Please use this identifier to cite or link to this item: https://repositorio.inpa.gov.br/handle/1/17566
Title: CRLI induces vascular smooth muscle relaxation and suggests a dual mechanism of eNOS activation by legume lectins via muscarinic receptors and shear stress
Authors: Rocha, Bruno Anderson Matias da
Barroso-Neto, Ito Liberato
Teixeira, Claudener S.
Santiago, Mayara Quiroz
Pires, Alana de Freitas
Souza, Luis Augusto Gomes
Nascimento, K. S.
Sampaio, Alexandre Holanda
Delatorre, Plínio
Assreuy, Ana Maria Sampaio
Cavada, B. S.
Keywords: Atropine
Calcium
Calcium Ion
Endothelial Nitric Oxide Synthase
Heparan Sulfate
Indometacin
Manganese
Mannose-binding Lectin
Mannoside
Muscarinic Receptor
Ng-nitroarginine Methyl Ester
Phenylephrine
Sodium Ion
Endothelial Nitric Oxide Synthase
Enzyme Inhibitor
Indometacin
Mannose-binding Lectin
Muscarinic Receptor
Ng-nitroarginine Methyl Ester
Nitric Oxide
Nonsteroid Antiinflammatory Agent
Nos3 Protein, Rat
Vegetable Protein
Animals Experiment
Animals Tissue
Aorta
Controlled Study
Crystal Structure
Electron
Enzyme Activation
Extracellular Calcium
Legume
Male
Mechanoreceptor
Metal Binding
Molecular Docking
Molecular Weight
Nonhuman
Protein Quaternary Structure
Rat
Shear Stress
Smooth Muscle Contractility
Stereochemistry
Synchrotron Radiation
Muscle, Smooth, Vascular
Vasodilatation
X-ray Diffraction
Animals
Antagonists And Inhibitors
Biosynthesis
Chemistry
Cytology
Drug Effects
Enzyme Activation
Enzymology
Fabaceae
Human
Metabolism
Muscle Relaxation
Muscle, Smooth, Vascular
Wistar Rat
Animal
Anti-inflammatory Agents, Non-steroidal
Enzyme Activation
Enzyme Inhibitors
Fabaceae
Humans
Indomethacin
Male
Mannose-binding Lectin
Muscle Relaxation
Muscle, Smooth, Vascular
Ng-nitroarginine Methyl Ester
Nitric Oxide
Nitric Oxide Synthase Type Iii
Plant Proteins
Rats
Rats, Wistar
Receptors, Muscarinic
Issue Date: 2015
metadata.dc.publisher.journal: Archives of Biochemistry and Biophysics
metadata.dc.relation.ispartof: Volume 565, Pags. 32-39
Abstract: Lectins are proteins able to recognize carbohydrates, without modifying their structure, via the carbohydrate-recognition domain (CRD). Here, the three-dimensional structure of the mannose-binding lectin isolated from Cymbosema roseum (CRLI) was determined with X-man molecule modeled into the carbohydrate recognition domain. CRLI relaxant activity in thoracic rat aorta was also investigated, and based on the results, a molecular docking of CRLI with heparan sulfate was performed to investigate the possible interaction with mechanoreceptors involved in vasorelaxation. CRLI (IC50 = 12.4 μg mL-1) elicited vasorelaxant response (96%) in endothelialized rat aorta contracted with phenylephrine. Endothelium-derived relaxant factors, extracellular calcium (Ca2+e) and muscarinic receptors were also evaluated as putative participants in the CRLI relaxant effect. CRLI relaxant effect was blocked by L-NAME, a nonselective inhibitor of nitric oxide synthase (NOS), and partially inhibited in a calcium-free solution (0Ca) and by atropine, but it remained unchanged in the presence of indomethacin and TEA. In summary, our data suggest interaction between CRLI and muscarinic receptors located in vascular endothelial cells leading to NOS activation triggered by a mechanism that involves Ca2+e along with the ability of CRLI to interact with heparan sulfate, a highly rated mechanoreceptor involved in eNOS activation. © 2014 Published by Elsevier Inc.
metadata.dc.identifier.doi: 10.1016/j.abb.2014.11.003
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