CRAMBESCIN C1 ACTS AS A SUBSTRATE OF iNOS and eNOS INCREASING NITRIC
OXIDE PRODUCTION WITH AN IN VIVO HYPOTENSIVE EFFECT
Abstract
1. Crambescins are guanidine alkaloids from the sponge Crambe crambe.
Crambescine C induces metallothionein genes and nitric oxide is one of
the triggers. We assayed in silico, in vitro and, in vivo the effect in
comparison with two analogs: crambescine A, and homo-crambescine C 2.
HepG2 gene expression was analyzed using microarrays and additionally
assays used isolated rat aortic rings. The targets of crambescines were
studied in silico. In vivo vasodilation in rats was done by direct
measurement. 3. Crambescines C and homo-crambescine C, but not
crambescine A, induced metallothioneins transcripts. HepG2 cells with
crambescine C increased nitric oxide production. Vasodilation was
observed in aortic ring and in vivo after injection in rats. In silico
analysis points to eNOS and iNOS as targets of crambescin C and source
of nitric oxide increment. 4. Crambescin C effect is mediated through
crambescing binding to the active site of eNOS and iNOS. In isolated rat
aortic rings CC and HCC induced an endothelium-dependent relaxation
related to eNOS activation and an endothelium-independent relaxation
related to iNOS activation, hence both compounds increase NO and reduce
vascular tone. 5. Crambescin C1 docking studies in iNOS and eNOS active
site revealed hydrogen bonding of the hydroxylated chain with residues
Glu377 and Glu361, involved in the substrate recognition, and explains
its higher binding affinity than Crambescin A1. The later interaction
and the extra polar contacts with its pyrimidine moiety, absent in the
endogenous substrate, explain its role as exogenous substrate of NOSs
and NO production.