Anti-inflammatory and Antinociceptive Activity of Chitin-binding Lectin from Canna Limbata Seeds

Anti-inflammatory and Antinociceptive Activity of Chitin-binding Lectin from Canna Limbata Seeds

Lectins are a structurally heterogeneous group of proteins or glycoproteins with at least one noncatalytic domain binding reversibly to a specific mono- or oligosaccharide. Monocot mannose-binding lectins are an extended superfamily of structurally and evolutionarily related proteins. In this study,...

Full description

Saved in:
Bibliographic Details
Published in:Applied biochemistry and biotechnology Vol. 171; no. 8; pp. 1944 - 1955
Main Authors: Araújo, Theolyta S, Teixeira, Claudener S, Falcão, Maria A. P, Junior, Vanir R. Pinto, Santiago, Mayara Quiroz, Benevides, Raquel G, Delatorre, Plínio, Martins, Jorge L, Alexandre-Moreira, Magna S, Cavada, Benildo S, Campesatto, Eliane A, Rocha, Bruno A. M
Format: Journal Article
Language:English
Published: Boston Springer-Verlag 01-12-2013
Springer US
Springer
Springer Nature B.V
Subjects:
Acetic acid
Analgesics - pharmacology
Animals
anti-inflammatory activity
Anti-Inflammatory Agents - pharmacology
Biochemistry
Biological and medical sciences
Biotechnology
Canna
Chemistry
Chemistry and Materials Science
Chitin
Chitin - metabolism
electrophoresis
Formaldehyde - toxicity
formalin
Fundamental and applied biological sciences. Psychology
Glycoproteins
Hemagglutination - drug effects
Humans
inflammation
Inflammation - chemically induced
Inflammation - drug therapy
Inflammation - pathology
lectins
Lectins - metabolism
Mass spectrometry
Mice
Pain - chemically induced
Pain - drug therapy
Pain - pathology
peritonitis
Pharmacology
Plant Extracts - chemistry
Plant Extracts - pharmacology
Protein Binding
Seeds
Seeds - chemistry
Zingiberales - chemistry
zymosan
Zymosan - toxicity
Lectin
Antinociceptive
Anti-inflammatory
Canna limbata
Chitin
Antiinflammatory agent
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Lectins are a structurally heterogeneous group of proteins or glycoproteins with at least one noncatalytic domain binding reversibly to a specific mono- or oligosaccharide. Monocot mannose-binding lectins are an extended superfamily of structurally and evolutionarily related proteins. In this study, we evaluated anti-inflammatory and antinociceptive effects of monocot lectin from the Canna limbata seeds (CLL). To accomplish this, CLL was purified and subjected to pharmacological assays: abdominal writhing induced by acetic acid, formalin, hot plate and Zymosan A-induced peritonitis tests. The CLL was purified by chromatographic chitin column, and the relative mass of 21 kDa observed in electrophoresis was confirmed by electrospray mass spectrometry, which also revealed that purified CLL consists of a dimer having a weight of 49,676 Da. The CLL showed nociceptive activity in the acetic acid test as well as peripheral antinociceptive response. The CLL also showed anti-inflammatory effect with the reduction of inflammation in the formalin test and neutrophil migration into the peritoneal cavity. This is the first report of anti-inflammatory activity for a monocot lectin, and it suggests a new pharmacological tool to understand inflammatory and antinociceptive processes mediated through lectins.
Bibliography:http://dx.doi.org/10.1007/s12010-013-0470-1
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0273-2289
1559-0291
DOI:10.1007/s12010-013-0470-1