Fenretinide binding to the lysosomal protein saposin D alters ceramide solubilization and hydrolysis-Reference-Cited by-同舟云学术

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

Published:2020 Issue:9 Volume:11 Page:1048-1052
ISSN:2632-8682
Container-title:RSC Medicinal Chemistry
language:en
Short-container-title:RSC Med. Chem.

Author:

Milliken Brandon T.¹²³⁴,Melegari Lindy¹²³⁴,Smith Gideon L.¹⁵⁶⁴,Grohn Kris⁷⁸⁴^ORCID,Wolfe Aaron J.⁷⁸⁴⁹⁸^ORCID,Moody Kelsey⁷⁸⁴⁹⁸,Bou-Abdallah Fadi¹⁵⁶⁴^ORCID,Doyle Robert P.¹²³⁴¹⁰^ORCID

Affiliation:

1. Department of Chemistry

2. Syracuse University

3. Syracuse

4. USA

5. State University of New York

6. Potsdam

7. Ichor Therapeutics, Inc

8. Lafayette

9. Lysoclear Inc.

10. Department of Medicine

Abstract

Fenretinide is a synthetic retinoid pharmaceutical linked to ceramide build-upin vivo.

Funder

National Institutes of Health

Publisher

Royal Society of Chemistry (RSC)

Subject

Organic Chemistry,Drug Discovery,Pharmaceutical Science,Pharmacology,Molecular Medicine,Biochemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2020/MD/D0MD00182A

Reference24 articles.

1. Saposin D: A sphingomyelinase activator

2. Saposins: structure, function, distribution, and molecular genetics.

3. Glycosphingolipids and sphingolipid activator proteins: Cell biology, biochemistry and molecular genetics

4. Lysosomal Proteolysis of Prosaposin, the Precursor of Saposins (Sphingolipid Activator Proteins): Its Mechanism and Inhibition by Ganglioside

5. Mutation in saposin D domain of sphingolipid activator protein gene causes urinary system defects and cerebellar Purkinje cell degeneration with accumulation of hydroxy fatty acid-containing ceramide in mouse