/img alt="Imagem da capa" class="recordcover" src="""/>
Artigo
CRLI induces vascular smooth muscle relaxation and suggests a dual mechanism of eNOS activation by legume lectins via muscarinic receptors and shear stress
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 carboh...
Autor principal: | Rocha, Bruno Anderson Matias da |
---|---|
Outros Autores: | 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. |
Grau: | Artigo |
Idioma: | English |
Publicado em: |
Archives of Biochemistry and Biophysics
2020
|
Assuntos: | |
Acesso em linha: |
https://repositorio.inpa.gov.br/handle/1/17566 |
id |
oai:repositorio:1-17566 |
---|---|
recordtype |
dspace |
spelling |
oai:repositorio:1-17566 CRLI induces vascular smooth muscle relaxation and suggests a dual mechanism of eNOS activation by legume lectins via muscarinic receptors and shear stress 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. 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 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. 2020-06-15T21:48:19Z 2020-06-15T21:48:19Z 2015 Artigo https://repositorio.inpa.gov.br/handle/1/17566 10.1016/j.abb.2014.11.003 en Volume 565, Pags. 32-39 Restrito Archives of Biochemistry and Biophysics |
institution |
Instituto Nacional de Pesquisas da Amazônia - Repositório Institucional |
collection |
INPA-RI |
language |
English |
topic |
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 |
spellingShingle |
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 Rocha, Bruno Anderson Matias da CRLI induces vascular smooth muscle relaxation and suggests a dual mechanism of eNOS activation by legume lectins via muscarinic receptors and shear stress |
topic_facet |
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 |
description |
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. |
format |
Artigo |
author |
Rocha, Bruno Anderson Matias da |
author2 |
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. |
author2Str |
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. |
title |
CRLI induces vascular smooth muscle relaxation and suggests a dual mechanism of eNOS activation by legume lectins via muscarinic receptors and shear stress |
title_short |
CRLI induces vascular smooth muscle relaxation and suggests a dual mechanism of eNOS activation by legume lectins via muscarinic receptors and shear stress |
title_full |
CRLI induces vascular smooth muscle relaxation and suggests a dual mechanism of eNOS activation by legume lectins via muscarinic receptors and shear stress |
title_fullStr |
CRLI induces vascular smooth muscle relaxation and suggests a dual mechanism of eNOS activation by legume lectins via muscarinic receptors and shear stress |
title_full_unstemmed |
CRLI induces vascular smooth muscle relaxation and suggests a dual mechanism of eNOS activation by legume lectins via muscarinic receptors and shear stress |
title_sort |
crli induces vascular smooth muscle relaxation and suggests a dual mechanism of enos activation by legume lectins via muscarinic receptors and shear stress |
publisher |
Archives of Biochemistry and Biophysics |
publishDate |
2020 |
url |
https://repositorio.inpa.gov.br/handle/1/17566 |
_version_ |
1787144134071418880 |
score |
11.755432 |