scholarly journals Tissue-Specific Amino Acid Transporter Partners ACE2 and Collectrin Differentially Interact With Hartnup Mutations

2009 ◽  
Vol 136 (3) ◽  
pp. 872-882.e3 ◽  
Author(s):  
Simone M.R. Camargo ◽  
Dustin Singer ◽  
Victoria Makrides ◽  
Katja Huggel ◽  
Klaas M. Pos ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Transporter ◽  
Specific Amino Acid ◽  
Tissue Specific ◽  
Acid Transporter

scholarly journals Uteroplacental Insufficiency Alters Gene Expression of Amino Acid Transporter LAT1 in a Tissue-Specific Manner in IUGR Fetal Rats

1999 ◽  
Vol 45 (4, Part 2 of 2) ◽  
pp. 285A-285A
Author(s):  
Jennifer L Kloesz ◽  
Elisa M Gruetzmacher ◽  
Anna E Tsirka ◽  
Robert H Lane
Keyword(s):  
Gene Expression ◽  
Amino Acid ◽  
Amino Acid Transporter ◽  
Tissue Specific ◽  
Fetal Rats ◽  
Specific Manner ◽  
Acid Transporter

scholarly journals Tadr Is an Axonal Histidine Transporter Required for Visual Neurotransmission in Drosophila

2021 ◽  
Author(s):  
Yongchao Han ◽  
Lei Peng ◽  
Tao Wang
Keyword(s):  
Amino Acid ◽  
Synaptic Transmission ◽  
Histidine Decarboxylase ◽  
De Novo ◽  
Critical Role ◽  
Amino Acid Transporter ◽  
Monoamine Neurotransmitter ◽  
Monoamine Neurotransmitters ◽  
Specific Amino Acid ◽  
Acid Transporter

AbstractNeurotransmitters are generated by de novo synthesis and are essential for sustained, high-frequency synaptic transmission. Histamine, a monoamine neurotransmitter, is synthesized through decarboxylation of histidine by Histidine decarboxylase (Hdc). However, little is known about how histidine is presented to Hdc as a precursor. Here, we identified a specific histidine transporter, TADR (Torn And Diminished Rhabdomeres), that is required for visual transmission in Drosophila. TADR and Hdc co-localized to neuronal terminals, and mutations in tadr reduced levels of histamine, thus disrupting visual synaptic transmission and phototaxis behavior. These results demonstrate that a specific amino acid transporter provides precursors for monoamine neurotransmitters, providing the first genetic evidence that a histidine amino acid transporter plays a critical role in synaptic transmission. These results suggest that TADR-dependent local de novo synthesis of histamine is required for synaptic transmission.

scholarly journals The Arabidopsis L-Type Amino Acid Transporter 5 (LAT5/PUT5) Is Expressed in the Phloem and Alters Seed Nitrogen Content When Knocked Out

Plants ◽  
2020 ◽  
Vol 9 (11) ◽  
pp. 1519
Author(s):  
Rowshon A. Begam ◽  
Jayne D’Entremont ◽  
Allen Good
Keyword(s):  
Amino Acid ◽  
Nitrogen Content ◽  
Amino Acid Transport ◽  
Amino Acid Transporter ◽  
Acid Transport ◽  
Specific Expression ◽  
Tissue Specific ◽  
Tissue Specific Expression ◽  
Wide Range ◽  
Acid Transporter

The Arabidopsis L-type Amino Acid Transporter-5 (LAT5; At3g19553) was recently studied for its role in developmental responses such as flowering and senescence, under an assumption that it is a polyamine uptake transporter (PUT5). The LATs in Arabidopsis have a wide range of substrates, including amino acids and polyamines. This report extensively studied the organ and tissue-specific expression of the LAT5/PUT5 and investigated its role in mediating amino acid transport. Organ-specific quantitative RT-PCR detected LAT5/PUT5 transcripts in all organs with a relatively higher abundance in the leaves. Tissue-specific expression analysis identified GUS activity in the phloem under the LAT5/PUT5 promoter. In silico analysis identified both amino acid transporter and antiporter domains conserved in the LAT5/PUT5 protein. The physiological role of the LAT5/PUT5 was studied through analyzing a mutant line, lat5-1, under various growth conditions. The mutant lat5-1 seedlings showed increased sensitivity to exogenous leucine in Murashige and Skoog growth medium. In soil, the lat5-1 showed reduced leaf growth and altered nitrogen content in the seeds. In planta radio-labelled leucine uptake studies showed increased accumulation of leucine in the lat5-1 plants compared to the wild type when treated in the dark prior to the isotopic feeding. These studies suggest that LAT5/PUT5 plays a role in mediating amino acid transport.

Increased expression of an amino acid transporter LAT1 in healing of acetic acid-induced chronic gastric ulcer in rats

2001 ◽  
Vol 120 (5) ◽  
pp. A153-A153
Author(s):  
S MIYAMOTO ◽  
K KATO ◽  
Y ISHII ◽  
S ASAI ◽  
T NAGAISHI ◽  
...  
Keyword(s):  
Acetic Acid ◽  
Gastric Ulcer ◽  
Amino Acid ◽  
Amino Acid Transporter ◽  
Chronic Gastric Ulcer ◽  
Acid Transporter

scholarly journals Identification and Characterization of Inhibitors of a Neutral Amino Acid Transporter, SLC6A19, Using Two Functional Cell-Based Assays

2018 ◽  
Vol 24 (2) ◽  
pp. 111-120 ◽  
Author(s):  
Sanjay J. Danthi ◽  
Beirong Liang ◽  
Oanh Smicker ◽  
Benjamin Coupland ◽  
Jill Gregory ◽  
...  
Keyword(s):  
Amino Acid ◽  
High Throughput Screening ◽  
Amino Acid Transporter ◽  
Neutral Amino Acid ◽  
Imaging Plate ◽  
Acid Uptake ◽  
Functional Assays ◽  
Neutral Amino Acid Transporter ◽  
Acid Transporter ◽  
Pharmacologically Active

SLC6A19 (B0AT1) is a neutral amino acid transporter, the loss of function of which results in Hartnup disease. SLC6A19 is also believed to have an important role in amino acid homeostasis, diabetes, and weight control. A small-molecule inhibitor of human SLC6A19 (hSLC6A19) was identified using two functional cell-based assays: a fluorescence imaging plate reader (FLIPR) membrane potential (FMP) assay and a stable isotope-labeled neutral amino acid uptake assay. A diverse collection of 3440 pharmacologically active compounds from the Microsource Spectrum and Tocriscreen collections were tested at 10 µM in both assays using MDCK cells stably expressing hSLC6A19 and its obligatory subunit, TMEM27. Compounds that inhibited SLC6A19 activity in both assays were further confirmed for activity and selectivity and characterized for potency in functional assays against hSLC6A19 and related transporters. A single compound, cinromide, was found to robustly, selectively, and reproducibly inhibit SLC6A19 in all functional assays. Structurally related analogs of cinromide were tested to demonstrate structure–activity relationship (SAR). The assays described here are suitable for carrying out high-throughput screening campaigns to identify modulators of SLC6A19.

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