1H NMR at 800 MHz facilitates detailed phospholipid follow-up during atherogenic modifications in low density lipoproteins

Pasi Soininen, K. Öörni, Hannu Maaheimo, R. Laatikainen, P. T. Kovanen, K. Kaski, M. Ala-Korpela (Corresponding Author)

Research output: Contribution to journalArticleScientificpeer-review

12 Citations (Scopus)

Abstract

The structure of low density lipoprotein (LDL) particles and, particularly, the enzymatic and oxidative modifications of their surface is crucial in the initiation of atherosclerosis. Due to the structural complexity of LDL, there is a lack of suitable methods for dynamic follow-up studies of the molecular mechanisms in native and modified particles in physiological conditions. Here, we report that phosphatidylcholine (PC), lysophosphatidylcholine (lyso-PC), and sphingomyelin (SM) can all be identified and quantified in LDL particles by 1H NMR spectroscopy at 800 MHz. The signal assignment for the lyso-PC is novel and we illustrate the applicability of the methodology in the case of lipid peroxidation that is generally considered as one of the key proatherogenic modifications of LDL. It was found, somewhat surprisingly, that the LDL-associated phospholipase A2 is activated in the very beginning of the formation of PC-hydroperoxides. The (patho)physiological rationale of the resulting lyso-PC generation is also briefly discussed.
Original languageEnglish
Pages (from-to)290-294
JournalBiochemical and Biophysical Research Communications
Volume360
Issue number1
DOIs
Publication statusPublished - 2007
MoE publication typeA1 Journal article-refereed

Fingerprint

LDL Lipoproteins
Phospholipids
Lysophosphatidylcholines
Nuclear magnetic resonance
1-Alkyl-2-acetylglycerophosphocholine Esterase
Sphingomyelins
Phosphatidylcholines
Lipid Peroxidation
Nuclear magnetic resonance spectroscopy
Atherosclerosis
Magnetic Resonance Spectroscopy
Proton Magnetic Resonance Spectroscopy
Lipids

Keywords

  • LDL
  • Lipoproteins
  • NMR spectroscopy
  • Phosphatidylcholine
  • Lysophosphatidylcholine
  • Sphingomyelin
  • Phospholipase A2
  • Lipoprotein-associated phospholipase A2
  • Lipid peroxidation
  • Atherosclerosis
  • Lipoprotein accumulation
  • Lipoprotein modifications

Cite this

Soininen, Pasi ; Öörni, K. ; Maaheimo, Hannu ; Laatikainen, R. ; Kovanen, P. T. ; Kaski, K. ; Ala-Korpela, M. / 1H NMR at 800 MHz facilitates detailed phospholipid follow-up during atherogenic modifications in low density lipoproteins. In: Biochemical and Biophysical Research Communications. 2007 ; Vol. 360, No. 1. pp. 290-294.
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abstract = "The structure of low density lipoprotein (LDL) particles and, particularly, the enzymatic and oxidative modifications of their surface is crucial in the initiation of atherosclerosis. Due to the structural complexity of LDL, there is a lack of suitable methods for dynamic follow-up studies of the molecular mechanisms in native and modified particles in physiological conditions. Here, we report that phosphatidylcholine (PC), lysophosphatidylcholine (lyso-PC), and sphingomyelin (SM) can all be identified and quantified in LDL particles by 1H NMR spectroscopy at 800 MHz. The signal assignment for the lyso-PC is novel and we illustrate the applicability of the methodology in the case of lipid peroxidation that is generally considered as one of the key proatherogenic modifications of LDL. It was found, somewhat surprisingly, that the LDL-associated phospholipase A2 is activated in the very beginning of the formation of PC-hydroperoxides. The (patho)physiological rationale of the resulting lyso-PC generation is also briefly discussed.",
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1H NMR at 800 MHz facilitates detailed phospholipid follow-up during atherogenic modifications in low density lipoproteins. / Soininen, Pasi; Öörni, K.; Maaheimo, Hannu; Laatikainen, R.; Kovanen, P. T.; Kaski, K.; Ala-Korpela, M. (Corresponding Author).

In: Biochemical and Biophysical Research Communications, Vol. 360, No. 1, 2007, p. 290-294.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

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AU - Soininen, Pasi

AU - Öörni, K.

AU - Maaheimo, Hannu

AU - Laatikainen, R.

AU - Kovanen, P. T.

AU - Kaski, K.

AU - Ala-Korpela, M.

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N2 - The structure of low density lipoprotein (LDL) particles and, particularly, the enzymatic and oxidative modifications of their surface is crucial in the initiation of atherosclerosis. Due to the structural complexity of LDL, there is a lack of suitable methods for dynamic follow-up studies of the molecular mechanisms in native and modified particles in physiological conditions. Here, we report that phosphatidylcholine (PC), lysophosphatidylcholine (lyso-PC), and sphingomyelin (SM) can all be identified and quantified in LDL particles by 1H NMR spectroscopy at 800 MHz. The signal assignment for the lyso-PC is novel and we illustrate the applicability of the methodology in the case of lipid peroxidation that is generally considered as one of the key proatherogenic modifications of LDL. It was found, somewhat surprisingly, that the LDL-associated phospholipase A2 is activated in the very beginning of the formation of PC-hydroperoxides. The (patho)physiological rationale of the resulting lyso-PC generation is also briefly discussed.

AB - The structure of low density lipoprotein (LDL) particles and, particularly, the enzymatic and oxidative modifications of their surface is crucial in the initiation of atherosclerosis. Due to the structural complexity of LDL, there is a lack of suitable methods for dynamic follow-up studies of the molecular mechanisms in native and modified particles in physiological conditions. Here, we report that phosphatidylcholine (PC), lysophosphatidylcholine (lyso-PC), and sphingomyelin (SM) can all be identified and quantified in LDL particles by 1H NMR spectroscopy at 800 MHz. The signal assignment for the lyso-PC is novel and we illustrate the applicability of the methodology in the case of lipid peroxidation that is generally considered as one of the key proatherogenic modifications of LDL. It was found, somewhat surprisingly, that the LDL-associated phospholipase A2 is activated in the very beginning of the formation of PC-hydroperoxides. The (patho)physiological rationale of the resulting lyso-PC generation is also briefly discussed.

KW - LDL

KW - Lipoproteins

KW - NMR spectroscopy

KW - Phosphatidylcholine

KW - Lysophosphatidylcholine

KW - Sphingomyelin

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KW - Lipoprotein-associated phospholipase A2

KW - Lipid peroxidation

KW - Atherosclerosis

KW - Lipoprotein accumulation

KW - Lipoprotein modifications

U2 - 10.1016/j.bbrc.2007.06.058

DO - 10.1016/j.bbrc.2007.06.058

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VL - 360

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JO - Biochemical and Biophysical Research Communications

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