6533b836fe1ef96bd12a11c0
RESEARCH PRODUCT
Membrane Transport of l-Arginine and Cationic Amino Acid Analogs
Giovanni E. MannEllen I. Closssubject
chemistry.chemical_classificationArginineChemistryCationic polymerizationnutritional and metabolic diseasesSubstrate (chemistry)TransporterMembrane transportAmino acidNitric oxidechemistry.chemical_compoundMembraneBiochemistrymental disorderscardiovascular diseasesdescription
Publisher Summary This chapter reviews the current knowledge of the mechanisms and regulation of cationic amino acids (CAA) carrier proteins and discusses the potential involvement of each transporter in supplying L-arginine for nitric oxide biosynthesis. The CAA L-arginine, the substrate for nitric oxide synthases (NOSs), is considered a semi-essential amino acid in most mammals. Consequently, mammalian cells must be capable of exchanging CAA with the environment. The bilayer of the plasma membrane is impermeable to polar molecules, and thus, specialized carrier proteins with distinct substrate specificity transport hydrophilic solutes such as amino acids. L-arginine shares the same transport systems with other CAA and their analogs. In addition, some CAA transport systems also interact with neutral amino acids (NAA). Hence, changes in the expression and/or activity of these transport systems will affect not only the transport of L-arginine, but also transport of other CAA, NAA, and CAA analogs, including some NOS inhibitors.
year | journal | country | edition | language |
---|---|---|---|---|
2000-01-01 |