Study on Cardiac Ischemia and Ischemia/Reperfusion Cause Wide Proteolysis of the Coronary Endothelial Luminal Membrane: An Approach to Possible Dysfunctions

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Study on Cardiac Ischemia and Ischemia/Reperfusion Cause Wide Proteolysis of the Coronary Endothelial Luminal Membrane: An Approach to Possible Dysfunctions

September 1, 2021 Medicine and Medical 0

Background: Ischemia and ischemia-reperfusion (I/R) are two common clinical insults that affect the molecular structure of the coronary vascular endothelial luminal membrane (VELM) and cause a variety of microvascular dysfunctions. The related metabolic alterations, on the other hand, are little understood. We hypothesised that metabolic changes cause ischemia and I/R-induced structural and functional VELM modifications. These changes must first be stated, and then the mechanisms driving them must be recognised.

VELM proteins were biotin-labeled in isolated perfused rat hearts during control circumstances. The hearts were divided into three groups: control (C), no flow ischemia (I; 25 min), and I/R. (I; 25 min, reperfusion 30 min). Two-dimensional electrophoresis was used to identify biotinylated luminal endothelial membrane proteins in these three groups. It should be noted, however, that the proteins were biotin-labeled during the control.

Results: Following 2D gel electrophoresis, a comparison of the protein profiles under the three conditions revealed changes in the molecular weight distribution, with MWC > MWI > MWI/R. Under ischemia conditions, an analysis of isoelectric points (pHi) revealed a shift toward more acidic pHi. During ischemia and I/R, 66 percent and 88 percent of the proteins identified during control changed their MW-pHi, respectively. There were 9 proteins identified as adhesins and G-protein coupled receptors among the missing proteins.

MW-pHi of most luminal glycocalyx proteins is altered by I and I/R insults due to the activation of non-specific hydrolyzing processes; suspect metalloproteases and glycanases. In order to maintain the integrity of the vascular endothelium membrane, it is vital to identify hydrolyzing enzymes that are responsible for numerous microvascular dysfunctions. Future treatments must include VELM as a target.

Author (S) Details

Blanca Arroyo-Flores
Departamento de Fisiologia y Farmacologia, Universidad Autonoma de San Luis Potosi, San Luis Potosi, Mexico.

Erika Chi-Ahumada
Departamento de Fisiologia y Farmacologia, Universidad Autonoma de San Luis Potosi, San Luis Potosi, Mexico.

Erika Briones-Cerecero
Departamento de Biologia Molecular, Instituto Potosino de Investigacion Cientifica y Tecnologica, San Luis Potosi, Mexico.

Alma Barajas-Espinosa
Departamento de Fisiologia y Farmacologia, Universidad Autonoma de San Luis Potosi, San Luis Potosi, Mexico.

Sandra Perez-Aguilar
Departamento de Fisiologia y Farmacologia, Universidad Autonoma de San Luis Potosi, San Luis Potosi, Mexico.

Ana Barba de la Rosa
Departamento de Biologia Molecular, Instituto Potosino de Investigacion Cientifica y Tecnologica, San Luis Potosi, Mexico.

Maureen Knabb
Department of Biology, West Chester University, West Chester, PA, USA.

Rafael Rubio
Departamento de Fisiologia y Farmacologia, Universidad Autonoma de San Luis Potosi, San Luis Potosi, Mexico.

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