-to-normal AFI ratio when treated with cleavable ACPP was 2.6±0.6 (p=0.003) and with uncleavable control was 1.4±0.5 (p=0.5). Considering cancer tissue alone, average AFI was 22.5 ±2.2 when treated with cleavable and 11.4 ±1.2 when treated with uncleavable ACPP (p=0.004). Tissue SUV when treated with cleavable ACPP was 2.5±0.8mg-1, whereas tissue treated with control ACPP was 1.7±1.0mg-1 (p=0.24). Zymography results show that inactive protease is ubiquitous in cancer and normal tissue while active form is more abundant in cancer. Conclusions In freshly resected human cancer tissue, uptake of cleavable ACPP is ∼2-fold greater than that of uncleavable ACPP. Furthermore, cleavable ACPP uptake is ∼2.5-fold greater in cancer compared to normal tissue. This differential uptake can potentially be used for in vivo imaging of cancer to guide surgical resection.
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Aljitawi, Omar S., Mathew Fitzgerald, Min Qui, Koyamangalath Krishnan, William L. Stone, and Guha Krishnaswamy. "Preferential Uptake of Gamma Tocopherol by Mast Cells. Does This Uptake Affect Mast Cell Cytokine Production?." Blood 104, no. 11 (November 16, 2004): 3793. http://dx.doi.org/10.1182/blood.v104.11.3793.3793.

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Abstract Vitamin E, the main lipid soluble antioxidant, exists in eight different forms, of which α-tocopherol and γ-tocopherol are the two major forms. Previous experiments showed vitamin E uptake by macrophages that contribute to inflammation and immunity. On the other hand, vitamin E has structural similarity to the thiazolidinedione, troglitazone, a peroxisome proliferator-activated receptor (PPAR) agonist. In previous experiments we found that troglitazone (TGZ), a PPAR gamma agonist, had a negative effect on mast cell cytokine production. We therefore wondered whether vitamin E enters human mast cells, and if so, does this modulate mast cell cytokine production? We choose (interleukin) IL-6 for its pro-inflammatory properties and because it’s known to be produced by mast cells in response to stimulants used in the experiment. In this study we try to answer these two questions. Cultured human mast cell line (HMC-1) was first incubated for 24 hrs with pharmacological concentrations of both alpha and gamma forms of vitamin E (10 μM). The mast cells were then activated with phorbol-12-myristate-13-acetate [PMA (50ng/ml)] and ionomycin (5μm) for 24 hours and cell-free supernatants collected. In additional experiments, IL-1ß (10ng/mL) was added to activate mast cells. IL-6 levels in the supernatants were determined in each well utilizing ELISA. Mast cell concentrations of alpha or gamma tocopherol were measured by high pressure liquid chromatography [HPLC] and electrochemical analysis. Mast cells pre-incubated in alpha and gamma forms of vitamin E at 10 μM did not affect mast cell IL-6 production. Mast cells, however, showed uptake of both forms of tocopherols but more pronounced uptake of the gamma form (13181.05 pmole/well of gamma compared to 8742.99 pmole/well of alpha tocopherol). We conclude that mast cells appear to store both alpha and gamma tocopherols but preferentially more gamma tocopherol. Though Vitamin E and PPAR agonists have similar structures, they did not show similar effect on mast cell cytokine production, suggesting they might have different mechanisms of action.
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20

Law, D., K. S. Hering-Smith, and L. L. Hamm. "Citrate transport in proximal cell line." American Journal of Physiology-Cell Physiology 263, no. 1 (July 1, 1992): C220—C225. http://dx.doi.org/10.1152/ajpcell.1992.263.1.c220.

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Citrate uptake into kidney proximal tubules occurs via an apical dicarboxylate transporter and a poorly characterized process in the basolateral membrane. We used OK cells, a cell line derived from opossum kidney, to study citrate transport in proximal tubule-like cells. Citrate uptake into cell monolayers was studied using [14C]citrate with [3H]mannitol as a volume marker. Citrate uptake into these cells was sodium dependent and saturable with increasing concentrations of citrate. In contrast to previous models, citrate transport was altered minimally by changes in pH from 6.2 to 7.0 and increased at pH 7.4 to 7.8. A variety of di- and tricarboxylates were tested for interaction with citrate transport. The dicarboxylates succinate, malate, and oxaloacetate at 1 mM concentration inhibited citrate uptake minimally (uptake at least 80% of control); one dicarboxylate, alpha-ketoglutarate, did inhibit citrate uptake significantly. In contrast, the tricarboxylates isocitrate and tricarballylate inhibited citrate uptake significantly, indicating probable competitive inhibition with the transport process. These characteristics are distinctly different from those of the apical membrane dicarboxylate transporter. 1,2,3-Benzenetricarboxylic acid, an inhibitor of the mitochondrial tricarboxylate transporter, did not alter citrate uptake. In conclusion, the OK proximal cell line exhibits a novel citrate transport process compared with the apical transport of citrate described in most proximal systems. This transport process probably involves the trivalent species of citrate in contrast to the usual predominant transport of divalent citrate. This transport process may represent a process similar to that in the basolateral membrane of the proximal tubule.
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21

Rhainds, David, and Louise Brissette. "Low density lipoprotein uptake: holoparticle and cholesteryl ester selective uptake." International Journal of Biochemistry & Cell Biology 31, no. 9 (September 1999): 915–31. http://dx.doi.org/10.1016/s1357-2725(99)00046-1.

