Effects of phosphatidylethanolamine glycation on lipid-protein interactions and membrane protein thermal stability
Non-enzymatic glycation of biomolecules has been implicated in the pathophysiology of aging and diabetes. Among the potential targets for glycation are biological membranes, characterized by a complex organization of lipids and proteins interacting and forming domains of different size and stability...
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Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_02646021_v416_n1_p145_Levi http://hdl.handle.net/20.500.12110/paper_02646021_v416_n1_p145_Levi |
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paper:paper_02646021_v416_n1_p145_Levi2023-06-08T15:23:13Z Effects of phosphatidylethanolamine glycation on lipid-protein interactions and membrane protein thermal stability Levi, Valeria Membrane protein Non-enzymatic glycation Phospholipid Plasma membrane Ca2+ - ATPase Protein-lipid interaction Different sizes Glycation In-vivo Lipid-protein interactions Membrane lipids Membrane protein Membrane proteins Non-enzymatic Non-enzymatic glycation Pathophysiology Phosphatidylethanolamine Plasma membrane Ca<sup>2+</sup> - ATPase Protein-lipid interaction Structural rearrangement Thermal denaturations Thermal unfolding Transmembrane Biological membranes Calcium Cell membranes Cytology Glucose Molecular biology Phospholipids Plasmas Proteins Pyrolysis Stability Membranes adenosine triphosphatase (calcium) adenosine triphosphatase (potassium sodium) aminophospholipid erythrocyte band 3 protein membrane lipid membrane protein phosphatidylethanolamine phospholipid 1,2 dimyristoylphosphatidylethanolamine 1,2-dimyristoylphosphatidylethanolamine adenosine triphosphatase (potassium sodium) advanced glycation end product detergent dimyristoylphosphatidylcholine erythrocyte band 3 protein glucose macrogol derivative membrane protein plasma membrane calcium transporting adenosine triphosphatase polyoxyethylene 10 dodecyl ether polyoxyethylene-10-dodecyl ether article binding affinity cell surface controlled study erythrocyte membrane glycation human human cell hyperglycemia lipid composition membrane structure priority journal protein folding protein glycosylation protein lipid interaction protein stability protein structure thermostability animal blood chemistry drug effect enzyme stability enzymology erythrocyte glycosylation micelle protein denaturation swine Animals Anion Exchange Protein 1, Erythrocyte Detergents Dimyristoylphosphatidylcholine Enzyme Stability Erythrocytes Glucose Glycosylation Glycosylation End Products, Advanced Humans Membrane Proteins Micelles Phosphatidylethanolamines Plasma Membrane Calcium-Transporting ATPases Polyethylene Glycols Protein Denaturation Sodium-Potassium-Exchanging ATPase Swine Non-enzymatic glycation of biomolecules has been implicated in the pathophysiology of aging and diabetes. Among the potential targets for glycation are biological membranes, characterized by a complex organization of lipids and proteins interacting and forming domains of different size and stability. In the present study, we analyse the effects of glycation on the interactions between membrane proteins and lipids. The phospholipid affinity for the transmembrane surface of the PMCA (plasma-membrane Ca2+-ATPase) was determined after incubating the protein or the phospholipids with glucose. Results show that the affinity between PMCA and the surrounding phospholipids decreases significantly after phosphospholipid glycation, but remains unmodified after glycation of the protein. Furthermore, phosphatidylethanolamine glycation decreases by ∼30% the stability of PMCA against thermal denaturation, suggesting that glycated aminophospholipids induce a structural rearrangement in the protein that makes it more sensitive to thermal unfolding. We also verified that lipid glycation decreases the affinity of lipids for two othermembrane proteins, suggesting that this effect might be common to membrane proteins. Extending these results to the in vivo situation, we can hypothesize that, under hyperglycaemic conditions, glycation of membrane lipids may cause a significant change in the structure and stability of membrane proteins, which may affect the normal functioning of membranes and therefore of cells. © The Authors Journal compilation. Fil:Levi, V. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2008 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_02646021_v416_n1_p145_Levi http://hdl.handle.net/20.500.12110/paper_02646021_v416_n1_p145_Levi |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-134 |
collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
topic |
Membrane protein Non-enzymatic glycation Phospholipid Plasma membrane Ca2+ - ATPase Protein-lipid interaction Different sizes Glycation In-vivo Lipid-protein interactions Membrane lipids Membrane protein Membrane proteins Non-enzymatic Non-enzymatic glycation Pathophysiology Phosphatidylethanolamine Plasma membrane Ca<sup>2+</sup> - ATPase Protein-lipid interaction Structural rearrangement Thermal denaturations Thermal unfolding Transmembrane Biological membranes Calcium Cell membranes Cytology Glucose Molecular biology Phospholipids Plasmas Proteins Pyrolysis Stability Membranes adenosine triphosphatase (calcium) adenosine triphosphatase (potassium sodium) aminophospholipid erythrocyte band 3 protein membrane lipid membrane protein phosphatidylethanolamine phospholipid 1,2 dimyristoylphosphatidylethanolamine 1,2-dimyristoylphosphatidylethanolamine adenosine triphosphatase (potassium sodium) advanced glycation end product detergent dimyristoylphosphatidylcholine erythrocyte band 3 protein glucose macrogol derivative membrane protein plasma membrane calcium transporting adenosine triphosphatase polyoxyethylene 10 dodecyl ether polyoxyethylene-10-dodecyl ether article binding affinity cell surface controlled study erythrocyte membrane glycation human human cell hyperglycemia lipid composition membrane structure priority journal protein folding protein glycosylation protein lipid interaction protein stability protein structure thermostability animal blood chemistry drug effect enzyme stability enzymology erythrocyte glycosylation micelle protein denaturation swine Animals Anion Exchange Protein 1, Erythrocyte Detergents Dimyristoylphosphatidylcholine Enzyme Stability Erythrocytes Glucose Glycosylation Glycosylation End Products, Advanced Humans Membrane Proteins Micelles Phosphatidylethanolamines Plasma Membrane Calcium-Transporting ATPases Polyethylene Glycols Protein Denaturation Sodium-Potassium-Exchanging ATPase Swine |
spellingShingle |
Membrane protein Non-enzymatic glycation Phospholipid Plasma membrane Ca2+ - ATPase Protein-lipid interaction Different sizes Glycation In-vivo Lipid-protein interactions Membrane lipids Membrane protein Membrane proteins Non-enzymatic Non-enzymatic glycation Pathophysiology Phosphatidylethanolamine Plasma membrane Ca<sup>2+</sup> - ATPase Protein-lipid interaction Structural rearrangement Thermal denaturations Thermal unfolding Transmembrane Biological membranes Calcium Cell membranes Cytology Glucose Molecular biology Phospholipids Plasmas Proteins Pyrolysis Stability Membranes adenosine triphosphatase (calcium) adenosine triphosphatase (potassium sodium) aminophospholipid erythrocyte band 3 protein membrane lipid membrane protein phosphatidylethanolamine phospholipid 1,2 dimyristoylphosphatidylethanolamine 1,2-dimyristoylphosphatidylethanolamine adenosine triphosphatase (potassium sodium) advanced glycation end product detergent dimyristoylphosphatidylcholine erythrocyte band 3 protein glucose macrogol derivative membrane protein plasma membrane calcium transporting adenosine triphosphatase polyoxyethylene 10 dodecyl ether polyoxyethylene-10-dodecyl ether article binding affinity cell surface controlled study erythrocyte membrane glycation human human cell hyperglycemia lipid composition membrane structure priority journal protein folding protein glycosylation protein lipid interaction protein stability protein structure thermostability animal blood chemistry drug effect enzyme stability enzymology erythrocyte glycosylation micelle protein denaturation swine Animals Anion Exchange Protein 1, Erythrocyte Detergents Dimyristoylphosphatidylcholine Enzyme Stability Erythrocytes Glucose Glycosylation Glycosylation End Products, Advanced Humans Membrane Proteins Micelles Phosphatidylethanolamines Plasma Membrane Calcium-Transporting ATPases Polyethylene Glycols Protein Denaturation Sodium-Potassium-Exchanging ATPase Swine Levi, Valeria Effects of phosphatidylethanolamine glycation on lipid-protein interactions and membrane protein thermal stability |
topic_facet |
