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• W2140549895 abstract "The regulation of the high affinity cationic amino acid transporter Cat-1 in Fao rat hepatoma cells by amino acid availability has been studied. Cat-1 mRNA level increased (3-fold) in 4 h in response to amino acid starvation and remained high for at least 24 h. This induction was independent of the presence of serum in the media and transcription and protein synthesis were required for induction to occur. When Fao cells were shifted from amino acid-depleted media to amino acid-fed media, the levels of the induced cat-1 mRNA returned to the basal level. In amino acid-fed cells, accumulation of cat-1mRNA was dependent on protein synthesis, indicating that a labile protein is required to sustain cat-1 mRNA level. No change in the transcription rate of the cat-1 gene during amino acid starvation was observed, indicating thatcat-1 is regulated at a post-transcriptional step. System y+ mediated transport of arginine was reduced by 50% in 1 h and by 70% in 24 h after amino acid starvation. However, when 24-h amino acid-starved Fao cells were preloaded with 2 mmlysine or arginine for 1 h prior to the transport assays, arginine uptake was trans-stimulated by 5-fold. This stimulation was specific for cationic amino acids, since alanine, proline, or leucine had no effect. These data lead to the hypothesis that amino acid starvation results in an increased cat-1 mRNA level to support synthesis of additional Cat-1 protein. The following lines of evidence support the hypothesis: (i) the use of inhibitors of protein synthesis in starved cells inhibits the trans-zero transport of arginine; (ii) cells starved for 1–24 h exhibited an increase of trans-stimulated arginine transport activity for the first 6 h and had no loss of activity at 24 h, suggesting that constant replenishment of the transporter protein occurs; (iii) immunofluorescent staining of 24-h fed and starved cells for cat-1 showed similar cell surface distribution; (iv) new protein synthesis is not required for trans-stimulation of arginine transport upon refeeding of 24-h starved cells. We conclude that the increased level of cat-1 mRNA in response to amino acid starvation support the synthesis of Cat-1 protein during starvation and increased amino acid transport upon substrate presentation. Therefore, the cat-1 mRNA content is regulated by a derepression/repression mechanism in response to amino acid availability. We propose that the amino acid-signal transduction pathway consists of a series of steps which include the post-transcriptional regulation of amino acid transporter genes. The regulation of the high affinity cationic amino acid transporter Cat-1 in Fao rat hepatoma cells by amino acid availability has been studied. Cat-1 mRNA level increased (3-fold) in 4 h in response to amino acid starvation and remained high for at least 24 h. This induction was independent of the presence of serum in the media and transcription and protein synthesis were required for induction to occur. When Fao cells were shifted from amino acid-depleted media to amino acid-fed media, the levels of the induced cat-1 mRNA returned to the basal level. In amino acid-fed cells, accumulation of cat-1mRNA was dependent on protein synthesis, indicating that a labile protein is required to sustain cat-1 mRNA level. No change in the transcription rate of the cat-1 gene during amino acid starvation was observed, indicating thatcat-1 is regulated at a post-transcriptional step. System y+ mediated transport of arginine was reduced by 50% in 1 h and by 70% in 24 h after amino acid starvation. However, when 24-h amino acid-starved Fao cells were preloaded with 2 mmlysine or arginine for 1 h prior to the transport assays, arginine uptake was trans-stimulated by 5-fold. This stimulation was specific for cationic amino acids, since alanine, proline, or leucine had no effect. These data lead to