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22

Simpson, S. J. "Unintentional Uptake." Science Signaling 1, no. 18 (May 6, 2008): ec171-ec171. http://dx.doi.org/10.1126/stke.118ec171.

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23

Winzerling, Joy J., Zeinab E. Jouni, and Donald J. Mcnamara. "Human peritoneal monocytic cells: Lipoprotein uptake and foam cell formation." Life Sciences 62, no. 6 (January 1998): 501–13. http://dx.doi.org/10.1016/s0024-3205(97)01146-6.

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24

Berkenstam, Anders, Jeanne Ahlberg, and Hans Glaumann. "Lysosomal uptake of isolated cell organelles microinjected into HeLa cells." Experimental Cell Research 163, no. 2 (April 1986): 301–8. http://dx.doi.org/10.1016/0014-4827(86)90061-3.

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25

Su, T. Z., C. D. Logsdon, and D. L. Oxender. "Chinese hamster ovary mRNA-dependent, Na(+)-independent L-leucine transport in Xenopus laevis oocytes." Molecular and Cellular Biology 12, no. 12 (December 1992): 5281–87. http://dx.doi.org/10.1128/mcb.12.12.5281-5287.1992.

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In freshly prepared uninjected folliculated oocytes, Na(+)-independent leucine uptake is mediated predominantly by a system L-like transport system. Removal of follicular cells, however, results in an irreversible loss of this transport activity. When total poly(A)+ mRNA derived from Chinese hamster ovary (CHO) cells was injected into prophase-arrested stage V or VI Xenopus laevis oocytes, enhanced expression of Na(+)-independent leucine transport was observed. The injected mRNAs associated with increased levels of leucine uptake were between 2 and 3 kb in length. The newly expressed leucine transport activity exhibited important differences from the known characteristics of system L, which is the dominant Na(+)-independent leucine transporter in CHO cells as well as in freshly isolated folliculated oocytes. The CHO mRNA-dependent leucine uptake in oocytes was highly sensitive to the cationic amino acids lysine, arginine, and and ornithine (> 95% inhibition). As with the leucine uptake, an enhanced lysine uptake was also observed in size-fractionated CHO mRNA-injected oocytes. The uptakes of leucine and lysine were mutually inhibitable, suggesting that the newly expressed transporter was responsible for uptakes of both leucine and lysine. The inhibition of uptake of lysine by leucine was Na+ independent, thus clearly distinguishing it from the previously reported endogenous system y+ activity. Furthermore, the high sensitivity to tryptophan of the CHO mRNA-dependent leucine transport was in sharp contrast to the properties of the recently cloned leucine transport-associated gene from rat kidney tissue, although leucine transport from both sources was sensitive to cationic amino acids. Our results suggest that there may be a family of leucine transporters operative in different tissues and possibly under different conditions.
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Nickel, Robert Sheppard, Elizabeth Seashore, Adina L. Alazraki, John T. Horan, Monica Bhatia, and Ann E. Haight. "Improved Splenic Function after Stem Cell Transplant for Sickle Cell Disease." Blood 124, no. 21 (December 6, 2014): 3966. http://dx.doi.org/10.1182/blood.v124.21.3966.3966.

