The C-terminal tails of 4,4'-diphenylmethane-bis(methyl) carbamate are essential for binding to receptor for advanced glycation end products to attenuate advanced glycation end products-induced inflammation and apoptosis responses in human umbilical vein

2016 ◽  
Vol 68 (1) ◽  
pp. 93-106 ◽  
Author(s):  
Liang Feng ◽  
Mao-mao Zhu ◽  
Wei-quan Bu ◽  
Chun-fei Wang ◽  
Zhao-guang Zheng ◽  
...  
Keyword(s):  
Advanced Glycation End Products ◽  
Umbilical Vein ◽  
Advanced Glycation ◽  
Human Umbilical Vein ◽  
Glycation End Products ◽  
End Products

scholarly journals Co-localization of the Receptor for Advanced Glycation End Products (RAGE) with S100 Calcium-Binding Protein B (S100B) in Human Umbilical Vein Endothelial

2019 ◽  
Vol 63 (1) ◽  
Author(s):  
Iris Serratos ◽  
Ambar López_Macay ◽  
Pilar Castellanos ◽  
José Gilberto Córdoba-Herrera ◽  
Ruy Pérez-Montfort ◽  
...  
Keyword(s):  
Advanced Glycation End Products ◽  
Calcium Binding ◽  
Binding Protein ◽  
Umbilical Vein ◽  
Calcium Binding Protein ◽  
Advanced Glycation ◽  
Human Umbilical Vein ◽  
S100 Calcium Binding Protein ◽  
Glycation End Products ◽  
End Products

The receptor for advanced glycation end products (RAGE) has been involved in the actions of inflammatory proteins such as S100 calcium binding protein B (S100B), among several others. Despite there being many studies available proposing several different modes of interaction between the receptor and the protein, it is necessary to reconcile these binding hypotheses. We evaluated the co-localization of RAGE and S100B in human umbilical vein endothelial cells (HUVEC’s) exposed to acute pro-inflammatory lipopolysaccharide (LPS). Co-localization of the receptor and the protein in umbilical cells exposed to pro-inflammatory stimuli was analyzed using an immunofluorescent assay. RAGE was present in umbilical cells, and its co-localization with S100B was stimulated in the presence of LPS. Our findings suggest an interaction between these proteins, possibly producing early inflammatory responses in umbilical cells. The understanding of the molecular mechanisms of this recognition is relevant to characterize the nature of the signaling associated with this receptor in inflammatory processes.

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