the hypothesis that amino acid starvation results in an increased cat-1 mRNA level to support synthesis of additional Cat-1 protein. The following lines of evidence support the hypothesis: (i) the use of inhibitors of protein synthesis in starved cells inhibits the trans-zero transport of arginine; (ii) cells starved for 1–24 h exhibited an increase of trans-stimulated arginine transport activity for the first 6 h and had no loss of activity at 24 h, suggesting that constant replenishment of the transporter protein occurs; (iii) immunofluorescent staining of 24-h fed and starved cells for cat-1 showed similar cell surface distribution; (iv) new protein synthesis is not required for trans-stimulation of arginine transport upon refeeding of 24-h starved cells. We conclude that the increased level of cat-1 mRNA in response to amino acid starvation support the synthesis of Cat-1 protein during starvation and increased amino acid transport upon substrate presentation. Therefore, the cat-1 mRNA content is regulated by a derepression/repression mechanism in response to amino acid availability. We propose that the amino acid-signal transduction pathway consists of a series of steps which include the post-transcriptional regulation of amino acid transporter genes. The signal(s) that initiate the molecular response to amino acid starvation and the mechanism of selectively increasing gene expression in mammalian cells are not known. Unlike mammalian cells, bacterial and yeast cells have the ability to compensate for the effects of amino acid starvation by inducing enzymes that promote de novoamino acid biosynthesis (1Hinnebusch A.G. Microbiol. Rev. 1988; 52: 248-273Crossref PubMed Google Scholar, 2Hope I.A. Struhl K. Cell. 1985; 43: 177-188Abstract Full Text PDF PubMed Scopus (265) Google Scholar, 3Abastado J.P. Miller P.F. Jackson B.M. Hinnebusch A.G. Mol. Cell. Biol. 1991; 11: 486-496Crossref PubMed Scopus (165) Google Scholar). In yeast, a specific protein (GCN4) compensates for amino acid starvation by activating the transcription of a group of genes encoding enzymes involved in amino acid biosynthesis (2Hope I.A. Struhl K. Cell. 1985; 43: 177-188Abstract Full Text PDF PubMed Scopus (265) Google Scholar). When yeast cells are grown in nutritionally complete medium the rate of translation of GCN4 is extremely low, but its translation is specifically enhanced in response to amino acid starvation. It has been suggested (4Kilberg M.S. Hutson R.G. Laine R.O. FASEB J. 1994; 8: 13-19Crossref PubMed Scopus (90) Google Scholar) that mammalian cells have a similar general control mechanism in response to amino acid starvation for genes which are involved in different aspects of amino acid metabolism (4Kilberg M.S. Hutson R.G. Laine R.O. FASEB J. 1994; 8: 13-19Crossref PubMed Scopus (90) Google Scholar, 5Laine R.O. Hutson R.H. Kilberg M.S. Prog. Nucleic Acid Res. Mol. Biol. 1996; 53: 219-248Crossref PubMed Scopus (29) Google Scholar, 6Guerrini L. Gong S.S. Mangasarian K. Basilico C. Mol. Cell. Biol. 1993; 13: 3202-3212Crossref PubMed Scopus (88) Google Scholar, 7Gong S.S. Guerrini L. Basilico C. Mol. Cell. Biol. 1991; 11: 6059-6066Crossref PubMed Scopus (81) Google Scholar, 8Hutson R.G. Kilberg M.S. Biochem. J. 1994; 304: 745-750Crossref PubMed Scopus (64) Google Scholar).It is clear that mammalian cells have mechanisms to respond to changes in amino acid availability (4Kilberg M.S. Hutson R.G. Laine R.O. FASEB J. 1994; 8: 13-19Crossref PubMed Scopus (90) Google Scholar, 5Laine R.O. Hutson R.H. Kilberg M.S. Prog. Nucleic Acid Res. Mol. Biol. 1996; 53: 219-248Crossref PubMed Scopus (29) Google Scholar). These mechanisms may involve the regulation of transcription, translation, and (or) mRNA stability (9Marten N.W. Burke E.J. Hayden J.M. Straus D.S. FASEB J. 1994; 8: 538-544Crossref PubMed Scopus (114) Google Scholar). However, there are very few studies of genes in which their synthesis is regulated