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Abstract Introduction: Splenic dysfunction is a critical complication of SCD that begins in early childhood and can cause fatal sepsis. Hematopoietic stem cell transplant (HSCT) is a proven cure for SCD, however, its long-term effect on the spleen in patients who had SCD is not well characterized. This information could be helpful to further inform medical professionals and families considering HSCT for SCD. Better understanding of the splenic function of patients after transplant for SCD could also provide important information regarding these patients' future risk of infection and other possible problems related to asplenia. Methods: We conducted a retrospective cohort study of pediatric patients who had HSCT for SCD at two transplant centers. Patients were excluded for analysis if they had pre-HSCT splenectomy, died less than one year post-transplant, failed to engraft, or had no post-HSCT spleen function testing. Tc99m liver-spleen (LS) scans and red blood cell (RBC) pit counts, validated tests to evaluate the spleen in SCD, were used to assess splenic function. Splenic uptake on scans was classified as either present or absent. RBC pit count was classified as either normal or abnormal. If a patient had multiple LS scans or RBC pit counts post-HSCT, then the most recent test was used for this analysis. Results: Fifty-five evaluable patients were identified (53 patients with a post-HSCT LS scan, 29 patients with a post-HSCT RBC pit count, and 27 patients with both tests). Almost all (52/55, 95%) patients had hemoglobin SS or Sβ0 disease. Median age at transplant was 8.8 years (range 1.8-22.0 years). Conditioning regimen and stem cell source varied, however, 48/55 (87%) received myeloablative conditioning and an HLA-identical sibling donor HSCT. At a median 2.0 years post-HSCT (range 0.9-8.9 years), 48/53 (91%) had spleen uptake present on LS scan. At a median 3.2 years post-HSCT (range 1.0-11.4 years), 24/29 (83%) had a normal RBC pit count. Analysis of patients who had both pre- and post-HSCT tests showed that patients had significantly improved outcomes post-HSCT: Table Pre-HSCT Post-HSCT p-value Spleen Uptake Present on LS scan 17/36 (47%) 32/36 (89%) 0.0002 Normal RBC pit count 6/20 (30%) 17/20 (85%) 0.0004 All patients (17/17, 100%) with LS scan spleen uptake pre-HSCT had uptake present post-HSCT compared to 15/19 (79%) patients with absent spleen uptake pre-HSCT had uptake present post-HSCT (p=0.11). Four patients had absent spleen uptake at 1 year post-HSCT but had uptake present at 2 years post-HSCT. Conclusion: Our study represents the largest comprehensive evaluation of long-term splenic function in patients after HSCT for SCD. Our results suggest that successful HSCT mitigates damage to the spleen induced by SCD. In patients with splenic function pre-transplant, HSCT appears to preserve this function. In patients lacking splenic function, HSCT appears to engender the return of function in most, but not all patients. Disclosures No relevant conflicts of interest to declare.
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27

Mitchell, A. M., S. W. Manley, E. J. Payne, and R. H. Mortimer. "Uptake of thyroxine in the human choriocarcinoma cell line JAR." Journal of Endocrinology 146, no. 2 (August 1995): 233–38. http://dx.doi.org/10.1677/joe.0.1460233.

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Abstract We have studied the uptake of 125I-thyroxine (125I-T4) in the human choriocarcinoma cell line JAR. Uptake of 125I-T4 was time-dependent, stereospecific and reversible, with a saturable component of 33% after 120 min of incubation. Kinetic analysis of the initial specific uptake rates indicated the presence of a single uptake process with a Michaelis constant of 59·4 ± 13·9 nm (n=12) and maximum velocity of 0·29 ± 0·06 pmol/min per mg protein. Uptake was dependent on intracellular energy as, in the presence of 2 mm potassium cyanide, saturable uptake was reduced to 60·6 ± 8·5% (n=4) of control uptake. Uptake was also temperature-dependent. Saturable 125I-T4 uptake after 60 min of incubation was 26·1 ± 3·0% at 25 °C (n=6) and 27·3 ± 5·7% at 4 °C of control uptake at 37 °C. Ouabain did not inhibit 125I-T4 uptake indicating that the uptake was independent of the Na gradient across the cell membrane. Although T4 uptake was stereospecific, as d-T4 failed to inhibit 125I-l-T4 uptake, it was not specific for T4, as tri-iodothyronine (T3) and reverse T3 also inhibited 125I-T4 uptake. We conclude that JAR cells have a saturable, stereospecific and reversible membrane transport mechanism for T4 which is dependent on intracellular energy, but independent of the Na+ gradient across the cell membrane. Journal of Endocrinology (1995) 146, 233–238
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Despres, J. P., B. S. Fong, P. Julien, J. Jimenez, and A. Angel. "Regional variation in HDL metabolism in human fat cells: effect of cell size." American Journal of Physiology-Endocrinology and Metabolism 252, no. 5 (May 1, 1987): E654—E659. http://dx.doi.org/10.1152/ajpendo.1987.252.5.e654.

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Abdominal obesity is related to reduced plasma high-density lipoprotein (HDL) cholesterol, and both are associated with cardiovascular disease risk. We have observed that plasma membranes from abdominal subcutaneous adipocytes have a greater HDL binding capacity than omental fat cell plasma membranes. The present study examined whether these binding characteristics could be due to differences in fat cell size or cholesterol concentration between the two adipose depots. Abdominal subcutaneous and deep omental fat were obtained from massively obese patients at surgery. Subcutaneous abdominal fat cells were significantly larger and their cellular cholesterol content greater than omental adipocytes. The uptake of HDL by collagenase-isolated fat cells was studied by incubating the cells for 2 h at 37 degrees C with 10 micrograms/ml 125I-HDL2 or 125I-HDL3. In both depots, the cellular uptake of 125I-HDL2 and 125I-HDL3 was specifically inhibited by addition of 25-fold excess unlabeled HDL and a close correlation was observed between the cellular uptake of 125I-HDL2 and 125I-HDL3. In obese patients, the uptake of 125I-HDL was higher in subcutaneous cells than in omental cells [5.85 +/- 0.53 vs. 2.74 +/- 0.30 pmol X 2 h-1. (10(6) cells)-1]. The cellular 125I-HDL uptake was significantly correlated with adipocyte size and fat cell cholesterol content but not with adipocyte cholesterol concentration. These results suggest that the higher HDL uptake observed in subcutaneous cells compared with omental cells in obesity is the result of differences in adipocyte size rather than differences in the cholesterol concentration (cholesterol-to-triglyceride ratio).(ABSTRACT TRUNCATED AT 250 WORDS)
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29

