scholarly journals Adenoviral modulation of the tumor-associated system L amino acid transporter, LAT1, alters amino acid transport, cell growth and 4F2/CD98 expressionwith cell-type specific effects in cultured hepatic cells

2005 ◽  
Vol 117 (3) ◽  
pp. 387-397 ◽  
Author(s):  
Bill T. Storey ◽  
Celine Fugere ◽  
Anne Lesieur-Brooks ◽  
Charles Vaslet ◽  
Nancy L. Thompson
Keyword(s):  
Amino Acid ◽  
Cell Growth ◽  
Amino Acid Transport ◽  
Amino Acid Transporter ◽  
Acid Transport ◽  
Cell Type ◽  
Hepatic Cells ◽  
Specific Effects ◽  
System L ◽  
Cell Type Specific

scholarly journals A rapid method for the functional reconstitution of amino acid transport systems from rat liver plasma membranes. Partial purification of System A

1988 ◽  
Vol 255 (3) ◽  
pp. 963-969 ◽  
Author(s):  
A R Quesada ◽  
J D McGivan
Keyword(s):  
Amino Acid ◽  
Rapid Method ◽  
Amino Acid Transport ◽  
Plasma Membranes ◽  
Transport Systems ◽  
Partial Purification ◽  
Acid Transport ◽  
Transport Activity ◽  
System A ◽  
System L

A rapid method for the functional reconstruction of amino acid transport from liver plasma-membrane vesicles using the neutral detergent decanoyl-N-glucamide (‘MEGA-10’) is described. The method is a modification of that previously employed in this laboratory for reconstitution of amino acid transport systems from kidney brush-border membranes [Lynch & McGivan (1987) Biochem. J. 244, 503-508]. The transport activities termed ‘System A’, ‘System N’, and ‘System L’ are all reconstituted. The reconstitution procedure is rapid and efficient and is suitable as an assay for transport activity in studies involving membrane fractionation. By using this reconstitution procedure, System A transport activity was partially purified by lectin-affinity chromatography.

Expression and regulation of 4F2hc and hLAT1 in human trophoblasts

2002 ◽  
Vol 282 (1) ◽  
pp. C196-C204 ◽  
Author(s):  
Yoko Okamoto ◽  
Masahiro Sakata ◽  
Kazuhiro Ogura ◽  
Toshiya Yamamoto ◽  
Masaaki Yamaguchi ◽  
...  
Keyword(s):  
Amino Acid ◽  
Cell Line ◽  
Transport System ◽  
Human Placenta ◽  
Amino Acid Transport ◽  
Calcium Ionophore ◽  
Acid Transport ◽  
Amino Acid Transport System ◽  
System L ◽  
Choriocarcinoma Cell Line

The neutral amino acid transport system L is a sodium-independent transport system in human placenta and choriocarcinoma cells. Recently, it was found that the heterodimer composed of hLAT1 (a light-chain protein) and 4F2 heavy chain (4F2hc), a type II transmembrane glycoprotein, is responsible for system L amino acid transport. We found that the mRNAs of 4F2hc and hLAT1 were expressed in the human placenta and a human choriocarcinoma cell line. The levels of the 4F2hc and hLAT1 proteins in the human placenta increased at full term compared with those at midtrimester. Immunohistochemical data showed that these proteins were localized mainly in the placental apical membrane. Data from leucine uptake experiments, Northern blot analysis, and immunoblot analysis showed that this transport system was partially regulated by protein kinase C and calcium ionophore in the human choriocarcinoma cell line. Our results suggest that the heterodimer of 4F2hc and hLAT1 may play an important role in placental amino acid transport system L.

Regulation of system L amino acid transport byTetrahymena thermophilia

1986 ◽  
Vol 156 (6) ◽  
pp. 891-895 ◽  
Author(s):  
James P. Davis ◽  
G. C. Stephens
Keyword(s):  
Amino Acid ◽  
Amino Acid Transport ◽  
Acid Transport ◽  
System L

scholarly journals Soy-dairy protein blend and whey protein ingestion after resistance exercise increases amino acid transport and transporter expression in human skeletal muscle

2014 ◽  
Vol 116 (11) ◽  
pp. 1353-1364 ◽  
Author(s):  
P. T. Reidy ◽  
D. K. Walker ◽  
J. M. Dickinson ◽  
D. M. Gundermann ◽  
M. J. Drummond ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Amino Acid ◽  
Whey Protein ◽  
Amino Acid Transport ◽  
Amino Acid Transporter ◽  
Acid Transport ◽  
Amino Acid Availability ◽  
Acid Transporter ◽  
Dairy Protein ◽  
Myofibrillar Protein Synthesis

