Homologous Canavalia Lectins Elicit Different Patterns of Antinociceptive Responses

Abstract

Canavalia gladiata (CGL), C. maritima (ConM) and C. brasiliensis (ConBr) lectins were evaluated in nociception models. ConBr inhibited first (32%) and second (100%) phases of the formalin test; CGL inhibited only the first (74%) and ConM only the second (59%) phase. Hypernociception evaluated in the Von Frey test was inhibited by ConM (55%), CGL (41%) and ConBr (38%). Acetic acid-induced abdominal writhing was reduced by ConBr (66%), CGL (52%) and ConM (60%). ConBr and CGL effects were reversed by the lectin association with its ligand sugar. The antinociceptive activity of the structural homologous lectins was differentiated by potency, efficacy and mechanisms.

ConA-Like Lectins: High Similarity Proteins as Models to Study Structure/Biological Activities Relationships

“…In a study by Assreuy et al (1997) [28], all tested lectins had anti-inflammatory effect, except for ConBr. This result was confirmed more recently by Pinto et al (2013) [30] and has been attributed to small structural differences between these lectins which may involve interaction with glycans.…”

“…Although they have high structural similarity, these lectins demonstrate different potency, efficacy and mechanisms in their biological activity, as demonstrated by comparing the studies noted above related to the results of inflammation and nociception. For instance, Pinto et al (2013) [30] evaluated the antinociceptive effect of CGL, ConM and ConBr in several nociception models. The effects occurred predominantly via peripheral nociception and showed different results according to the potency of the elicited effect.…”

Anti-inflammatory and anti-necrotic effects of lectins from Canavalia ensiformis and Canavalia brasiliensis in experimental acute pancreatitis

“…Antinociceptive [22,24]; and anti-in ammatory [39,23]; properties of Diocleinae lectins, have previously been reported in animal experimental models. However, to-date there has been no study showing antiin ammatory activities of ConA and ConBr.…”

“…Many of the biological activities of lectins in general are related to an interaction with sugars present on the cell surface [48]. Proof of participation of the lectin domain in processes of cell recognition and interaction has been shown by inhibition of the lectin effect by binding to its speci c sugar/glycoconjugate [22,23,24,39). ConA and ConBr are glucose/mannose ligands lectins which have had biological activities previously attributed to their lectin domain [23,49,50].…”

“…They promote apoptosis in human leukemic cells lines, in a mitochondrial-dependent manner, while preserving healthy cells [20]. In addition, these lectins exert immunomodulatory and antinociceptive properties in experimental models in vivo [21][22][23][24].…”