Hamzah, Rabab N., Karrer M. Alghazali, Alexandru S. Biris, and Robert J. Griffin. "Exosome Traceability and Cell Source Dependence on Composition and Cell-Cell Cross Talk." International Journal of Molecular Sciences 22, no. 10 (May 19, 2021): 5346. http://dx.doi.org/10.3390/ijms22105346.

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Exosomes are small vesicles with an average diameter of 100 nm that are produced by many, if not all, cell types. Exosome cargo includes lipids, proteins, and nucleic acids arranged specifically in the endosomes of donor cells. Exosomes can transfer the donor cell components to target cells and can affect cell signaling, proliferation, and differentiation. Important new information about exosomes’ remote communication with other cells is rapidly being accumulated. Recent data indicates that the results of this communication depend on the donor cell type and the environment of the host cell. In the field of cancer research, major questions remain, such as whether tumor cell exosomes are equally taken up by cancer cells and normal cells and whether exosomes secreted by normal cells are specifically taken up by other normal cells or also tumor cells. Furthermore, we do not know how exosome uptake is made selective, how we can trace exosome uptake selectivity, or what the most appropriate methods are to study exosome uptake and selectivity. This review will explain the effect of exosome source and the impact of the donor cell growth environment on tumor and normal cell interaction and communication. The review will also summarize the methods that have been used to label and trace exosomes to date.
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30

Ford, D. M., R. H. Dahl, C. A. Lamp, and B. A. Molitoris. "Apically and basolaterally internalized aminoglycosides colocalize in LLC-PK1 lysosomes and alter cell function." American Journal of Physiology-Cell Physiology 266, no. 1 (January 1, 1994): C52—C57. http://dx.doi.org/10.1152/ajpcell.1994.266.1.c52.

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Aminoglycosides bind to apical and basolateral (BL) membranes of renal epithelial cells. However, little is known regarding differential uptake and intracellular processing after internalization across these distinct surface membrane domains. To examine these processes independently, LLC-PK1 cells were grown on porous filters, which allow selective access to both domains. Apical and BL membrane uptakes of gentamicin (0.5 mM), quantified using [3H]gentamicin, were linear from 2 to 24 h (r = 0.99). The 4-h apical gentamicin uptake was 667 +/- 59 pmol/mg protein, the BL 748 +/- 26 pmol/mg protein, and concurrent apical and BL uptake 1,389 +/- 22 pmol/mg protein. Aminoglycoside uptake, documented using indirect immunogold techniques, occurred via the apical and BL endocytic systems and colocalized with cationic ferritin. Aminoglycosides internalized via the apical (gentamicin) and BL (tobramycin) membrane converged at the lysosomal level. Gentamicin incorporated via either domain significantly decreased lysosomal N-acetylglucosaminidase below control values (P < 0.05). We conclude that, after binding, aminoglycosides are internalized equally across apical and BL membranes of LLC-PK1 cells via receptor-mediated endocytosis, colocalize within the lysosomal compartment, and alter cellular function similarly.
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31

Phoaubon, Supathra, Kornkamon Lertsuwan, Jarinthorn Teerapornpuntakit, and Narattaphol Charoenphandhu. "Hepcidin induces intestinal calcium uptake while suppressing iron uptake in Caco-2 cells." PLOS ONE 16, no. 10 (October 13, 2021): e0258433. http://dx.doi.org/10.1371/journal.pone.0258433.

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Abnormal calcium absorption and iron overload from iron hyperabsorption can contribute to osteoporosis as found in several diseases, including hemochromatosis and thalassemia. Previous studies in thalassemic mice showed the positive effects of the iron uptake suppressor, hepcidin, on calcium transport. However, whether this effect could be replicated in other conditions is not known. Therefore, this study aimed to investigate the effects of hepcidin on iron and calcium uptake ability under physiological, iron uptake stimulation and calcium uptake suppression. To investigate the potential mechanism, effects of hepcidin on the expression of iron and calcium transporter and transport-associated protein in Caco-2 cells were also determined. Our results showed that intestinal cell iron uptake was significantly increased by ascorbic acid together with ferric ammonium citrate (FAC), but this phenomenon was suppressed by hepcidin. Interestingly, hepcidin significantly increased calcium uptake under physiological condition but not under iron uptake stimulation. While hepcidin significantly suppressed the expression of iron transporter, it had no effect on calcium transporter expression. This indicated that hepcidin-induced intestinal cell calcium uptake did not occur through the stimulation of calcium transporter expression. On the other hand, 1,25(OH)2D3 effectively induced intestinal cell calcium uptake, but it did not affect intestinal cell iron uptake or iron transporter expression. The 1,25(OH)2D3-induced intestinal cell calcium uptake was abolished by 12 mM CaCl2; however, hepcidin could not rescue intestinal cell calcium uptake suppression by CaCl2. Taken together, our results showed that hepcidin could effectively and concurrently induce intestinal cell calcium uptake while reducing intestinal cell iron uptake under physiological and iron uptake stimulation conditions, suggesting its therapeutic potential for inactive calcium absorption, particularly in thalassemic patients or patients who did not adequately respond to 1,25(OH)2D3.
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32

