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Thematische Bibliographien / Aminoglycosides uptake

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Zeitschriftenartikel

Auswahl der wissenschaftlichen Literatur zum Thema „Aminoglycosides uptake“

Autor: Grafiati

Veröffentlicht am 25. Mai 2024

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Zeitschriftenartikel zum Thema "Aminoglycosides uptake"

1

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 (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

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2

Rodriguez, Mônica B., and Sérgio O. P. Costa. "Spontaneous kanamycin-resistant Escherichia coli mutant with altered periplasmic oligopeptide permease protein (OppA) and impermeability to aminoglycosides." Revista de Microbiologia 30, no. 2 (1999): 153–56. http://dx.doi.org/10.1590/s0001-37141999000200013.

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A spontaneous kanamycin-resistant Escherichia coli mutant, showing cross resistance to five other aminoglycosides and absence of the OppA protein was isolated. [3H]-dihydrostreptomycin uptake is reduced in this mutant, implying that the oligopeptide transport system is involved in accumulation of aminoglycosides, although apparently not related with aminoglycoside permeability alteration due to bacterial adaptation to osmotic changes.

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3

McCollister, Bruce D., Matthew Hoffman, Maroof Husain, and Andrés Vázquez-Torres. "Nitric Oxide Protects Bacteria from Aminoglycosides by Blocking the Energy-Dependent Phases of Drug Uptake." Antimicrobial Agents and Chemotherapy 55, no. 5 (2011): 2189–96. http://dx.doi.org/10.1128/aac.01203-10.

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ABSTRACTOur investigations have identified a mechanism by which exogenous production of nitric oxide (NO) induces resistance of Gram-positive and -negative bacteria to aminoglycosides. An NO donor was found to protectSalmonellaspp. against structurally diverse classes of aminoglycosides of the 4,6-disubstituted 2-deoxystreptamine group. Likewise, NO generated enzymatically by inducible NO synthase of gamma interferon-primed macrophages protected intracellularSalmonellaagainst the cytotoxicity of gentamicin. NO levels that elicited protection against aminoglycosides repressedSalmonellarespirato

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4

Ezraty, Benjamin, Alexandra Vergnes, Manuel Banzhaf, et al. "Fe-S Cluster Biosynthesis Controls Uptake of Aminoglycosides in a ROS-Less Death Pathway." Science 340, no. 6140 (2013): 1583–87. http://dx.doi.org/10.1126/science.1238328.

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All bactericidal antibiotics were recently proposed to kill by inducing reactive oxygen species (ROS) production, causing destabilization of iron-sulfur (Fe-S) clusters and generating Fenton chemistry. We find that the ROS response is dispensable upon treatment with bactericidal antibiotics. Furthermore, we demonstrate that Fe-S clusters are required for killing only by aminoglycosides. In contrast to cells, using the major Fe-S cluster biosynthesis machinery, ISC, cells using the alternative machinery, SUF, cannot efficiently mature respiratory complexes I and II, resulting in impendence of t

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5

Mao, Weimin, Mark S. Warren, Angela Lee, Anita Mistry, and Olga Lomovskaya. "MexXY-OprM Efflux Pump Is Required for Antagonism of Aminoglycosides by Divalent Cations inPseudomonas aeruginosa." Antimicrobial Agents and Chemotherapy 45, no. 7 (2001): 2001–7. http://dx.doi.org/10.1128/aac.45.7.2001-2007.2001.

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ABSTRACT Antagonism of aminoglycosides by divalent cations is well documented for Pseudomonas aeruginosa and is regarded as one of the problems in aminoglycoside therapy. It is generally considered that divalent cations interfere with uptake of aminoglycosides at both the outer and inner membranes. It has been demonstrated recently that aminoglycosides can be removed from cells ofP. aeruginosa by the three-component multidrug resistance efflux pump MexXY-OprM. We sought to investigate the interplay between efflux and uptake in resistance to aminoglycosides inP. aeruginosa. To do so, we studied

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6

Kang, Hyung Sub, Dirk Kerstan, Long-jun Dai, Gordon Ritchie, and Gary A. Quamme. "Aminoglycosides inhibit hormone-stimulated Mg2+ uptake in mouse distal convoluted tubule cells." Canadian Journal of Physiology and Pharmacology 78, no. 8 (2000): 595–602. http://dx.doi.org/10.1139/y00-038.