Membrane protein Non-enzymatic glycation Phospholipid Plasma membrane Ca2+ - ATPase Protein-lipid interaction Different sizes Glycation In-vivo Lipid-protein interactions Membrane lipids Membrane protein Membrane proteins Non-enzymatic Non-enzymatic glycation Pathophysiology Phosphatidylethanolamine Plasma membrane Ca<sup>2+</sup> - ATPase Protein-lipid interaction Structural rearrangement Thermal denaturations Thermal unfolding Transmembrane Biological membranes Calcium Cell membranes Cytology Glucose Molecular biology Phospholipids Plasmas Proteins Pyrolysis Stability Membranes adenosine triphosphatase (calcium) adenosine triphosphatase (potassium sodium) aminophospholipid erythrocyte band 3 protein membrane lipid membrane protein phosphatidylethanolamine phospholipid 1,2 dimyristoylphosphatidylethanolamine 1,2-dimyristoylphosphatidylethanolamine adenosine triphosphatase (potassium sodium) advanced glycation end product detergent dimyristoylphosphatidylcholine erythrocyte band 3 protein glucose macrogol derivative membrane protein plasma membrane calcium transporting adenosine triphosphatase polyoxyethylene 10 dodecyl ether polyoxyethylene-10-dodecyl ether article binding affinity cell surface controlled study erythrocyte membrane glycation human human cell hyperglycemia lipid composition membrane structure priority journal protein folding protein glycosylation protein lipid interaction protein stability protein structure thermostability animal blood chemistry drug effect enzyme stability enzymology erythrocyte glycosylation micelle protein denaturation swine Animals Anion Exchange Protein 1, Erythrocyte Detergents Dimyristoylphosphatidylcholine Enzyme Stability Erythrocytes Glucose Glycosylation Glycosylation End Products, Advanced Humans Membrane Proteins Micelles Phosphatidylethanolamines Plasma Membrane Calcium-Transporting ATPases Polyethylene Glycols Protein Denaturation Sodium-Potassium-Exchanging ATPase Swine |
description |
Non-enzymatic glycation of biomolecules has been implicated in the pathophysiology of aging and diabetes. Among the potential targets for glycation are biological membranes, characterized by a complex organization of lipids and proteins interacting and forming domains of different size and stability. In the present study, we analyse the effects of glycation on the interactions between membrane proteins and lipids. The phospholipid affinity for the transmembrane surface of the PMCA (plasma-membrane Ca2+-ATPase) was determined after incubating the protein or the phospholipids with glucose. Results show that the affinity between PMCA and the surrounding phospholipids decreases significantly after phosphospholipid glycation, but remains unmodified after glycation of the protein. Furthermore, phosphatidylethanolamine glycation decreases by ∼30% the stability of PMCA against thermal denaturation, suggesting that glycated aminophospholipids induce a structural rearrangement in the protein that makes it more sensitive to thermal unfolding. We also verified that lipid glycation decreases the affinity of lipids for two othermembrane proteins, suggesting that this effect might be common to membrane proteins. Extending these results to the in vivo situation, we can hypothesize that, under hyperglycaemic conditions, glycation of membrane lipids may cause a significant change in the structure and stability of membrane proteins, which may affect the normal functioning of membranes and therefore of cells. © The Authors Journal compilation. |
author |
Levi, Valeria |
author_facet |
Levi, Valeria |
author_sort |
Levi, Valeria |
title |
Effects of phosphatidylethanolamine glycation on lipid-protein interactions and membrane protein thermal stability |
title_short |
Effects of phosphatidylethanolamine glycation on lipid-protein interactions and membrane protein thermal stability |
title_full |
Effects of phosphatidylethanolamine glycation on lipid-protein interactions and membrane protein thermal stability |
title_fullStr |
Effects of phosphatidylethanolamine glycation on lipid-protein interactions and membrane protein thermal stability |
title_full_unstemmed |
Effects of phosphatidylethanolamine glycation on lipid-protein interactions and membrane protein thermal stability |
title_sort |
effects of phosphatidylethanolamine glycation on lipid-protein interactions and membrane protein thermal stability |
publishDate |
2008 |
url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_02646021_v416_n1_p145_Levi http://hdl.handle.net/20.500.12110/paper_02646021_v416_n1_p145_Levi |
work_keys_str_mv |
AT levivaleria effectsofphosphatidylethanolamineglycationonlipidproteininteractionsandmembraneproteinthermalstability |
_version_ |
1768543943766573056 |