Cargando…

Enzymatic Suppression of the Membrane Conductance Associated with the Glutamine Transporter SNAT3 Expressed in Xenopus Oocytes by Carbonic Anhydrase II

The transport activity of the glutamine/neutral amino acid transporter SNAT3 (former SN1, SLC38A3), expressed in oocytes of the frog Xenopus laevis is associated with a non-stoichiometrical membrane conductance selective for Na(+) and/or H(+) (Schneider, H.P., S. Bröer, A. Bröer, and J.W. Deitmer. 2...

Descripción completa

Detalles Bibliográficos
Autores principales:	Weise, Alexandra, Becker, Holger M., Deitmer, Joachim W.
Formato:	Texto
Lenguaje:	English
Publicado:	The Rockefeller University Press 2007
Materias:	Articles
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2151638/ https://www.ncbi.nlm.nih.gov/pubmed/17664347 http://dx.doi.org/10.1085/jgp.200709809

Ejemplares similares

Transport metabolons with carbonic anhydrases
por: Deitmer, Joachim W., et al.
Publicado: (2013)

Proton Transport in Cancer Cells: The Role of Carbonic Anhydrases
por: Becker, Holger M., et al.
Publicado: (2021)

Transport Activity of the Sodium Bicarbonate Cotransporter NBCe1 Is Enhanced by Different Isoforms of Carbonic Anhydrase
por: Schueler, Christina, et al.
Publicado: (2011)

The role of membrane acid/base transporters and carbonic anhydrases for cellular pH and metabolic processes
por: Deitmer, Joachim W., et al.
Publicado: (2015)

A surface proton antenna in carbonic anhydrase II supports lactate transport in cancer cells
por: Noor, Sina Ibne, et al.
Publicado: (2018)

Catalytically inactive carbonic anhydrase‐related proteins enhance transport of lactate by MCT1
por: Aspatwar, Ashok, et al.
Publicado: (2019)

Glutamine Uptake via SNAT6 and Caveolin Regulates Glutamine–Glutamate Cycle
por: Gandasi, Nikhil R., et al.
Publicado: (2021)

PKC-Mediated Modulation of Astrocyte SNAT3 Glutamine Transporter Function at Synapses in Situ
por: Dong, Wuxing, et al.
Publicado: (2018)

Carbonic anhydrase IX and acid transport in cancer
por: Becker, Holger M.
Publicado: (2019)

Role of Carbonic Anhydrase IV in the Bicarbonate-Mediated Activation of Murine and Human Sperm
por: Wandernoth, Petra M., et al.
Publicado: (2010)

Inhibition of the glutamine transporter SNAT1 confers neuroprotection in mice by modulating the mTOR-autophagy system
por: Yamada, Daisuke, et al.
Publicado: (2019)

NRF2 regulates the glutamine transporter Slc38a3 (SNAT3) in kidney in response to metabolic acidosis
por: Lister, Adam, et al.
Publicado: (2018)

Hypoxia-induced carbonic anhydrase IX facilitates lactate flux in human breast cancer cells by non-catalytic function
por: Jamali, Somayeh, et al.
Publicado: (2015)

Xenopus Oocyte’s Conductance for Bioactive Compounds Screening and Characterization
por: Cheikh, Amani, et al.
Publicado: (2019)

The “www” of Xenopus laevis Oocytes: The Why, When, What of Xenopus laevis Oocytes in Membrane Transporters Research
por: Bhatt, Manan, et al.
Publicado: (2022)

Optimizing plant transporter expression in Xenopus oocytes
por: Feng, Huimin, et al.
Publicado: (2013)

Transport Metabolons and Acid/Base Balance in Tumor Cells
por: Becker, Holger M., et al.
Publicado: (2020)

Increased expression of glutamine transporter SNAT2/SLC38A2 promotes glutamine dependence and oxidative stress resistance, and is associated with worse prognosis in triple-negative breast cancer
por: Morotti, Matteo, et al.
Publicado: (2020)

Expression of Glutamine Transporter Slc38a3 (SNAT3) During Acidosis is Mediated by a Different Mechanism than Tissue-Specific Expression
por: Balkrishna, Sarojini, et al.
Publicado: (2014)

Oocyte shuttle, a recombinant protein transporting donor DNA into the Xenopus oocyte in situ
por: Rungger, Duri, et al.
Publicado: (2017)

Actin in Xenopus oocytes
Publicado: (1978)

Reduction of epileptiform activity in ketogenic mice: The role of monocarboxylate transporters
por: Forero-Quintero, Linda S., et al.
Publicado: (2017)

Characterization and Regulation of the Amino Acid Transporter SNAT2 in the Small Intestine of Piglets
por: Li, Guangran, et al.
Publicado: (2015)

Unique regulation of Na‐glutamine cotransporter SN2/SNAT5 in rabbit intestinal crypt cells during chronic enteritis
por: Singh, Soudamani, et al.
Publicado: (2017)

Boric acid transport activity of human aquaporins expressed in Xenopus oocytes
por: Ushio, Kazutaka, et al.
Publicado: (2022)

The proteoglycan-like domain of carbonic anhydrase IX mediates non-catalytic facilitation of lactate transport in cancer cells
por: Ames, Samantha, et al.
Publicado: (2018)

Microinjection of Xenopus Laevis Oocytes
por: Cohen, Sarah, et al.
Publicado: (2009)

Identification of a Disulfide Bridge Important for Transport Function of SNAT4 Neutral Amino Acid Transporter
por: Padmanabhan Iyer, Rugmani, et al.
Publicado: (2013)

Remnants of the Balbiani body are required for formation of RNA transport granules in Xenopus oocytes
por: Yang, Chao, et al.
Publicado: (2022)

Boric acid transport activity of marine teleost aquaporins expressed in Xenopus oocytes
por: Kumagai, Shiori, et al.
Publicado: (2023)

PATs and SNATs: Amino Acid Sensors in Disguise
por: Fan, Shih-Jung, et al.
Publicado: (2018)

The Effect of Nanoparticles on the Structure and Enzymatic Activity of Human Carbonic Anhydrase I and II
por: Cabaleiro-Lago, Celia, et al.
Publicado: (2020)

THE EFFECTS OF VINBLASTINE ON ISOLATED XENOPUS OOCYTES
por: Dumont, James N., et al.
Publicado: (1972)

Visualizing RNA Localization in Xenopus Oocytes
por: Gagnon, James A., et al.
Publicado: (2010)

In Vitro Reconstruction of Xenopus Oocyte Ovulation
por: Tokmakov, Alexander A., et al.
Publicado: (2019)

HPV16 E6 and E7 Oncoproteins Stimulate the Glutamine Pathway Maintaining Cell Proliferation in a SNAT1-Dependent Fashion
por: Ortiz-Pedraza, Yunuen, et al.
Publicado: (2023)

Carbonic anhydrase influences asymmetric sodium and acetate transport across omasum of sheep
por: Rabbani, Imtiaz, et al.
Publicado: (2021)

Conformational Change of H64 and Substrate Transportation: Insight Into a Full Picture of Enzymatic Hydration of CO(2) by Carbonic Anhydrase
por: Fu, Yuzhuang, et al.
Publicado: (2021)

The contribution of SNAT1 to system A amino acid transporter activity in human placental trophoblast
por: Desforges, M., et al.
Publicado: (2010)

Role of Amino Acid Transporter SNAT1/SLC38A1 in Human Melanoma
por: Böhme-Schäfer, Ines, et al.
Publicado: (2022)

Cannot write session to /tmp/vufind_sessions/sess_i49gpnt3oike5iorm6a441ubj8