Identification of ApoA4 as a sphingosine 1-phosphate chaperone in ApoM- and albumin-deficient mice [Research Articles]

In this study, we report the identification of ApoA4 as a novel S1P binding protein. Recombinant ApoA4 bound to S1P, activated multiple S1P receptors, and promoted vascular endothelial barrier function, all reflective of its function as a S1P chaperone in the absence of ApoM and albumin. We suggest that multiple S1P chaperones evolved to support complex and essential extracellular signaling functions of this lysolipid mediator in a redundant manner.

Source: The Journal of Lipid Research - October 31, 2019 Category: Lipidology Authors: Obinata, H., Kuo, A., Wada, Y., Swendeman, S., Liu, C. H., Blaho, V. A., Nagumo, R., Satoh, K., Izumi, T., Hla, T. Tags: Research Articles Source Type: research