A method for distinguishing 1-acyl from 2-acyl lysophosphatidylcholines generated in biological systems

Phospholipases A1 and A2 frequently coexist in biological systems. Generation of lysophosphatidylcholine (LPC) in such systems cannot be assigned to any of these types of enzymes unless the position of the fatty acid in the lysocompound can be unambiguously determined. We here present a simple metho...

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Autores principales: Florin-Christensen, J., Narvaez-Vasquez, J., Florin-Christensen, M., Ryan, C.A.
Formato: JOUR
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Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00032697_v276_n1_p13_FlorinChristensen
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spelling todo:paper_00032697_v276_n1_p13_FlorinChristensen2023-10-03T13:55:49Z A method for distinguishing 1-acyl from 2-acyl lysophosphatidylcholines generated in biological systems Florin-Christensen, J. Narvaez-Vasquez, J. Florin-Christensen, M. Ryan, C.A. 1-acyl-lysophosphatidylcholine 2-acyllysophosphatidylcholine Lysocompounds Phospholipase A1 Phospholipase A2 Positional analysis fatty acid lysophosphatidylcholine phospholipase A1 phospholipase A2 acylation analytic method article enzyme assay hydrolysis nonhuman priority journal Phospholipases A1 and A2 frequently coexist in biological systems. Generation of lysophosphatidylcholine (LPC) in such systems cannot be assigned to any of these types of enzymes unless the position of the fatty acid in the lysocompound can be unambiguously determined. We here present a simple method to achieve this purpose. It is based on the initial chemical acylation of the isolated LPC with a labeled fatty acid, followed by the enzymatic analysis of the resulting phosphatidylcholine (PC), using snake or bee venom phospholipase A2. Thus, if treatment of the PC with this enzyme releases a labeled free fatty acid, it is demonstrated that the initial LPC was acylated at position sn-1, whereas if the product of hydrolysis yields labeled LPC, then the initial LPC was acylated at position sn-2. This is the first method devised to determine the source of LPC in the presence of mixtures of phospholipases A1 and A2 in complex biological systems. Fil:Florin-Christensen, J. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Florin-Christensen, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00032697_v276_n1_p13_FlorinChristensen
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic 1-acyl-lysophosphatidylcholine
2-acyllysophosphatidylcholine
Lysocompounds
Phospholipase A1
Phospholipase A2
Positional analysis
fatty acid
lysophosphatidylcholine
phospholipase A1
phospholipase A2
acylation
analytic method
article
enzyme assay
hydrolysis
nonhuman
priority journal
spellingShingle 1-acyl-lysophosphatidylcholine
2-acyllysophosphatidylcholine
Lysocompounds
Phospholipase A1
Phospholipase A2
Positional analysis
fatty acid
lysophosphatidylcholine
phospholipase A1
phospholipase A2
acylation
analytic method
article
enzyme assay
hydrolysis
nonhuman
priority journal
Florin-Christensen, J.
Narvaez-Vasquez, J.
Florin-Christensen, M.
Ryan, C.A.
A method for distinguishing 1-acyl from 2-acyl lysophosphatidylcholines generated in biological systems
topic_facet 1-acyl-lysophosphatidylcholine
2-acyllysophosphatidylcholine
Lysocompounds
Phospholipase A1
Phospholipase A2
Positional analysis
fatty acid
lysophosphatidylcholine
phospholipase A1
phospholipase A2
acylation
analytic method
article
enzyme assay
hydrolysis
nonhuman
priority journal
description Phospholipases A1 and A2 frequently coexist in biological systems. Generation of lysophosphatidylcholine (LPC) in such systems cannot be assigned to any of these types of enzymes unless the position of the fatty acid in the lysocompound can be unambiguously determined. We here present a simple method to achieve this purpose. It is based on the initial chemical acylation of the isolated LPC with a labeled fatty acid, followed by the enzymatic analysis of the resulting phosphatidylcholine (PC), using snake or bee venom phospholipase A2. Thus, if treatment of the PC with this enzyme releases a labeled free fatty acid, it is demonstrated that the initial LPC was acylated at position sn-1, whereas if the product of hydrolysis yields labeled LPC, then the initial LPC was acylated at position sn-2. This is the first method devised to determine the source of LPC in the presence of mixtures of phospholipases A1 and A2 in complex biological systems.
format JOUR
author Florin-Christensen, J.
Narvaez-Vasquez, J.
Florin-Christensen, M.
Ryan, C.A.
author_facet Florin-Christensen, J.
Narvaez-Vasquez, J.
Florin-Christensen, M.
Ryan, C.A.
author_sort Florin-Christensen, J.
title A method for distinguishing 1-acyl from 2-acyl lysophosphatidylcholines generated in biological systems
title_short A method for distinguishing 1-acyl from 2-acyl lysophosphatidylcholines generated in biological systems
title_full A method for distinguishing 1-acyl from 2-acyl lysophosphatidylcholines generated in biological systems
title_fullStr A method for distinguishing 1-acyl from 2-acyl lysophosphatidylcholines generated in biological systems
title_full_unstemmed A method for distinguishing 1-acyl from 2-acyl lysophosphatidylcholines generated in biological systems
title_sort method for distinguishing 1-acyl from 2-acyl lysophosphatidylcholines generated in biological systems
url http://hdl.handle.net/20.500.12110/paper_00032697_v276_n1_p13_FlorinChristensen
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