Analysis of Molecular Species Profiles of Ceramide-1-phosphate and Sphingomyelin Using MALDI-TOF Mass Spectrometry

Ceramide-1-phosphate (C1P) is a potential signaling molecule that modulates various cellular functions in animals. It has been known that C1P with different N-acyl lengths induce biological responses differently. However, molecular species profiles of the C1P in animal tissues have not been extensiv...

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Veröffentlicht in:Lipids Jg. 51; H. 2; S. 263 - 270
Hauptverfasser: Yamashita, Ryouhei, Tabata, Yumika, Iga, Erina, Nakao, Michiyasu, Sano, Shigeki, Kogure, Kentaro, Tokumura, Akira, Tanaka, Tamotsu
Format: Journal Article
Sprache:Englisch
Veröffentlicht: Berlin/Heidelberg Springer Berlin Heidelberg 01.02.2016
Springer Nature B.V
Schlagworte:
Animal tissues
Animals
Biomedical and Life Sciences
brain
Brain Chemistry
Ceramides - chemistry
Ceramides - classification
Ceramide‐1‐phosphate
desorption
Intestine, Small - chemistry
Ionization
Kidney - chemistry
Kidneys
Life Sciences
Lipidology
liver
Liver - chemistry
Liver - metabolism
Mass spectrometry
matrix-assisted laser desorption-ionization mass spectrometry
Matrix‐assisted laser desorption/ionization time‐of‐flight mass spectrometry
Medical Biochemistry
Medicinal Chemistry
Methods
Mice
Microbial Genetics and Genomics
Molecular species
Neurochemistry
Nutrition
phosphates
phospholipase D
Skin - chemistry
small intestine
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Sphingomyelin
sphingomyelins
Sphingomyelins - chemistry
Sphingomyelins - classification
Streptomyces chromofuscus
Tissue Distribution
Molecular species
Sphingomyelin
Ceramide-1-phosphate
Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
ISSN:0024-4201, 1558-9307, 1558-9307
Online-Zugang:Volltext
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Zusammenfassung:Ceramide-1-phosphate (C1P) is a potential signaling molecule that modulates various cellular functions in animals. It has been known that C1P with different N-acyl lengths induce biological responses differently. However, molecular species profiles of the C1P in animal tissues have not been extensively examined yet. Here, we developed a method for determination of the molecular species of a C1P using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry with Phos-tag, a phosphate capture molecule. The amounts of total C1P in skin, brain, liver, kidney and small intestine of mice were determined to be 344, 151, 198, 96 and 90 pmol/g wet weight, respectively. We found a C1P species having an α-hydroxypalmitoyl residue (h-C1P, 44 pmol/g wet weight) in mouse skin. The h-C1P was detected only in the skin, and not other tissues of mice. The same analysis was applied to sphingomyelin after conversion of sphingomyelin to C1P by Streptomyces chromofuscus phospholipase D. We found that molecular species profiles of sphingomyelin in skin, kidney and small intestine of mice were similar to those of C1P in corresponding tissues. In contrast, molecular species profiles of sphingomyelin in liver and brain were quite different from those of C1P in these tissues, indicating selective synthesis or degradation of C1P in these tissues. The method described here will be useful for detection of changes in molecular species profiles of C1P and sphingomyelin.
Bibliographie:http://dx.doi.org/10.1007/s11745-015-4082-0
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ISSN:0024-4201
1558-9307
1558-9307
DOI:10.1007/s11745-015-4082-0