| The solute carrier SLC7A1 may act as a protein transporter at the blood-brain barrier. | The solute carrier SLC7A1 may act as a protein transporter at the blood-brain barrier.
Kurtyka M, Wessely F, Bau S, Ifie E, He L, de Wit NM, Pedersen ABV, Keller M, Webber C, de Vries HE, Ansorge O, Betsholtz C, De Bock M, Chaves C, Brodin B, Nielsen MS, Neuhaus W, Bell RD, Letoha T, Meyer AH, Leparc G, Lenter M, Lesuisse D, Cader ZM, Buckley ST, Loryan I, Pietrzik CU. | 07/18/2024 |
| Cationic amino acid transporter-1 (CAT-1) promotes fibroblast-like synoviocyte proliferation and cytokine secretion by taking up L-arginine in rheumatoid arthritis. | Cationic amino acid transporter-1 (CAT-1) promotes fibroblast-like synoviocyte proliferation and cytokine secretion by taking up L-arginine in rheumatoid arthritis.
Lu Y, Hao C, Yu S, Ma Z, Fu X, Qin M, Ding M, Xu Z, Fan L., Free PMC Article | 10/22/2022 |
| Endothelial-specific overexpression of cationic amino acid transporter-1 prevents loss of kidney function in heart failure. | Endothelial-specific overexpression of cationic amino acid transporter-1 prevents loss of kidney function in heart failure.
Giam B, Nomura H, Kuruppu S, Chu PY, Essid S, Kiriazis H, Du XJ, Kaye DM, Rajapakse NW. | 03/28/2021 |
| A time-dependent decrease in serum and tissue ADMA and increase in mRNA expression of DDAH-1 and PRMT-1 as well as higher rates of mRNA expression of CAT-1 and lower rates of CAT-2A and CAT-2B were found after 8-week MCD diet. | MCD diet-induced steatohepatitis is associated with alterations in asymmetric dimethylarginine (ADMA) and its transporters.
Di Pasqua LG, Berardo C, Rizzo V, Richelmi P, Croce AC, Vairetti M, Ferrigno A. | 02/4/2017 |
| Endothelial CAT-1 overexpression can counter the ability of oxidative stress. | Endothelial cationic amino acid transporter-1 overexpression blunts the effects of oxidative stress on pressor responses to behavioural stress in mice.
Rajapakse NW, Konstantinidis G, Evans RG, Nguyen-Huu TP, Kaye DM, Head GA. | 08/22/2015 |
| L-argine transporters CAT-1 and CAT-2A expression and function are significantly increased in Duchenne muscular dystrophy mice. | Nitric oxide signalling pathway in Duchenne muscular dystrophy mice: up-regulation of L-arginine transporters.
Ramachandran J, Schneider JS, Crassous PA, Zheng R, Gonzalez JP, Xie LH, Beuve A, Fraidenraich D, Peluffo RD., Free PMC Article | 02/9/2013 |
| findings suggest a novel role for GRB2 in ecotropic MLV entry and infection by facilitating mCAT-1 trafficking | GRB2 interaction with the ecotropic murine leukemia virus receptor, mCAT-1, controls virus entry and is stimulated by virus binding.
Chen Z, Kolokoltsov AA, Wang J, Adhikary S, Lorinczi M, Elferink LA, Davey RA., Free PMC Article | 04/14/2012 |
| analysis of how a bifunctional intronic element regulates the expression of the arginine/lysine transporter Cat-1 via mechanisms involving the purine-rich element binding protein A (Pur alpha) | A bifunctional intronic element regulates the expression of the arginine/lysine transporter Cat-1 via mechanisms involving the purine-rich element binding protein A (Pur alpha).
Huang CC, Chiribau CB, Majumder M, Chiang CM, Wek RC, Kelm RJ Jr, Khalili K, Snider MD, Hatzoglou M., Free PMC Article | 01/21/2010 |
| Ecotropic mouse gammaretroviruses entry and virus-induced syncytium formation using the CAT-1 receptor are mediated by a small number of critical amino acid residues in receptor and virus Env. | Role of receptor polymorphism and glycosylation in syncytium induction and host range variation of ecotropic mouse gammaretroviruses.
Yan Y, Jung YT, Wu T, Kozak CA., Free PMC Article | 01/21/2010 |
| Ecotropic MuLV and its env protein downregulate the MuLV receptor (CAT1) via interaction of CAT1 with clathrin adaptor protein complexes. | Ecotropic murine leukemia virus envelope protein affects interaction of cationic amino acid transporter 1 with clathrin adaptor protein complexes, leading to receptor downregulation.
Fujisawa R, Masuda M. | 01/21/2010 |
| In a neuronal cell model, y+,L and y+ transport systems are the predominant form of arginine uptake mechanisms and the transport of arginine is altered by membrane potential and redox factors. | Y+ and y+ L arginine transporters in neuronal cells expressing tyrosine hydroxylase.
Bae SY, Xu Q, Hutchinson D, Colton CA. | 01/21/2010 |
| data suggest that direct interaction of eNOS with CAT-1 enhances NO release by a mechanism not involving arginine transport. | Interaction of the endothelial nitric oxide synthase with the CAT-1 arginine transporter enhances NO release by a mechanism not involving arginine transport.
Li C, Huang W, Harris MB, Goolsby JM, Venema RC., Free PMC Article | 01/21/2010 |