Sato, Toshinori, Hajime Miyaguchi, and Yoshio Okahata. "Cell uptake of albumin with synthetic glycolipid." Drug Delivery System 10, no. 3 (1995): 199–200. http://dx.doi.org/10.2745/dds.10.199.

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33

Kusoglu, Ahmet, Anthony Kwong, Kyle T. Clark, Haluna P. Gunterman, and Adam Z. Weber. "Water Uptake of Fuel-Cell Catalyst Layers." Journal of The Electrochemical Society 159, no. 9 (2012): F530—F535. http://dx.doi.org/10.1149/2.031209jes.

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34

Wang, Jing, Lixin Liu, Wen Zhu, Yongming Chen, and Chun Wang. "Cancer Cell Uptake of Polymer Hydrogel Nanotubes." Journal of Biomedical Nanotechnology 10, no. 11 (November 1, 2014): 3329–36. http://dx.doi.org/10.1166/jbn.2014.1923.

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35

Vila, M., M. T. Portolés, P. A. A. P. Marques, M. J. Feito, M. C. Matesanz, C. Ramírez-Santillán, G. Gonçalves, S. M. A. Cruz, A. Nieto, and M. Vallet-Regi. "Cell uptake survey of pegylated nanographene oxide." Nanotechnology 23, no. 46 (October 23, 2012): 465103. http://dx.doi.org/10.1088/0957-4484/23/46/465103.

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36

GARBO, GRETA M., RICK W. KECK, STEVEN H. SELMAN, and MARTHA KREIMER-BIRN BAUM. "Hematoporphyrin Derivative Uptake and Tumor Cell Density." Annals of the New York Academy of Sciences 514, no. 1 Mechanisms of (December 1987): 328–29. http://dx.doi.org/10.1111/j.1749-6632.1987.tb48789.x.

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37

Elsworth, Brendan, Caroline D. Keroack, and Manoj T. Duraisingh. "Elucidating Host Cell Uptake by Malaria Parasites." Trends in Parasitology 35, no. 5 (May 2019): 333–35. http://dx.doi.org/10.1016/j.pt.2019.03.005.

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38

Ohkubo, Satoko, Koichi Nagata, and Norimichi Nakahata. "Adenosine uptake-dependent C6 cell growth inhibition." European Journal of Pharmacology 577, no. 1-3 (December 2007): 35–43. http://dx.doi.org/10.1016/j.ejphar.2007.08.025.

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39

Winslow, Robert M. "A model for red cell O2 uptake." International Journal of Clinical Monitoring and Computing 2, no. 2 (June 1985): 81–93. http://dx.doi.org/10.1007/bf02916236.

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40

Holm, Tina, Henrik Johansson, Pontus Lundberg, Margus Pooga, Maria Lindgren, and Ülo Langel. "Studying the uptake of cell-penetrating peptides." Nature Protocols 1, no. 2 (August 2006): 1001–5. http://dx.doi.org/10.1038/nprot.2006.174.

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41

Palouzier-Paulignan, B., M. C. Chamoin, and J. P. Ternaux. "Choline uptake in cholinergic nodose cell bodies." Neuroscience 43, no. 2-3 (January 1991): 687–96. http://dx.doi.org/10.1016/0306-4522(91)90327-k.

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42

Holm, Tina, Semharai Netzereab, Mats Hansen, Ülo Langel, and Mattias Hällbrink. "Uptake of cell-penetrating peptides in yeasts." FEBS Letters 579, no. 23 (September 2, 2005): 5217–22. http://dx.doi.org/10.1016/j.febslet.2005.07.099.

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43

Chothe, Paresh, Nagendra Singh, and Vadivel Ganapathy. "Evidence for two different broad-specificity oligopeptide transporters in intestinal cell line Caco-2 and colonic cell line CCD841." American Journal of Physiology-Cell Physiology 300, no. 6 (June 2011): C1260—C1269. http://dx.doi.org/10.1152/ajpcell.00299.2010.

