Unknown

Dataset Information

0

Fenretinide binding to the lysosomal protein saposin D alters ceramide solubilization and hydrolysis.


ABSTRACT: Fenretinide is a synthetic retinoid pharmaceutical linked to ceramide build-up in vivo. Saposin D is an intralysosomal protein necessary for ceramide binding/degradation. We show, via electronic absorption spectroscopy, fluorescence spectroscopy, and ceramide hydrolysis assays, that fenretinide is bound by saposin D {K a = (1.45 ± 0.49) × 105 M-1}, and affects ceramide solubilization/degradation.

SUBMITTER: Milliken BT 

PROVIDER: S-EPMC7513591 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature

altmetric image

Publications

Fenretinide binding to the lysosomal protein saposin D alters ceramide solubilization and hydrolysis.

Milliken Brandon T BT   Melegari Lindy L   Smith Gideon L GL   Grohn Kris K   Wolfe Aaron J AJ   Moody Kelsey K   Bou-Abdallah Fadi F   Doyle Robert P RP  

RSC medicinal chemistry 20200714 9


Fenretinide is a synthetic retinoid pharmaceutical linked to ceramide build-up <i>in vivo</i>. Saposin D is an intralysosomal protein necessary for ceramide binding/degradation. We show, <i>via</i> electronic absorption spectroscopy, fluorescence spectroscopy, and ceramide hydrolysis assays, that fenretinide is bound by saposin D {<i>K</i> <sub>a</sub> = (1.45 ± 0.49) × 10<sup>5</sup> M<sup>-1</sup>}, and affects ceramide solubilization/degradation. ...[more]

Similar Datasets

| S-EPMC5558615 | biostudies-literature
| S-EPMC4498711 | biostudies-literature
| S-EPMC10052200 | biostudies-literature
| S-EPMC3366851 | biostudies-literature
| S-EPMC8533494 | biostudies-literature
| S-EPMC2266064 | biostudies-literature
| S-EPMC1838443 | biostudies-literature
| S-EPMC9307309 | biostudies-literature
| S-EPMC7073989 | biostudies-literature
| S-EPMC8072984 | biostudies-literature