Identification of Three Cationic Amino Acid Transporters in Placental Trophoblast: Cloning, Expression, and Characterization of hCAT-1

1999 ◽  
Vol 171 (1) ◽  
pp. 55-62 ◽  
Author(s):  
S.G. Kamath ◽  
T.C. Furesz ◽  
B.A. Way ◽  
C.H. Smith
Keyword(s):  
Amino Acid ◽  
Amino Acid Transporters ◽  
Cationic Amino Acid

Characterization of cationic amino acid transporters (hCATs) 1 and 2 in human skin

2008 ◽  
Vol 129 (3) ◽  
pp. 321-329 ◽  
Author(s):  
Kristin Jaeger ◽  
Friedrich Paulsen ◽  
Johannes Wohlrab
Keyword(s):  
Amino Acid ◽  
Human Skin ◽  
Amino Acid Transporters ◽  
Cationic Amino Acid

Real-time functional characterization of cationic amino acid transporters using a new FRET sensor

2015 ◽  
Vol 468 (4) ◽  
pp. 563-572 ◽  
Author(s):  
Liviu Vanoaica ◽  
Alok Behera ◽  
Simone M. R. Camargo ◽  
Ian C. Forster ◽  
François Verrey
Keyword(s):  
Amino Acid ◽  
Real Time ◽  
Functional Characterization ◽  
Amino Acid Transporters ◽  
Cationic Amino Acid

Identification and characterization of cationic amino acid transporters (CATs) in tea plant (Camellia sinensis)

2017 ◽  
Vol 84 (1) ◽  
pp. 57-69 ◽  
Author(s):  
Lin Feng ◽  
Tianyuan Yang ◽  
Zhaoliang Zhang ◽  
Fangdong Li ◽  
Qi Chen ◽  
...  
Keyword(s):  
Amino Acid ◽  
Camellia Sinensis ◽  
Tea Plant ◽  
Amino Acid Transporters ◽  
Cationic Amino Acid ◽  
Identification And Characterization

Na(+)-independent transport (uniport) of amino acids and glucose in mammalian cells.

1994 ◽  
Vol 196 (1) ◽  
pp. 93-108
Author(s):  
D K Kakuda ◽  
C L MacLeod
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Mammalian Cells ◽  
Glucose Transporter ◽  
Sequence Similarity ◽  
Amino Acid Sequence Similarity ◽  
Amino Acid Transporters ◽  
Cationic Amino Acid ◽  
Transporter Family ◽  
Share Amino Acid Sequence

Recent advances have made possible the isolation of the genes and their cDNAs encoding Na(+)-independent amino acid transporters. Two classes of amino acid 'uniporters' have been isolated. One class contains the mCAT (murine cationic amino acid transporter) gene family that encodes proteins predicted to span the membrane 12-14 times and exhibits structural properties similar to the GLUT (glucose transporter) family and to other well-known transporters. The other class consists of two known genes, rBAT (related to B system amino acid transporters) and 4F2hc, that share amino acid sequence similarity with alpha-amylases and alpha-glucosidases. They are type II glycoproteins predicted to span the membrane only once, yet they mediate the Na(+)-independent transport of cationic and zwitterionic amino acids in Xenopus oocytes. Mutations in the human rBAT gene have been identified by Palacín and his co-workers in several families suffering from a heritable form of cystinuria. This important finding clearly establishes a key role for rBAT in cystine transport. The two classes of amino acid transporters are compared with the well-studied GLUT family of Na(+)-independent glucose transporters.

scholarly journals Nitric oxide can acutely modulate its biosynthesis through a negative feedback mechanism on l-arginine transport in cardiac myocytes

2010 ◽  
Vol 299 (2) ◽  
pp. C230-C239 ◽  
Author(s):  
Jiaguo Zhou ◽  
David D. Kim ◽  
R. Daniel Peluffo
Keyword(s):  
Nitric Oxide ◽  
Amino Acid ◽  
Cardiac Myocytes ◽  
Amino Acid Transporters ◽  
No Production ◽  
Cardiac Muscle Cells ◽  
No Donor ◽  
Rat Cardiomyocytes ◽  
Cationic Amino Acid ◽  
Intervention Point

Nitric oxide (NO) plays a central role as a cellular signaling molecule in health and disease. In the heart, NO decreases the rate of spontaneous beating and the velocity and extent of shortening and accelerates the velocity of relengthening. Since the cationic amino acid l-arginine (l-Arg) is the substrate for NO production by NO synthases (NOS), we tested whether the transporters that mediate l-Arg import in cardiac muscle cells represent an intervention point in the regulation of NO synthesis. Electrical currents activated by l-Arg with low apparent affinity in whole cell voltage-clamped rat cardiomyocytes were found to be rapidly and reversibly inhibited by NO donors. Radiotracer uptake studies performed on cardiac sarcolemmal vesicles revealed the presence of high-affinity/low-capacity and low-affinity/high-capacity components of cationic amino acid transport that were inhibited by the NO donor S-nitroso- N-acetyl-dl-penicillamine. NO inhibited uptake in a noncompetitive manner with Ki values of 275 and 827 nM for the high- and low-affinity component, respectively. Fluorescence spectroscopy experiments showed that millimolar concentrations of l-Arg initially promoted and then inhibited the release of endogenous NO in cardiomyocytes. Likewise, l-Arg currents measured in cardiac myocytes voltage clamped in the presence of 460 nM free intracellular Ca2+, a condition in which a Ca-CaM complex should activate endogenous NO production, showed fast activation followed by inhibition of l-Arg transport. The NOS inhibitor N-nitro-l-arginine methyl ester, but not blockers of downstream reactions, specifically removed this inhibitory component. These results demonstrate that NO acutely regulates its own biosynthesis by modulating the availability of l-Arg via cationic amino acid transporters.

Sign in / Sign up

Export Citation Format

Share Document