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CRAMBESCIN C1 ACTS AS A SUBSTRATE OF iNOS and eNOS INCREASING NITRIC OXIDE PRODUCTION WITH AN IN VIVO HYPOTENSIVE EFFECT
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  • Juan Rubiolo,
  • Emilio Lence,
  • Concepción González-Belo,
  • María Roel,
  • José Gil-Longo,
  • Manuel Campos-Toimil,
  • Olivier Thomas,
  • Antonio González-Cantalapiedra,
  • Henar López-Alonso,
  • Mercedes Vieytes,
  • Eva Ternon,
  • Luis Botana
Juan Rubiolo
UNIVERSIDAD DE SANTIAGO DE COMPOSTELA
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Emilio Lence
CiQUS
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Concepción González-Belo
Universidade de Santiago de Compostela
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María Roel
Universidad de Santiago de Compostela
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José Gil-Longo
Universidade de Santiago de Compostela
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Manuel Campos-Toimil
Universidade de Santiago de Compostela
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Olivier Thomas
National University of Ireland Galway
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Antonio González-Cantalapiedra
Universidade de Santiago de Compostela
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Henar López-Alonso
UNIVERSIDAD DE SANTIAGO DE COMPOSTELA
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Mercedes Vieytes
Universidade de Santiago de Compostela
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Eva Ternon
Université Côte d’Azur
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Luis Botana
Universidad de Santiago de Compostela

Corresponding Author:luis.botana@usc.es

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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.