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Recently the existence of two different Na+-coupled oligopeptide transport systems has been described in mammalian cells. These transport systems are distinct from the previously known H+/peptide cotransporters PEPT1 and PEPT2, which transport only dipeptides and tripeptides. To date, the only peptide transport system known to exist in the intestine is PEPT1. Here we investigated the expression of the Na+-coupled oligopeptide transporters in intestinal cell lines, using the hydrolysis-resistant synthetic oligopeptides deltorphin II and [d-Ala2,d-Leu5]enkephalin (DADLE) as model substrates. Caco-2 cells and CCD841 cells, both representing epithelial cells from human intestinal tract, were able to take up these oligopeptides. Uptake of deltorphin II was mostly Na+ dependent, with more than 2 Na+ involved in the uptake process. In contrast, DADLE uptake was only partially Na+ dependent. The uptake of both peptides was also influenced by H+ and Cl−, although to a varying degree. The processes responsible for the uptake of deltorphin II and DADLE could be differentiated not only by their Na+ dependence but also by their modulation by small peptides. Several dipeptides and tripeptides stimulated deltorphin II uptake but inhibited DADLE uptake. These modulating small peptides were, however, not transportable substrates for the transport systems that mediate deltorphin II or DADLE uptake. These two oligopeptide transport systems were also able to take up several nonopioid oligopeptides, consisting of 9–17 amino acids. This represents the first report on the existence of transport systems in intestinal cells that are distinct from PEPT1 and capable of transporting oligopeptides consisting of five or more amino acids.
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44

Petersen, Fernanda C., Lin Tao, and Anne A. Scheie. "DNA Binding-Uptake System: a Link between Cell-to-Cell Communication and Biofilm Formation." Journal of Bacteriology 187, no. 13 (July 1, 2005): 4392–400. http://dx.doi.org/10.1128/jb.187.13.4392-4400.2005.

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ABSTRACT DNA has recently been described as a major structural component of the extracellular matrix in biofilms. In streptococci, the competence-stimulating peptide (CSP) cell-to-cell signal is involved in competence for genetic transformation, biofilm formation, and autolysis. Among the genes regulated in response to the CSP are those involved in binding and uptake of extracellular DNA. We show in this study that a functional DNA binding-uptake system is involved in biofilm formation. A comGB mutant of Streptococcus mutans deficient in DNA binding and uptake, but unaffected in signaling, showed reduced biofilm formation. During growth in the presence of DNase I, biofilm was reduced in the wild type to levels similar to those found with the comGB mutant, suggesting that DNA plays an important role in the wild-type biofilm formation. We also showed that growth in the presence of synthetic CSP promoted significant release of DNA, with similar levels in the wild type and in the comGB mutant. The importance of the DNA binding-uptake system in biofilm formation points to possible novel targets to fight infections.
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45

Delvaux, M., M. J. Bastie, J. Chentoufi, E. J. Cragoe, N. Vaysse, and A. Ribet. "Amiloride and analogues inhibit Na(+)-H+ exchange and cell proliferation in AR42J pancreatic cell line." American Journal of Physiology-Gastrointestinal and Liver Physiology 259, no. 5 (November 1, 1990): G842—G849. http://dx.doi.org/10.1152/ajpgi.1990.259.5.g842.

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To study the relation between activation of the Na(+)-H+ antiporter and gastrointestinal cell proliferation, we characterized this antiporter in a pancreatic cell line (AR42J) and studied the effects of mitogenic and nonmitogenic agents as well as those of Na(+)-H+ exchange blocking agents on DNA synthesis. Characteristics of amiloride-sensitive Na+ uptake were those of the Na(+)-H+ exchanger: 1) Na+ uptake was increased by intracellular acidification and depended on external [Na+] and pH; 2) concentrations for half-maximal inhibition (IC50) of Na+ uptake (3 mM [Na+] in medium) were 40 nM 5-(N,N-hexamethylene)amiloride (HA) less than 0.1 microM 5-(N-ethyl-N-isopropyl)amiloride (EIPA) less than 1 microM 5-(N,N-dimethyl)-amiloride (DMA) less than 40 microM amiloride; 3) IC50 for amiloride and analogues to inhibit Na+ uptake depended on [Na+] in medium (in 25 mM Na+ medium, the IC50 values were higher than in 3 mM and were 1 microM EIPA less than 10 microM DMA less than 0.3 mM amiloride). Growth factors for AR42J cells (dialyzed fetal calf serum and epidermal growth factor) activated Na+ uptake in a dose-dependent manner. Bombesin, which is nonmitogenic for AR42J cells, also increased Na+ uptake, indicating that activation of the antiporter is not sufficient to initiate cell proliferation in the AR42J cell line. The effects of Na(+)-H+ exchange blocking agents were tested on serum-stimulated cell proliferation. Decreasing external Na+ dramatically decreased AR42J cell proliferation. Amiloride and analogues inhibited [3H]thymidine incorporation in the same range of concentrations as that with which they inhibited Na(+)-H+ exchange.(ABSTRACT TRUNCATED AT 250 WORDS)
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46

Chen, Ruohua, Xiang Zhou, Gang Huang, and Jianjun Liu. "Fructose 1,6-Bisphosphatase 1 Expression Reduces 18F-FDG Uptake in Clear Cell Renal Cell Carcinoma." Contrast Media & Molecular Imaging 2019 (January 6, 2019): 1–6. http://dx.doi.org/10.1155/2019/9463926.