by amino acid availability (9Marten N.W. Burke E.J. Hayden J.M. Straus D.S. FASEB J. 1994; 8: 538-544Crossref PubMed Scopus (114) Google Scholar). Positive and negative effects of amino acid limitation on mRNA levels of specific genes have been reported (9Marten N.W. Burke E.J. Hayden J.M. Straus D.S. FASEB J. 1994; 8: 538-544Crossref PubMed Scopus (114) Google Scholar). Specific examples of mRNAs or proteins for which synthesis is enhanced in response to amino acid deprivation include: serine dehydratase (10Ogawa H. Fujioka M. Su Y. Kanamoto R. Pitot H.C. J. Biol. Chem. 1991; 266: 20412-20417Abstract Full Text PDF PubMed Google Scholar); asparagine synthase (7Gong S.S. Guerrini L. Basilico C. Mol. Cell. Biol. 1991; 11: 6059-6066Crossref PubMed Scopus (81) Google Scholar); ornithine decarboxylase (11Chen Z.P. Chen K.Y. J. Biol. Chem. 1992; 267: 6946-6951Abstract Full Text PDF PubMed Google Scholar, 12Ponjanpelto P. Holtta E. Mol. Cell. Biol. 1990; 10: 5814-5821Crossref PubMed Scopus (48) Google Scholar); System A (13Bracy D.S. Handlogten M.E. Barber E.F. Han H.-P. Kilberg M.S. J. Biol. Chem. 1986; 261: 1514-1520Abstract Full Text PDF PubMed Google Scholar) and System L (14Shotwell M.A. Mattes P.M. Jayme D.W. Oxender D.L. J. Biol. Chem. 1982; 257: 2974-2980Abstract Full Text PDF PubMed Google Scholar) amino acid transport; IGFBP-1 (15Straus D.S. Burke E.J. Marten N.W. Endocrinology. 1993; 132: 1090-1100Crossref PubMed Scopus (82) Google Scholar); c-jun and c-myc(12Ponjanpelto P. Holtta E. Mol. Cell. Biol. 1990; 10: 5814-5821Crossref PubMed Scopus (48) Google Scholar); gadd153, b-actin, ubiquitin c, phosphoglycerate kinase, c/EBPa and c/EBPβ (9Marten N.W. Burke E.J. Hayden J.M. Straus D.S. FASEB J. 1994; 8: 538-544Crossref PubMed Scopus (114) Google Scholar); ribosomal protein L17 and S25 (16Laine R.O. Laipis P.J. Shay N.F. Kilberg M.S. J. Biol. Chem. 1991; 266: 16969-16972Abstract Full Text PDF PubMed Google Scholar, 17Laine R.O. Shay N.F. Kilberg M.S. J. Biol. Chem. 1994; 269: 9693-9697Abstract Full Text PDF PubMed Google Scholar).In mammals, dietary protein deficiency results in decreased levels of serum proteins including albumin (8Hutson R.G. Kilberg M.S. Biochem. J. 1994; 304: 745-750Crossref PubMed Scopus (64) Google Scholar). In the case of albumin, it has been suggested that the decreased protein and mRNA levels are mainly due to reduced mRNA stability (9Marten N.W. Burke E.J. Hayden J.M. Straus D.S. FASEB J. 1994; 8: 538-544Crossref PubMed Scopus (114) Google Scholar). For asparagine synthase, amino acid starvation increases the mRNA level, and this increase depends on de novo protein synthesis (4Kilberg M.S. Hutson R.G. Laine R.O. FASEB J. 1994; 8: 13-19Crossref PubMed Scopus (90) Google Scholar, 5Laine R.O. Hutson R.H. Kilberg M.S. Prog. Nucleic Acid Res. Mol. Biol. 1996; 53: 219-248Crossref PubMed Scopus (29) Google Scholar, 6Guerrini L. Gong S.S. Mangasarian K. Basilico C. Mol. Cell. Biol. 1993; 13: 3202-3212Crossref PubMed Scopus (88) Google Scholar, 7Gong S.S. Guerrini L. Basilico C. Mol. Cell. Biol. 1991; 11: 6059-6066Crossref PubMed Scopus (81) Google Scholar, 8Hutson R.G. Kilberg M.S. Biochem. J. 1994; 304: 745-750Crossref PubMed Scopus (64) Google Scholar).In conditions of decreased amino acid availability, it is expected that there will be a coordinate increase in catabolism of cellular proteins, amino acid biosynthesis, and amino acid transport across the plasma membrane to provide cells with sufficient amino acids for cell survival. Regulation of amino acid transport by amino acid availability has been described for System A. System A-mediated transport of neutral amino acids is induced by amino acid starvation (18Kilberg M.S. Trends Biochem. Sci. 1996; 2: 183-186Google Scholar) and this induction is sensitive to actinomycin D and cycloheximide. These studies support the concept of regulation of amino acid transport at a molecular level. Given that the gene for System A-mediated amino acid transporter has not been cloned, direct studies at a molecular level are not possible.Transport of cationic amino acids into most mammalian cells is mainly mediated through System y+. Three related proteins encoding y+-like activity have been isolated (Cat-1, Cat-2, and Cat-2a) (19Kakuda D.K. Finley K.D. Dionne V.E. MacLeod C.L. Transgene. 