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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Vydané v:	Lipids Ročník 51; číslo 2; s. 263 - 270
Hlavní autori:	Yamashita, Ryouhei, Tabata, Yumika, Iga, Erina, Nakao, Michiyasu, Sano, Shigeki, Kogure, Kentaro, Tokumura, Akira, Tanaka, Tamotsu
Médium:	Journal Article
Jazyk:	English
Vydavateľské údaje:	Berlin/Heidelberg Springer Berlin Heidelberg 01.02.2016 Springer Nature B.V
Predmet:	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
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Shrnutí:	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.
Bibliografia:	http://dx.doi.org/10.1007/s11745-015-4082-0 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23
ISSN:	0024-4201 1558-9307 1558-9307
DOI:	10.1007/s11745-015-4082-0