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L-homoarginine is a substrate of the cationic amino acid transporters CAT1, CAT2A and CAT2B.
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Estradiol increases arginine transport and CAT-1 activity through modulation of constitutive signaling transduction pathways involving ERK. Progesterone inhibits arginine transport and CAT-1 via both PKCalpha and ERK1/2 phosphorylation.
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The rs41318021 polymorphism in the SLC7A1 gene was not associated with essential hypertension in 50-year-old subjects.
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Overexpression of arginine transporter CAT-1 is associated with accumulation of L-arginine and cell growth in human colorectal cancer tissue.
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CAT1, CAT2, and CAT3 localized in adult brains but with uneven distribution.
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mRNA levels for high-affinity CAT-1, expressed as a percentage of the wild-type value, are increased by an average 12% and 32% in mdx and transgenic mdx:utr mice respectively.
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The data demonstrates that CAT1 significantly (but most likely not exclusively) contributes to the cellular uptake of asymmetric dimethylarginine.
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In hypoxic human pulmonary microvascular endothelial cells, overexpression of CAT-1 resulted in significantly greater L-arginine transport and NO production
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In acute congestive heart failure acute renal impairment function and the modulation of metabolism and extracellular transport by the DDAH-1/CAT-1 system determine high ADMA and SDMA levels after therapy for acute congestive heart failure.
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Insulin increased hCATs-L-arginine transport, maximal transport capacity, and hCAT-1 expression. Sp1 nuclear protein abundance and binding to DNA, and SLC7A1 promoter activity was increased by insulin.
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Data show that the CAT-1 isoform plays a role in arginine uptake.
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PKC activation also resulted in ubiquitination of CAT-1
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analysis of the genomic organization
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Stable polarized expression of hCAT-1 in an epithelial cell line.
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Keratinocytes express cationic amino acid transporters 1 and 2. Cationic amino acid transporter mediated L-arginine essential for inducible nitric oxide synthase and arginase enzyme, which modulate proliferation and differentiation of epidermal cells.
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Insulin-mediated stimulation of the L-arginine/NO pathway is thus associated with increased hCAT-1 and hCAT-2B mRNA, and eNOS expression
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Glomerular arginine uptake is elevated through modulation of CAT-1 expression, thus, contributing to the pathogenesis of hyperfiltration. Increased nitric oxide formation may play a role in this process.
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protein kinase C(PKC) did not phosphorylate human cationic amino acid transporter hCAT-1 directly as evidenced by in vivo phosphorylation experiments and mutational analysis, indicating an indirect action of PKC on hCAT-1
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The CAT-1 is thought to supply substrate to endothelial NOS by virtue of its co-localisation with this enzyme.
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The present study identifies a key functionally active polymorphism in the 3'UTR of SLC7A1 [which] may account for the apparent link between altered endothelial function, L-arginine, and nitric oxide metabolism and predisposition to essential hypertension