Increasing amino acid availability (via infusion or ingestion) at rest or postexercise enhances amino acid transport into human skeletal muscle. It is unknown whether alterations in amino acid availability, from ingesting different dietary proteins, can enhance amino acid transport rates and amino acid transporter (AAT) mRNA expression. We hypothesized that the prolonged hyperaminoacidemia from ingesting a blend of proteins with different digestion rates postexercise would enhance amino acid transport into muscle and AAT expression compared with the ingestion of a rapidly digested protein. In a double-blind, randomized clinical trial, we studied 16 young adults at rest and after acute resistance exercise coupled with postexercise (1 h) ingestion of either a (soy-dairy) protein blend or whey protein. Phenylalanine net balance and transport rate into skeletal muscle were measured using stable isotopic methods in combination with femoral arteriovenous blood sampling and muscle biopsies obtained at rest and 3 and 5 h postexercise. Phenylalanine transport into muscle and mRNA expression of select AATs [system L amino acid transporter 1/solute-linked carrier (SLC) 7A5, CD98/SLC3A2, system A amino acid transporter 2/SLC38A2, proton-assisted amino acid transporter 1/SLC36A1, cationic amino acid transporter 1/SLC7A1] increased to a similar extent in both groups ( P < 0.05). However, the ingestion of the protein blend resulted in a prolonged and positive net phenylalanine balance during postexercise recovery compared with whey protein ( P < 0.05). Postexercise myofibrillar protein synthesis increased similarly between groups. We conclude that, while both protein sources enhanced postexercise AAT expression, transport into muscle, and myofibrillar protein synthesis, postexercise ingestion of a protein blend results in a slightly prolonged net amino acid balance across the leg compared with whey protein.

scholarly journals Monoterpene Glycoside ESK246 from Pittosporum Targets LAT3 Amino Acid Transport and Prostate Cancer Cell Growth

2014 ◽  
Vol 9 (6) ◽  
pp. 1369-1376 ◽  
Author(s):  
Qian Wang ◽  
Tanja Grkovic ◽  
Josep Font ◽  
Sarah Bonham ◽  
Rebecca H Pouwer ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Amino Acid ◽  
Cell Growth ◽  
Cancer Cell ◽  
Amino Acid Transport ◽  
Prostate Cancer Cell ◽  
Acid Transport ◽  
Cancer Cell Growth ◽  
Monoterpene Glycoside

scholarly journals Expression of the surface antigen 4F2hc affects system-L-like neutral-amino-acid-transport activity in mammalian cells

1997 ◽  
Vol 324 (2) ◽  
pp. 535-541 ◽  
Author(s):  
Stefan BRÖER ◽  
Angelika BRÖER ◽  
Bernd HAMPRECHT
Keyword(s):  
Amino Acid ◽  
Surface Antigen ◽  
Amino Acid Transport ◽  
Cho Cells ◽  
Mammalian Cells ◽  
Primary Cultures ◽  
Transport Systems ◽  
Acid Transport ◽  
Transport Activity ◽  
System L

Mammalian cells possess a variety of amino acid-transport systems with overlapping substrate specificity. System L is one of the major amino acid-transport systems of non-epithelial cells. By expression cloning we have recently demonstrated that the surface antigen 4F2hc (CD98) is a necessary component for expression of system-L-like amino acid-transport activity in C6-BU-1 rat glioma cells [Bröer, Bröer and Hamprecht (1995) Biochem. J. 312, 863–870]. 4F2hc mRNA was detected in CHO cells, COS cells, activated lymphocytes isolated from mouse spleen and primary cultures of astrocytes. In all these cell types, Na+-independent isoleucine transport was mediated by system L. No contribution of system y+L to isoleucine or arginine transport was detected in C6-BU-1 cells. In lymphocytes, both system-L-like amino acid-transport activity and 4F2hc mRNA levels increased after treatment with phorbol ester plus ionomycin. Antisense oligonucleotides caused modest inhibition of Na+-independent isoleucine transport in C6-BU-1 cells and primary cultures of astroglial cells, whereas arginine transport was unaffected. Overexpression of 4F2hc cDNA in CHO cells resulted in an increase in Na+-independent isoleucine transport.

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