Abstract
Bryothamnion seaforthii lectin (BSL) induced reversible concentration-related relaxation of endothelized aorta, maximal at 30μg/ml (IC50= 4.8 ± 0.6μg/ml). This effect was inhibited by L-NAME and reversed by mucin, probably via interaction with a specific lectin-binding site on the endothelium activating nitric oxide synthase.
Keywords: Lectin, agglutinin, Bryothamnion seaforthii, nitric oxide synthase, red marine alga
Protein & Peptide Letters
Title: Bryothamnion seaforthii Lectin Relaxes Vascular Smooth Muscle: Involvement of Endothelium and NO Synthase
Volume: 17 Issue: 3
Author(s): Ricardo F. Lima, David N. Criddle, Pedro Marcos G. Soares, Samile Pereira Ribeiro, Benildo S. Cavada, Kyria S. Nascimento, Alexandre H. Sampaio and Ana Maria S. Assreuy
Affiliation:
Keywords: Lectin, agglutinin, Bryothamnion seaforthii, nitric oxide synthase, red marine alga
Abstract: Bryothamnion seaforthii lectin (BSL) induced reversible concentration-related relaxation of endothelized aorta, maximal at 30μg/ml (IC50= 4.8 ± 0.6μg/ml). This effect was inhibited by L-NAME and reversed by mucin, probably via interaction with a specific lectin-binding site on the endothelium activating nitric oxide synthase.
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Lima F. Ricardo, Criddle N. David, Soares G. Pedro Marcos, Ribeiro Pereira Samile, Cavada S. Benildo, Nascimento S. Kyria, Sampaio H. Alexandre and Assreuy S. Ana Maria, Bryothamnion seaforthii Lectin Relaxes Vascular Smooth Muscle: Involvement of Endothelium and NO Synthase, Protein & Peptide Letters 2010; 17 (3) . https://dx.doi.org/10.2174/092986610790780332
DOI https://dx.doi.org/10.2174/092986610790780332 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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