Journal
BIOSCIENCE REPORTS
Volume 38, Issue -, Pages -Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BSR20181288
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Funding
- CREST from the JST/AMED
- Leading Advanced Projects for medical innovation (LEAP) from AMED [15H05906]
- JSPS KAKENHI [16H06236]
- Research Fund of MITSUKOSHI Health and Welfare Foundation 2017
- Japan Heart Foundation
- MSD Life Science Foundation
- Public Interest Incorporated Foundation
- Astellas Grant for Research on Atherosclerosis Update
- Grants-in-Aid for Scientific Research [16H06236] Funding Source: KAKEN
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Dihydro-sphingosine 1-phosphate (DH-S1P) is an analog of sphingosine 1-phosphate (S1P), which is a potent lysophospholipid mediator. DH-S1P has been proposed to exert physiological properties similar to S1P. Although S1P is known to be carried on HDL via apolipoprotein M (apoM), the association between DH-S1P and HDL/apoM has not been fully elucidated. Therefore, in the present study, we aimed to elucidate this association and to compare it with that of S1P and HDL/apoM. First, we investigated the distributions of S1P and DH-S1P among lipoproteins and lipoprotein-depleted fractions in human serum and plasma samples and observed that both S1P and DH-S1P were detected on HDL; furthermore, elevated amounts of DH-S1P in serum samples were distributed to the lipoprotein-depleted fraction to a greater degree than to the HDL fraction. Concordantly, a preference for HDL over albumin was only observed for S1P, and not for DH-S1P, when the molecules were secreted from platelets. Regarding the association with HDL, although both S1P and DH-S1P prefer to bind to HDL, HDL preferentially accepts S1P over DH-S1P. For the association with apoM, S1P was not detected on HDL obtained from apoM knockout mice, while DH-S1P was detected. Moreover, apoM retarded the degradation of S1P, but not of DH-S1P. These results suggest that S1P binds to HDL via apoM, while DH-S1P binds to HDL in a non-specific manner. Thus, DH-S1P is not a mere analog of S1P and might possess unique clinical significance.
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