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The clinical use of aminoglycosides often leads to renal magnesium wasting and hypomagnesemia. Of the nephron segments, both the thick ascending limb of Henle's loop and the distal tubule play significant roles in renal magnesium conservation but the distal convoluted tubule exerts the final control of urinary excretion. An immortalized mouse distal convoluted tubule (MDCT) cell line has been extensively used to study the cellular mechanisms of magnesium transport in this nephron segment. Peptide hormones, such as parathyroid hormone (PTH), glucagon, calcitonin, and arginine vasopressin (AVP)

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7

Jassem, Agatha N., James E. A. Zlosnik, Deborah A. Henry, Robert E. W. Hancock, Robert K. Ernst, and David P. Speert. "In VitroSusceptibility of Burkholderia vietnamiensis to Aminoglycosides." Antimicrobial Agents and Chemotherapy 55, no. 5 (2011): 2256–64. http://dx.doi.org/10.1128/aac.01434-10.

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ABSTRACTBurkholderia cepaciacomplex (BCC) bacteria are opportunistic pathogens that can cause severe disease in cystic fibrosis (CF) patients and other immunocompromised individuals and are typically multidrug resistant. Here we observed that unlike other BCC species, most environmental and clinicalBurkholderia vietnamiensisisolates were intrinsically susceptible to aminoglycosides but not to cationic antimicrobial peptides or polymyxin B. Furthermore, strains acquired aminoglycoside resistance during chronic CF infection, a phenomenon that could be induced under tobramycin or azithromycin pre

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8

Hadidi, Kaivin, Ezequiel Wexselblatt, Jeffrey D. Esko, and Yitzhak Tor. "Cellular uptake of modified aminoglycosides." Journal of Antibiotics 71, no. 1 (2017): 142–45. http://dx.doi.org/10.1038/ja.2017.131.

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9

Jiang, Meiyan, Hongzhe Li, Anastasiya Johnson, et al. "Inflammation up-regulates cochlear expression of TRPV1 to potentiate drug-induced hearing loss." Science Advances 5, no. 7 (2019): eaaw1836. http://dx.doi.org/10.1126/sciadv.aaw1836.

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Aminoglycoside antibiotics are essential for treating life-threatening bacterial infections, despite the risk of lifelong hearing loss. Infections induce inflammation and up-regulate expression of candidate aminoglycoside-permeant cation channels, including transient receptor potential vanilloid-1 (TRPV1). Heterologous expression of TRPV1 facilitated cellular uptake of (fluorescently tagged) gentamicin that was enhanced by agonists, and diminished by antagonists, of TRPV1. Cochlear TRPV1 was immunolocalized near the apical membranes of sensory hair cells, adjacent supporting cells, and margina

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10

Schlessinger, D. "Failure of aminoglycoside antibiotics to kill anaerobic, low-pH, and resistant cultures." Clinical Microbiology Reviews 1, no. 1 (1988): 54–59. http://dx.doi.org/10.1128/cmr.1.1.54.

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The critical inhibition of ribosome function by aminoglycosides has long been established. But the binding of drug to ribosomes is reversible: why then are aminoglycosides bactericidal? Several groups have shown that irreversible action (lethality) results from irreversible uptake into susceptible cells; conversely, resistance in cases such as anaerobiosis is associated with the failure of uptake. Oddly, the pattern of results excludes all traditional transport mechanisms; most unusual is the apparent dependence of uptake on the interaction of drug with ribosomes. A traditional view that ribos

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