Overview
- Raiteri, M. et al. (1990) Eur. J. Pharmacol. 184, 239.
- Saitoh, T. et al. (1994) Br. J. Pharmacol. 113, 165.
- Schmieden, V. et al. (1999) Mol. Pharmacol. 56, 464.
- Legendre, P. (2001) Cell. Mol. Life Sci. 58, 760.
- de Koning, T.J. et al. (2003) Biochem. J. 371, 653.
- Alomone Labs L-Serine inhibits specific binding of Strychnine to rat spinal cord Strychnine-sensitive Glycine receptors.Percent inhibition of specific binding of 10 nM [3H]Strychnine to membranes from rat spinal cord was plotted against concentrations of L-Serine (#S-135), (green circles) and of (-)-Strychnine (assay standard, black squares) and used to calculate IC50 and Ki values for L-Serine (IC50 ≈ 1.50 mM, and Ki ≈ 0.85 mM).
- de Koning, T.J. et al. (2003) Biochem. J. 371, 653.
L-Serine is an endogenous agonist of glycine receptors with an effective concentration of 0.1-5 mM.
L-Serine is a conditional essential amino-acid and cannot be synthesized in sufficient quantities to meet with cellular demands. It is mostly obtained by dietary intake, biosynthesis from the glycolytic intermediate 3-phospho-glycerate and by protein and phospholipid degradation. In addition to its role in cell proliferation, L-Serine is utilized in multiple pathways and processes including gluconeogenesis, cystathionine formation and phospholipid synthesis.
Contrary to other amino-acid catabolism deficiencies which are often characterized by extensive neurological dysfunction no such deficiencies have been discovered for L-Serine. Plasma levels increases in serine (and glycine) and urinary excretion have been reported in patients suffering from schizophrenia and psychosis but currently these findings remain controversial1.
L-Serine (#S-135) is a highly pure, synthetic, and biologically active compound.