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L‐cysteine/cystathionine‐β‐synthase‐induced relaxation in mouse aorta involves a L‐serine/sphingosine‐1‐phosphate/NO pathway
Author(s) -
Mitidieri Emma,
Gurgone Danila,
Caiazzo Elisabetta,
Tramontano Teresa,
Cicala Carla,
Sorrentino Raffaella,
d'Emmanuele di Villa Bianca Roberta
Publication year - 2020
Publication title -
british journal of pharmacology
Language(s) - Uncategorized
Resource type - Journals
SCImago Journal Rank - 2.432
H-Index - 211
eISSN - 1476-5381
pISSN - 0007-1188
DOI - 10.1111/bph.14654
Subject(s) - serine , cystathionine beta synthase , cysteine , biochemistry , chemistry , cystathionine gamma lyase , phosphorylation , enzyme
Among the three enzymes involved in the transsulfuration pathway, only cystathionine β-synthase (CBS) converts L-cysteine into L-serine and H 2 S. L-serine is also involved in the de novo sphingolipid biosynthesis through a condensation with palmitoyl-CoA by the action of serine palmitoyltransferase (SPT). Here, we have investigated if L-serine contributes to the vasorelaxant effect.