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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Autor principal: Levi, Valeria
Publicado: 2008
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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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spelling 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
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