This review aims to describe the action sites of the oxidative stress products for 4-hydroxy-2E-nonenal, on subcellular fractions of eukaryotic cells from several tissues. Described also are; the detoxification mechanisms from derivatives of 4-hydroxy-2E-nonenal. All dangerous compounds for subcellular fractions are metabolites of a respiratory chain that can give stable products of oxidative compounds and are intermediates of other oxidation reaction chains. Finally, the balancing among the illustrated processes to identify the relative oxidative power of several metabolic chains useful to make evident subcellular damages or detoxification processes is discussed.
Aldehydes/metabolism , Aldehydes/toxicity , Lipid Peroxidation/drug effects , Organelles/drug effects , Organelles/metabolism , Oxidative Stress/drug effects , Animals , Cross-Linking Reagents/metabolism , Cross-Linking Reagents/toxicity , Endoplasmic Reticulum Stress/drug effects , Endoplasmic Reticulum Stress/physiology , Humans , Lipid Peroxidation/physiology , Mitochondria/drug effects , Mitochondria/metabolism , Oxidative Stress/physiology
In the following paper, authors describe glycans present on cell membranes as they affect the folding, the spatial arrangement, the behavior and the interaction with the substrate of some membrane proteins. Authors describe the synthesis and assembly of a glycan on a protein, the formation of N-glycans, the maturation of an N-glycan in different cellular compartments, the structure of the glycocalyx and how it interacts with any pathogens. The study of the E-cadherin and the potassium channel to demonstrate how glycans affect the spatial arrangement, the stability and activity of the glycoproteins on the membranes. Subsequently, authors analyze the correlation between disorder glycosylation and human health. Authors define glycosylation disorders as a genetic defect that alter the structure or biosynthesis of glycans (sugar chains) in one or more biosynthetic pathways. Human glycosylation disorders reflect the disruption of early steps in the pathways of glycan biosynthesis. More in details, authors analyze the role of glycoprotein in tumor cell adhesion, in particular, in cells MCF-7 and MDA-MB-231 on zeolite scaffold. In the same time, the role of metalloproteinase is described in the mobilization of cancer cells and in metastasis.
Cell Membrane/metabolism , Cell Membrane/pathology , Glycoproteins/metabolism , Polysaccharides/metabolism , Animals , Carbohydrates/physiology , Glycosylation , Humans , Neoplasms/metabolism , Neoplasms/pathology
