Purification and Characterization of Mitochondrial Mg2+-Independent Sphingomyelinase from Rat Brain

Authors

Jong Min Choi
Yongwei Piao
Kyong Hoon Ahn
Seok Kyun Kim
Jong Hoon Won
Jae Hong Lee
Ji Min Jang
In Chul Shin
Zhicheng Fu
Sung Yun Jung
Eui Man Jeong
Dae Kyong Kim

Publication Date

9-30-2023

Journal

Molecules and Cells

DOI

10.14348/molcells.2023.0074

PMID

37305954

PMCID

PMC10495687

PubMedCentral® Posted Date

6-12-2023

PubMedCentral® Full Text Version

Post-print

Published Open-Access

no

Keywords

Rats, Animals, Sphingomyelins, Sphingomyelin Phosphodiesterase, Cytochromes c, Ceramides, Mitochondria, Brain

Abstract

Sphingomyelinase (SMase) catalyzes ceramide production from sphingomyelin. Ceramides are critical in cellular responses such as apoptosis. They enhance mitochondrial outer membrane permeabilization (MOMP) through self-assembly in the mitochondrial outer membrane to form channels that release cytochrome c from intermembrane space (IMS) into the cytosol, triggering caspase-9 activation. However, the SMase involved in MOMP is yet to be identified. Here, we identified a mitochondrial Mg

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