1993; 1: 91-101Google Scholar, 20Closs E.I. Lyons C.R. Kelly C. Cunningham J.M. J. Biol. Chem. 1993; 268: 20796-20800Abstract Full Text PDF PubMed Google Scholar). All three proteins function as transporters for the cationic amino acids arginine, lysine, and ornithine, but they differ in their affinity for substrate. Cat-1 and Cat-2 have a 10-fold higher affinity than Cat-2a (19Kakuda D.K. Finley K.D. Dionne V.E. MacLeod C.L. Transgene. 1993; 1: 91-101Google Scholar, 20Closs E.I. Lyons C.R. Kelly C. Cunningham J.M. J. Biol. Chem. 1993; 268: 20796-20800Abstract Full Text PDF PubMed Google Scholar). The biological significance of having multiple transporters for cationic amino acids in mammalian cells is not known. However, it has been suggested that these genes may be expressed and regulated in a cell-specific manner, thus facilitating amino acid transport in and out of mammalian cells in response to specific nutritional needs within a particular tissue (21Malandro M.S. Kilberg M.S. Annu. Rev. Biochem. 1996; 65: 305-336Crossref PubMed Scopus (180) Google Scholar). In this regard, the family of amino acid transporters for cationic substrates resembles the family of Na+-independent glucose transporters (22Kakuda D.K. MacLeod C.L. J. Exp. Biol. 1994; 196: 93-108PubMed Google Scholar).No molecular studies regarding adaptive regulation of System y+ to amino acid starvation have been published. Studies of amino acid deprivation in entire animals are not feasible, mainly because of the dramatic changes that occur in the circulating hormones, which regulate the expression of a variety of genes. Therefore, the use of in vitro systems is initially required to identify the regulatory signals for amino acid-dependent gene expression. As shown in this report, Fao cells are ideal to study the adaptive regulation of Cat-1-mediated transport because they do not express the Cat-2 and Cat-2a transporters. Here, we show that the regulation of thecat-1 gene in rat hepatoma Fao cells is responsive to amino acid deprivation and re-exposure to individual amino acids. The signal(s) that initiate the molecular response to amino acid starvation and the mechanism of selectively increasing gene expression in mammalian cells are not known. Unlike mammalian cells, bacterial and yeast cells have the ability to compensate for the effects of amino acid starvation by inducing enzymes that promote de novoamino acid biosynthesis (1Hinnebusch A.G. Microbiol. Rev. 1988; 52: 248-273Crossref PubMed Google Scholar, 2Hope I.A. Struhl K. Cell. 1985; 43: 177-188Abstract Full Text PDF PubMed Scopus (265) Google Scholar, 3Abastado J.P. Miller P.F. Jackson B.M. Hinnebusch A.G. Mol. Cell. Biol. 1991; 11: 486-496Crossref PubMed Scopus (165) Google Scholar). In yeast, a specific protein (GCN4) compensates for amino acid starvation by activating the transcription of a group of genes encoding enzymes involved in amino acid biosynthesis (2Hope I.A. Struhl K. Cell. 1985; 43: 177-188Abstract Full Text PDF PubMed Scopus (265) Google Scholar). When yeast cells are grown in nutritionally complete medium the rate of translation of GCN4 is extremely low, but its translation is specifically enhanced in response to amino acid starvation. It has been suggested (4Kilberg M.S. Hutson R.G. Laine R.O. FASEB J. 1994; 8: 13-19Crossref PubMed Scopus (90) Google Scholar) that mammalian cells have a similar general control mechanism in response to amino acid starvation for genes which are involved in different aspects of amino acid metabolism (4Kilberg M.S. Hutson R.G. Laine R.O. FASEB