Disease relevance of Serine-borate

• The extents of peptidolysis of [3]LTC4 and [3]LTD4 by 100 microliter of pulmonary edema fluid attained respective mean maximum levels of 74.5 +/- 2.9% (N = 5) and 37.7 +/- 10.2% (N = 4) after 30 min at 37 degrees C and were inhibited by serine-borate and by cysteine, respectively [1].

High impact information on Serine-borate

• These studies, kinetic investigations, equilibrium dialysis experiments, and other data support the view that inhibition is produced by formation of serine-borate complex which binds at the gamma-glutamyl binding site of the light subunit of gamma-glutamyl transpeptidase [2].
• Inhibitors of GGT activity, acivicin and serine-borate, are capable of dampening or blocking the effect of R1881 on growth [3].
• The uptake of glutamate in the reconstituted system was sensitive to the temperature of incubation and to the inhibitors (serine-borate, azaserine, and 6-diazo-5-oxo-L-norleucine) of gamma-glutamyl transpeptidase activity [4].
• Superfusion of L-Gln-loaded capillaries in a buffer containing gamma-glutamyl transpeptidase (GGT) inhibitors, serine borate (SB) or 6-diazo-5-oxo-L-norleucine (DON), increased the basal L-Gln release and made it irresponsive to subsequent treatment with TRY [5].
• We showed [Biochem. J. (1981) 194, 99-102] that inhibition of gamma-glutamyl transpeptidase in vivo with serine-borate decreases amino acid uptake by mammary gland [6].

Biological context of Serine-borate

• Glutathione-mediated, gamma-glutamyltranspeptidase-dependent mutagenesis of TA100 cells was inhibited by serine-borate complex, a known gamma-glutamyltranspeptidase inhibitor, and potentiated by glycylglycine, a known gamma-glutamyltranspeptidase enhancer [7].
• Finally, inhibition of GGT by either the Serine/Borate complex or by Acivicin resulted in cell apoptosis [8].
• Liberation of glycine was inhibited (74-83%) by serine borate (20 mM), indicating a gamma-glutamyltransferase-dependent hydrolysis of GSH [9].

Anatomical context of Serine-borate

• The gamma-glutamyl transpeptidase implanted ghost membranes exhibited the uptake of L-glutamate which was inhibited by serine-borate, an inhibitor of transpeptidase activity [10].
• HPLC analysis indicated that over 94% of [35S]-GSH remained intact in the epithelium and cortex in the presence or absence of gamma-glutamyl transpeptidase inhibitor, serine borate [11].
• The erythrocyte enzyme had the same kinetic properties as serum and liver enzymes and was inhibited by serine-borate mixture, a specific inhibitor of the enzyme [12].
• The enzyme isolated from the plasma membrane of WI-38 cells, like the enzyme from kidney and brain, was found to be irreversibly inhibited by iodoacetamide, reversibly by serine-borate, and had a strong specificity for certain amino acids [13].
• To determine whether luminal cysteine accumulation resulted from mucosal secretion of GSH and subsequent degradation by brush-border gamma-glutamyltransferase (gamma-GT) and dipeptidases, acivicin or serine-borate was used to inhibit gamma-GT [14].

Associations of Serine-borate with other chemical compounds

• Caput luminal GGT transpeptidation activity was significantly inhibited by serine-borate and was optimal at pH 8 [15].
• Serine-borate, a competitive inhibitor of GGT, blocked the restoration of intracellular glutathione [16].
• We found that y-glutamyl transpeptidase activity induces NF-kappaB DNA binding activity, an effect which is significantly reduced by the addition of GGT inhibitors (Serine/Borate complex and Acivicin) [8].
• LTC4 formation, measured in vitro, was linear for > 10 min at 25 degrees C in the presence of 50 mM serine borate (an inhibitor of gamma-glutamyl transpeptidase), with Km values for LTA4 and GSH of 56 microM and 8.5 mM, respectively [17].

Gene context of Serine-borate

• This induction depends on GGT activity as it is prevented by the Serine/Borate complex, a GGT inhibitor [8].
• This could be inhibited by the gamma-glutamyltransferase inhibitor serine-borate [18].

Analytical, diagnostic and therapeutic context of Serine-borate

• Over 94% of plasma-derived GSH remained in its original molecular form of GSH in the lens, during the 10 min perfusion both with and without the GGT inhibitor, serine borate [19].

References