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Purpose. To determine the relationship between fructose 1,6-bisphosphatase 1 (FBP1) expression and fluorine 18 (18F) fluorodeoxyglucose (FDG) uptake in patients with clear cell renal cell carcinoma (ccRCC), and to investigate how 18F-FDG uptake and FBP1 expression are related to tumor metabolism and tumor differentiation grade. Materials and Methods. A total of 54 patients with ccRCC underwent 18F-FDG combined positron emission tomography and computed tomography (PET/CT) before tumor resection. The maximum standardized uptake value (SUVmax) for the primary tumor was calculated from the 18F-FDG uptake. The relationship between SUVmax of primary tumor and the expression of FBP1, hexokinase 2 (HK2), and glucose transporter 1 (GLUT1) was analyzed via immunohistochemical analysis. Results. We identified an inverse relationship between FBP1 expression and SUVmax (P=0.031). SUVmax was higher in patients with high-grade ccRCC (mean, 11.6 ± 5.0) than in those with low-grade ccRCC (mean, 3.8 ± 1.6, P<0.001). FBP1 expression was significantly lower in patients with high-grade ccRCC (mean, 0.23 ± 0.1) than in those with low-grade ccRCC (mean, 0.57 ± 0.08; P=0.018). FBP1 status could be predicted with an accuracy of 66.7% when a SUVmax cutoff value of 3.55 was used. GLUT1 expression in ccRCC was positively correlated with 18F-FDG uptake and FBP1 status, whereas HK2 expression was not. Conclusion. SUVmax in patients with ccRCC is inversely associated with the expression of FBP1, and FBP1 may inhibit 18F-FDG uptake via regulating GLUT1. SUVmax is higher in patients with high-grade ccRCC than in those with low-grade ccRCC, which could be the result of lower FBP1 expression in patients with high-grade ccRCC.
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47

van der Putten, HH, BJ Joosten, PH Klaren, and ME Everts. "Uptake of tri-iodothyronine and thyroxine in myoblasts and myotubes of the embryonic heart cell line H9c2(2-1)." Journal of Endocrinology 175, no. 3 (December 1, 2002): 587–96. http://dx.doi.org/10.1677/joe.0.1750587.

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Uptake of tri-iodothyronine (T(3)) was compared with that of thyroxine (T(4)) in the embryonic heart cell line H9c2 (2-1). These cells propagate as myoblasts and form differentiated myotubes upon reduction of the serum concentration, as indicated by a 31-fold increase in creatine kinase activity. Protein and DNA content per well were around 2-fold higher in myotubes than in myoblasts. When expressed per well, T(3) and T(4) uptake were, compared with myoblasts, 1.9- to 2-fold and 3.1- to 4-fold higher in myotubes respectively. On the other hand, the characteristics of T(3) and T(4) uptake were similar in myoblasts and myotubes. At any time-point, T(4) uptake was 2-fold higher than that of T(3), and both uptakes were energy but not Na(+) dependent. T(3) and T(4) uptake exhibited mutual inhibition in myoblasts and myotubes: 10 microM unlabeled T(3) reduced T(4) uptake by 51-60% (P<0.001), while 10 microM T(4) inhibited T(3) uptake by 48-51% (P<0.001). Furthermore, T(3) and T(4) uptake in myoblasts was dose-dependently inhibited by tryptophan (maximum inhibition around 70%; P<0.001). Exposure of the cells to T(3) or T(4) during differentiation significantly increased the fusion index (35 and 40%; P < 0.01). Finally, both myoblasts and myotubes showed a small deiodinase type I activity, while deiodinase type II activity was undetectable. In conclusion, T(3) and T(4) share a common energy-dependent transport system in H9c2(2-1) cells, that may be important for the availability of thyroid hormone during differentiation.
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48

Morrison, R. F., and E. R. Seidel. "Cell spreading and the regulation of ornithine decarboxylase." Journal of Cell Science 108, no. 12 (December 1, 1995): 3787–94. http://dx.doi.org/10.1242/jcs.108.12.3787.