J. 1994; 8: 13-19Crossref PubMed Scopus (90) Google Scholar, 5Laine R.O. Hutson R.H. Kilberg M.S. Prog. Nucleic Acid Res. Mol. Biol. 1996; 53: 219-248Crossref PubMed Scopus (29) Google Scholar, 6Guerrini L. Gong S.S. Mangasarian K. Basilico C. Mol. Cell. Biol. 1993; 13: 3202-3212Crossref PubMed Scopus (88) Google Scholar, 7Gong S.S. Guerrini L. Basilico C. Mol. Cell. Biol. 1991; 11: 6059-6066Crossref PubMed Scopus (81) Google Scholar, 8Hutson R.G. Kilberg M.S. Biochem. J. 1994; 304: 745-750Crossref PubMed Scopus (64) Google Scholar). It is clear that mammalian cells have mechanisms to respond to changes in amino acid availability (4Kilberg M.S. Hutson R.G. Laine R.O. FASEB J. 1994; 8: 13-19Crossref PubMed Scopus (90) Google Scholar, 5Laine R.O. Hutson R.H. Kilberg M.S. Prog. Nucleic Acid Res. Mol. Biol. 1996; 53: 219-248Crossref PubMed Scopus (29) Google Scholar). These mechanisms may involve the regulation of transcription, translation, and (or) mRNA stability (9Marten N.W. Burke E.J. Hayden J.M. Straus D.S. FASEB J. 1994; 8: 538-544Crossref PubMed Scopus (114) Google Scholar). However, there are very few studies of genes in which their synthesis is regulated by amino acid availability (9Marten N.W. Burke E.J. Hayden J.M. Straus D.S. FASEB J. 1994; 8: 538-544Crossref PubMed Scopus (114) Google Scholar). Positive and negative effects of amino acid limitation on mRNA levels of specific genes have been reported (9Marten N.W. Burke E.J. Hayden J.M. Straus D.S. FASEB J. 1994; 8: 538-544Crossref PubMed Scopus (114) Google Scholar). Specific examples of mRNAs or proteins for which synthesis is enhanced in response to amino acid deprivation include: serine dehydratase (10Ogawa H. Fujioka M. Su Y. Kanamoto R. Pitot H.C. J. Biol. Chem. 1991; 266: 20412-20417Abstract Full Text PDF PubMed Google Scholar); asparagine synthase (7Gong S.S. Guerrini L. Basilico C. Mol. Cell. Biol. 1991; 11: 6059-6066Crossref PubMed Scopus (81) Google Scholar); ornithine decarboxylase (11Chen Z.P. Chen K.Y. J. Biol. Chem. 1992; 267: 6946-6951Abstract Full Text PDF PubMed Google Scholar, 12Ponjanpelto P. Holtta E. Mol. Cell. Biol. 1990; 10: 5814-5821Crossref PubMed Scopus (48) Google Scholar); System A (13Bracy D.S. Handlogten M.E. Barber E.F. Han H.-P. Kilberg M.S. J. Biol. Chem. 1986; 261: 1514-1520Abstract Full Text PDF PubMed Google Scholar) and System L (14Shotwell M.A. Mattes P.M. Jayme D.W. Oxender D.L. J. Biol. Chem. 1982; 257: 2974-2980Abstract Full Text PDF PubMed Google Scholar) amino acid transport; IGFBP-1 (15Straus D.S. Burke E.J. Marten N.W. Endocrinology. 1993; 132: 1090-1100Crossref PubMed Scopus (82) Google Scholar); c-jun and c-myc(12Ponjanpelto P. Holtta E. Mol. Cell. Biol. 1990; 10: 5814-5821Crossref PubMed Scopus (48) Google Scholar); gadd153, b-actin, ubiquitin c, phosphoglycerate kinase, c/EBPa and c/EBPβ (9Marten N.W. Burke E.J. Hayden J.M. Straus D.S. FASEB J. 1994; 8: 538-544Crossref PubMed Scopus (114) Google Scholar); ribosomal protein L17 and S25 (16Laine R.O. Laipis P.J. Shay N.F. Kilberg M.S. J. Biol. Chem. 1991; 266: 16969-16972Abstract Full Text PDF PubMed Google Scholar, 17Laine R.O. Shay N.F. Kilberg M.S. J. Biol. Chem. 1994; 269: 9693-9697Abstract Full Text PDF PubMed Google Scholar). In mammals, dietary protein deficiency results in decreased levels of serum proteins including albumin (8Hutson R.G. Kilberg M.S. Biochem. J. 1994; 304: 745-750Crossref PubMed Scopus (64) Google Scholar). In the case of albumin, it has been suggested that the decreased protein and mRNA levels are mainly due to reduced mRNA stability (9Marten N.W. Burke E.J. Hayden J.M. Straus D.S. FASEB J. 1994; 8: 538-544Crossref PubMed Scopus (114) Google Scholar). For asparagine synthase, amino acid starvation increases the mRNA level, and this increase depends on de novo protein synthesis (4Kilberg M.S. Hutson R.G. Laine R.O. FASEB J. 1994; 8: 13-19Crossref PubMed Scopus (90) Google Scholar, 5Laine R.O. Hutson