CATs and HATs: the SLC7 family of amino acid transporters

Abstract

The SLC7 family is divided into two subgroups, the cationic amino acid transporters (the CAT family, SLC7A1-4) and the glycoprotein-associated amino acid transporters (the gpaAT family,

Functional and molecular analysis of d-serine transport in retinal Müller cells

“…It was clear that Na + was essential for the uptake process, while Cl -was not. The requirement for Na + ruled out the Na + -independent transporters system asc (asc-1 and asc-2) and system L (LAT1 and LAT2) (reviewed in Verrey et al, 2004) as mediators of D-serine uptake in Müller cells. It was clear from our studies that the stoichiometry of D-serine uptake in the presence of Na + was 1:1.…”

Bioanalytical profile of the l-arginine/nitric oxide pathway and its evaluation by capillary electrophoresis

“…L-Arginine has been shown to be a key or preferable substrate in several reminiscent mammalian transport systems, including system y + and in the fewer capacity systems b 0,+ , B 0,+ , B 0 , and y +,L [40,104]. Most of these transport systems have been identified in a tight alliance with elevated synthesis of NO belong to SLC7 family (HUGO; phylogenetically-driven Solute Carrier Family nomenclature) [105], except for the sodiumdependent B 0,+ [106,107] which represents a unique mammalian member A14 of the sodium neurotransmitter symporter family (SNF, SLC6A14). Three transporters comprising a cationic amino acid transporters subfamily of SLC7, CAT (member SLC7A1-A4), are considered as high-capacitance essential substrate providers for normal NOS activity in different tissues [42].…”

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

“…Functional expression of LAT1 in the plasma membrane requires an additional single transmembrane glycoprotein known as 4F2 antigen or heavy chain and together these form a heterodimeric complex known as CD98. [8][9][10][11][12][13] The glycoprotein-associated transporters are a novel class of amino acid transporters recently the subject of much interest not only in relation to transport but also to CD98-linked functions in cell activation, integrin signaling, cell fusion and malignant transformation. [14][15][16][17] Our research has utilized a tetracycline-inducible adenoviral expression system (TET-Off) system to alter levels of LAT1 and 4F2 in vitro.…”

“…As the field has progressed, various terms have been used for cationic amino acid transporters and heterodimeric amino acid transporters. 8 We consistently use the terms LAT1 and 4F2 for the light and heavy chains of the CD98 complex in our study although TA1, 7 E16 7 and SLC7A5 8 have been utilized in previous research describing the CD98 light chain and CD98hc and SLC3A2 have also been used to describe the heavy chain. 8 Despite implications that LAT1 may represent an attractive clinical target for tumor and other pathological forms of cell proliferation, it is not yet known if specific modulation of LAT1, independent of CD98, may impact function.…”

“…8 We consistently use the terms LAT1 and 4F2 for the light and heavy chains of the CD98 complex in our study although TA1, 7 E16 7 and SLC7A5 8 have been utilized in previous research describing the CD98 light chain and CD98hc and SLC3A2 have also been used to describe the heavy chain. 8 Despite implications that LAT1 may represent an attractive clinical target for tumor and other pathological forms of cell proliferation, it is not yet known if specific modulation of LAT1, independent of CD98, may impact function. Our current studies were designed to ask whether an inducible adenoviral expression system was effective in driving short term blocked expression and overexpression of LAT1 in an in vitro hepatic model and to relate such modulation to functional effects including transport and cell growth.…”