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The aim of this study was to investigate the effect of cell spreading on the induction of ornithine decarboxylase and the rate of putrescine uptake in anchorage-dependent and anchorage-independent cells. Plating non-transformed IEC-6 epithelial cells at high versus low cell density restricted cell spreading from 900 microns 2 to approximately 140 microns 2, blunted the transient induction of ornithine decarboxylase activity from 202 to 32 pmol 14CO2/mg protein per hour and reduced the rate of [14C] putrescine uptake from 46 to 23 pmol/10(5) cells per hour. The mean spreading area of the cell population was controlled by coating tissue culture dishes with the nonadhesive polymer, polyHEMA. Ornithine decarboxylase activity and putrescine uptake correlated with cell spreading with minimal spreading (263 microns 2) corresponding to an 83% decrease in ornithine decarboxylase activity and 51% decrease in the rate of putrescine uptake. Adding the RGD peptide, Gly-Arg-Gly-Glu-Ser-Pro to the medium of sparsely plated cells resulted in rapid reductions in cell spreading concomitant with dose-dependent decreases in ornithine decarboxylase activity and putrescine uptake. Finally, minimizing cell spreading by depriving cells of substratum contact completely abolished serum-induced increases in ornithine decarboxylase and reduced the rate of putrescine uptake by 47%. In contrast to IEC-6 cells, ornithine decarboxylase of neoplastic HTC-116 cells was constitutively expressed with basal and stimulated activity (193 and 982 pmol 14CO2/mg protein per hour, respectively) completely independent of cell adhesion. Putrescine uptake, however, was abolished in the absence of cell adhesion. These data suggest that the induction of ornithine decarboxylase activity and the rate of putrescine uptake correlate with spreading of anchorage-dependent IEC-6 cells and that ornithine decarboxylase activity but not putrescine uptake, appears to be independent of spreading of neoplastic HTC-116 cells.
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49

Podolsky, Michael J., Deepti Gupta, Arnold Ha, Ryan Ta, Amin Khalifeh-Soltani, William McKleroy, Ritwik Datta, Dean Sheppard, and Kamran Atabai. "Cell division cycle 7 kinase is a negative regulator of cell-mediated collagen degradation." American Journal of Physiology-Lung Cellular and Molecular Physiology 315, no. 3 (September 1, 2018): L360—L370. http://dx.doi.org/10.1152/ajplung.00144.2018.

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Although extensive work has delineated many of the mechanisms of extracellular matrix (ECM) production, far less is known about pathways that regulate ECM degradation. This is particularly true of cellular internalization and degradation of matrix, which play an underappreciated role in ECM metabolism and lung fibrosis. For example, genetic perturbation of this pathway leads to exacerbated fibrosis in experimental animal models. In this work, we present the results of an unbiased screen of Drosophila phagocytes that yielded multiple genes that, when silenced, led to increased collagen uptake. We further describe the function of cell division cycle 7 kinase (CDC7) as a specific suppressor of collagen uptake. We show that the genetic or pharmacological inhibition of CDC7 results in increased expression of the collagen endocytic receptor Endo180. Chromobox 5 (CBX5) is a putative target of CDC7, and genetic silencing of CBX5 also results in increased Endo180 and collagen uptake. Finally, CRISPR-mediated activation of Endo180 expression results in increased collagen uptake, suggesting that CDC7 regulates collagen internalization through increased Endo180 expression. Targeting the regulatory elements of the collagen degradative machinery may be a useful therapeutic approach in diseases of fibrosis or malignancy.
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50

Ohrui, T., W. Skach, M. Thompson, J. Matsumoto-Pon, C. Calayag, and J. H. Widdicombe. "Radiotracer studies of cystic fibrosis transmembrane conductance regulator expressed in Xenopus oocytes." American Journal of Physiology-Cell Physiology 266, no. 6 (June 1, 1994): C1586—C1593. http://dx.doi.org/10.1152/ajpcell.1994.266.6.c1586.

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We measured fluxes of radiotracers in Xenopus oocytes expressing the cystic fibrosis transmembrane conductance regulator (CFTR). Addition of adenosine 3',5'-cyclic monophosphate (cAMP)-elevating agents [forskolin and 3-isobutyl-1-methylxanthine (I/F)] led to large increases in uptake of 36Cl, 125I, and 82Br into oocytes expressing wild-type CFTR or delta F508 CFTR but not sham-injected oocytes. I/F also stimulated halide efflux from CFTR and delta F508 oocytes in the sequence Cl > Br > I. cAMP-induced increases in 36Cl efflux from delta F508 oocytes were approximately 20% of those in CFTR oocytes. Increases in halide efflux were blocked by diphenylamine-2-carboxylic acid but not by 4,4'-diisothiocyanostilbene-2,2'-disulfonic acid. The phorbol ester, phorbol 12-myristate 13-acetate, also stimulated 36Cl efflux from CFTR oocytes. ATP uptakes into CFTR and sham oocytes were similar, and both were reduced by I/F. However, ATP uptake into I/F-treated CFTR oocytes was slightly greater (approximately 40%) than into I/F-treated sham oocytes. Urea uptake into CFTR and sham oocytes was similar and in both cases was increased by I/F. However, the I/F-induced increase in urea uptake into CFTR oocytes was significantly greater than for sham oocytes. I/F stimulated formate uptake into CFTR oocytes but not into sham oocytes. Fluxes of 22Na, 86Rb, 35SO4, 32PO4, and mannitol were unaltered by expression and activation of CFTR.
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