scholarly journals Expression Cloning of a Na+-independent Aromatic Amino Acid Transporter with Structural Similarity to H+/Monocarboxylate Transporters

2001 ◽  
Vol 276 (20) ◽  
pp. 17221-17228 ◽  
Author(s):  
Do Kyung Kim ◽  
Yoshikatsu Kanai ◽  
Arthit Chairoungdua ◽  
Hirotaka Matsuo ◽  
Seok Ho Cha ◽  
...  
Keyword(s):  
Amino Acid ◽  
Aromatic Amino Acid ◽  
Structural Similarity ◽  
Amino Acid Transporter ◽  
Expression Cloning ◽  
Monocarboxylate Transporters ◽  
Acid Transporter

scholarly journals Amino Acid Transporter LAT1 (SLC7A5) Mediates MeHg-Induced Oxidative Stress Defense in the Human Placental Cell Line HTR-8/SVneo

2021 ◽  
Vol 22 (4) ◽  
pp. 1707
Author(s):  
Sebastian Granitzer ◽  
Raimund Widhalm ◽  
Martin Forsthuber ◽  
Isabella Ellinger ◽  
Gernot Desoye ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Amino Acid ◽  
De Novo ◽  
Structural Similarity ◽  
Amino Acid Transporter ◽  
Cell Number ◽  
Mehg Exposure ◽  
Acid Transporter ◽  
And Oxidative Stress

The placental barrier can protect the fetus from contact with harmful substances. The potent neurotoxin methylmercury (MeHg), however, is very efficiently transported across the placenta. Our previous data suggested that L-type amino acid transporter (LAT)1 is involved in placental MeHg uptake, accepting MeHg-L-cysteine conjugates as substrate due to structural similarity to methionine. The aim of the present study was to investigate the antioxidant defense of placental cells to MeHg exposure and the role of LAT1 in this response. When trophoblast-derived HTR-8/SVneo cells were LAT1 depleted by siRNA-mediated knockdown, they accumulated less MeHg. However, they were more susceptible to MeHg-induced toxicity. This was evidenced in decreased cell viability at a usually noncytotoxic concentration of 0.03 µM MeHg (~6 µg/L). Treatment with ≥0.3 µM MeHg increased cytotoxicity, apoptosis rate, and oxidative stress of HTR-8/SVneo cells. These effects were enhanced under LAT1 knockdown. Reduced cell number was seen when MeHg-exposed cells were cultured in medium low in cysteine, a constituent of the tripeptide glutathione (GSH). Because LAT1-deficient HTR-8/SVneo cells have lower GSH levels than control cells (independent of MeHg treatment), we conclude that LAT1 is essential for de novo synthesis of GSH, required to counteract oxidative stress. Genetic predisposition to decreased LAT1 function combined with MeHg exposure could increase the risk of placental damage.

scholarly journals Functional analysis of human aromatic amino acid transporter MCT10/TAT1 using the yeast Saccharomyces cerevisiae

2017 ◽  
Vol 1859 (10) ◽  
pp. 2076-2085 ◽  
Author(s):  
Satoshi Uemura ◽  
Takahiro Mochizuki ◽  
Goyu Kurosaka ◽  
Takanori Hashimoto ◽  
Yuki Masukawa ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Functional Analysis ◽  
Amino Acid ◽  
Aromatic Amino Acid ◽  
Amino Acid Transporter ◽  
Yeast Saccharomyces Cerevisiae ◽  
Acid Transporter

scholarly journals Dietary homeostasis challenge in mice lacking aromatic amino acid transporter TAT1/Slc16a10

2011 ◽  
Vol 25 (S1) ◽  
Author(s):  
Luca Mariotta ◽  
Tamara Ramadan ◽  
Dustin Singer ◽  
Simone MR Camargo ◽  
François Verrey
Keyword(s):  
Amino Acid ◽  
Aromatic Amino Acid ◽  
Amino Acid Transporter ◽  
Acid Transporter

Basolateral aromatic amino acid transporter TAT1 (Slc16a10) functions as an efflux pathway

2005 ◽  
Vol 206 (3) ◽  
pp. 771-779 ◽  
Author(s):  
Tamara Ramadan ◽  
Simone M.R. Camargo ◽  
Vanessa Summa ◽  
Peter Hunziker ◽  
Serge Chesnov ◽  
...  
Keyword(s):  
Amino Acid ◽  
Aromatic Amino Acid ◽  
Amino Acid Transporter ◽  
Acid Transporter ◽  
Efflux Pathway

scholarly journals Aromatic Amino Acid Transporter AAT-9 ofCaenorhabditis elegansLocalizes to Neurons and Muscle Cells

2004 ◽  
Vol 279 (47) ◽  
pp. 49268-49273 ◽  
Author(s):  
Emilija Veljkovic ◽  
Andrea Bacconi ◽  
Attila Stetak ◽  
Alex Hajnal ◽  
Susan Stasiuk ◽  
...  
Keyword(s):  
Amino Acid ◽  
Aromatic Amino Acid ◽  
Muscle Cells ◽  
Amino Acid Transporter ◽  
Acid Transporter

scholarly journals Aromatic Amino Acid Auxotrophs Constructed by Recombinant Marker Exchange in Methylophilus methylotrophus AS1 Cells Expressing the aroP-Encoded Transporter of Escherichia coli

2009 ◽  
Vol 76 (1) ◽  
pp. 75-83 ◽  
Author(s):  
Yurgis A. V. Yomantas ◽  
Irina L. Tokmakova ◽  
Natalya V. Gorshkova ◽  
Elena G. Abalakina ◽  
Svetlana M. Kazakova ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acids ◽  
Amino Acid ◽  
Aromatic Amino Acid ◽  
Target Genes ◽  
Aromatic Amino Acids ◽  
Amino Acid Transporter ◽  
Methylotrophic Bacteria ◽  
Methylophilus Methylotrophus ◽  
Acid Transporter

ABSTRACT The isolation of auxotrophic mutants, which is a prerequisite for a substantial genetic analysis and metabolic engineering of obligate methylotrophs, remains a rather complicated task. We describe a novel method of constructing mutants of the bacterium Methylophilus methylotrophus AS1 that are auxotrophic for aromatic amino acids. The procedure begins with the Mu-driven integration of the Escherichia coli gene aroP, which encodes the common aromatic amino acid transporter, into the genome of M. methylotrophus. The resulting recombinant strain, with improved permeability to certain amino acids and their analogues, was used for mutagenesis. Mutagenesis was carried out by recombinant substitution of the target genes in the chromosome by linear DNA using the FLP-excisable marker flanked with cloned homologous arms longer than 1,000 bp. M. methylotrophus AS1 genes trpE, tyrA, pheA, and aroG were cloned in E. coli, sequenced, disrupted in vitro using a Kmr marker, and electroporated into an aroP carrier recipient strain. This approach led to the construction of a set of marker-less M. methylotrophus AS1 mutants auxotrophic for aromatic amino acids. Thus, introduction of foreign amino acid transporter genes appeared promising for the following isolation of desired auxotrophs on the basis of different methylotrophic bacteria.

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