R.H. Kilberg M.S. Prog. Nucleic Acid Res. Mol. Biol. 1996; 53: 219-248Crossref PubMed Scopus (29) Google Scholar, 6Guerrini L. Gong S.S. Mangasarian K. Basilico C. Mol. Cell. Biol. 1993; 13: 3202-3212Crossref PubMed Scopus (88) Google Scholar, 7Gong S.S. Guerrini L. Basilico C. Mol. Cell. Biol. 1991; 11: 6059-6066Crossref PubMed Scopus (81) Google Scholar, 8Hutson R.G. Kilberg M.S. Biochem. J. 1994; 304: 745-750Crossref PubMed Scopus (64) Google Scholar). In conditions of decreased amino acid availability, it is expected that there will be a coordinate increase in catabolism of cellular proteins, amino acid biosynthesis, and amino acid transport across the plasma membrane to provide cells with sufficient amino acids for cell survival. Regulation of amino acid transport by amino acid availability has been described for System A. System A-mediated transport of neutral amino acids is induced by amino acid starvation (18Kilberg M.S. Trends Biochem. Sci. 1996; 2: 183-186Google Scholar) and this induction is sensitive to actinomycin D and cycloheximide. These studies support the concept of regulation of amino acid transport at a molecular level. Given that the gene for System A-mediated amino acid transporter has not been cloned, direct studies at a molecular level are not possible. Transport of cationic amino acids into most mammalian cells is mainly mediated through System y+. Three related proteins encoding y+-like activity have been isolated (Cat-1, Cat-2, and Cat-2a) (19Kakuda D.K. Finley K.D. Dionne V.E. MacLeod C.L. Transgene. 1993; 1: 91-101Google Scholar, 20Closs E.I. Lyons C.R. Kelly C. Cunningham J.M. J. Biol. Chem. 1993; 268: 20796-20800Abstract Full Text PDF PubMed Google Scholar). All three proteins function as transporters for the cationic amino acids arginine, lysine, and ornithine, but they differ in their affinity for substrate. Cat-1 and Cat-2 have a 10-fold higher affinity than Cat-2a (19Kakuda D.K. Finley K.D. Dionne V.E. MacLeod C.L. Transgene. 1993; 1: 91-101Google Scholar, 20Closs E.I. Lyons C.R. Kelly C. Cunningham J.M. J. Biol. Chem. 1993; 268: 20796-20800Abstract Full Text PDF PubMed Google Scholar). The biological significance of having multiple transporters for cationic amino acids in mammalian cells is not known. However, it has been suggested that these genes may be expressed and regulated in a cell-specific manner, thus facilitating amino acid transport in and out of mammalian cells in response to specific nutritional needs within a particular tissue (21Malandro M.S. Kilberg M.S. Annu. Rev. Biochem. 1996; 65: 305-336Crossref PubMed Scopus (180) Google Scholar). In this regard, the family of amino acid transporters for cationic substrates resembles the family of Na+-independent glucose transporters (22Kakuda D.K. MacLeod C.L. J. Exp. Biol. 1994; 196: 93-108PubMed Google Scholar). No molecular studies regarding adaptive regulation of System y+ to amino acid starvation have been published. Studies of amino acid deprivation in entire animals are not feasible, mainly because of the dramatic changes that occur in the circulating hormones, which regulate the expression of a variety of genes. Therefore, the use of in vitro systems is initially required to identify the regulatory signals for amino acid-dependent gene expression. As shown in this report, Fao cells are ideal to study the adaptive regulation of Cat-1-mediated transport because they do not express the Cat-2 and Cat-2a transporters. Here, we show that the regulation of thecat-1 gene in rat hepatoma Fao cells is responsive to amino acid deprivation and re-exposure to individual amino acids. We thank Dr. Loyd Culp for his assistance in performing the immunofluorescense studies." @default.
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• W2140549895 title "Adaptive Regulation of the Cationic Amino Acid Transporter-1 (Cat-1) in Fao Cells" @default.
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