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

Authors

  • Iris Serratos Departamento de Química, Universidad Autónoma Metropolitana-Iztapalapa, México.
  • Ambar López_Macay Laboratorio de Enfermedades Neuromusculares, División de Neurociencias, Instituto Nacional de Rehabilitación, SSA. México
  • Pilar Castellanos Departamento de Ingeniería Eléctrica, Universidad Autónoma Metropolitana-Iztapalapa, México
  • José Gilberto Córdoba-Herrera Departamento de Química, Universidad Autónoma Metropolitana-Iztapalapa, México
  • Ruy Pérez-Montfort Departamento de Bioquímica y Biología Estructural, Instituto de Fisiología Celular, Universidad Nacional Autónoma de México. México
  • Nallely Cabrera Departamento de Bioquímica y Biología Estructural, Instituto de Fisiología Celular, Universidad Nacional Autónoma de México. México
  • Fabián Arechavaleta-Velasco Unidad de Investigación Médica en Medicina Reproductiva, Hospital Gineco-Obstetricia, IMSS, México
  • Pablo Domínguez-López Unidad de Investigación Médica en Medicina Reproductiva, Hospital Gineco-Obstetricia, IMSS, México
  • Abel Santamaría Laboratorio de Aminoácidos Excitadores, Instituto Nacional de Neurología y Neurocirugía, SSA. México

DOI:

https://doi.org/10.29356/jmcs.v63i1.574

Keywords:

Inflammation, Lipopolysaccharide, Molecular recognition, Co-localization, Umbilical endothelial cells

Abstract

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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References

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Published

2019-01-10

Issue

Vol. 63 No. 1 (2019): Regular Issue

Section

Regular Articles

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