Lipidomic "deep profiling": An enhanced workflow to reveal new molecular species of signaling lipids

Pradeep Narayanaswamy; Sudhirkumar Shinde; Robert Sulc; Rachel Kraut; Gregory Staples; Chung Hwee Thiam; Rudolf Grimm; Börje Sellergren; Federico Torta; Markus R. Wenk

doi:10.1021/ac4039652

Lipidomic "deep profiling": An enhanced workflow to reveal new molecular species of signaling lipids

Pradeep Narayanaswamy
, Sudhirkumar Shinde
, Robert Sulc
, Rachel Kraut
, Gregory Staples
, Chung Hwee Thiam
, Rudolf Grimm
, Börje Sellergren
, Federico Torta^*
, Markus R. Wenk

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

75 Citations (Scopus)

Abstract

Current mass spectrometry-based lipidomics aims to comprehensively cover wide ranges of lipid classes. We introduce a strategy to capture phospho-monoester lipids and improve the detection of long-chain base phosphates (LCB-Ps, e.g., sphingosine-1-phosphate). Ten novel LCB-Ps (d18:2, t20:1, odd carbon forms) were discovered and characterized in tissues from human and mouse, as well in D. melanogaster and S. cerevisiae. These findings have immediate relevance for our understanding of sphingosine-1-phosphate biosynthesis, signaling, and degradation.

Original language	English
Pages (from-to)	3043-3047
Number of pages	5
Journal	Analytical Chemistry
Volume	86
Issue number	6
DOIs	https://doi.org/10.1021/ac4039652
Publication status	Published - 18 Mar 2014
Externally published	Yes

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title = "Lipidomic {"}deep profiling{"}: An enhanced workflow to reveal new molecular species of signaling lipids",

abstract = "Current mass spectrometry-based lipidomics aims to comprehensively cover wide ranges of lipid classes. We introduce a strategy to capture phospho-monoester lipids and improve the detection of long-chain base phosphates (LCB-Ps, e.g., sphingosine-1-phosphate). Ten novel LCB-Ps (d18:2, t20:1, odd carbon forms) were discovered and characterized in tissues from human and mouse, as well in D. melanogaster and S. cerevisiae. These findings have immediate relevance for our understanding of sphingosine-1-phosphate biosynthesis, signaling, and degradation.",

author = "Pradeep Narayanaswamy and Sudhirkumar Shinde and Robert Sulc and Rachel Kraut and Gregory Staples and Thiam, \{Chung Hwee\} and Rudolf Grimm and B{\"o}rje Sellergren and Federico Torta and Wenk, \{Markus R.\}",

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doi = "10.1021/ac4039652",

language = "English",

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T2 - An enhanced workflow to reveal new molecular species of signaling lipids

AU - Narayanaswamy, Pradeep

AU - Shinde, Sudhirkumar

AU - Sulc, Robert

AU - Kraut, Rachel

AU - Staples, Gregory

AU - Thiam, Chung Hwee

AU - Grimm, Rudolf

AU - Sellergren, Börje

AU - Torta, Federico

AU - Wenk, Markus R.

PY - 2014/3/18

Y1 - 2014/3/18

N2 - Current mass spectrometry-based lipidomics aims to comprehensively cover wide ranges of lipid classes. We introduce a strategy to capture phospho-monoester lipids and improve the detection of long-chain base phosphates (LCB-Ps, e.g., sphingosine-1-phosphate). Ten novel LCB-Ps (d18:2, t20:1, odd carbon forms) were discovered and characterized in tissues from human and mouse, as well in D. melanogaster and S. cerevisiae. These findings have immediate relevance for our understanding of sphingosine-1-phosphate biosynthesis, signaling, and degradation.

AB - Current mass spectrometry-based lipidomics aims to comprehensively cover wide ranges of lipid classes. We introduce a strategy to capture phospho-monoester lipids and improve the detection of long-chain base phosphates (LCB-Ps, e.g., sphingosine-1-phosphate). Ten novel LCB-Ps (d18:2, t20:1, odd carbon forms) were discovered and characterized in tissues from human and mouse, as well in D. melanogaster and S. cerevisiae. These findings have immediate relevance for our understanding of sphingosine-1-phosphate biosynthesis, signaling, and degradation.

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M3 - Article

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SN - 0003-2700

VL - 86

SP - 3043

EP - 3047

JO - Analytical Chemistry

JF - Analytical Chemistry

IS - 6

ER -

Lipidomic "deep profiling": An enhanced workflow to reveal new molecular species of signaling lipids

Abstract

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