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Article

A novel mechanism of lysosomal acid sphingomyelinase maturation: requirement for carboxyl-terminal proteolytic processing.

The Journal of biological chemistry - 4 Feb 2011

Jenkins Russell W, Idkowiak-Baldys Jolanta, Simbari Fabio, Canals Daniel, Roddy Patrick, Riner Clarke D, Clarke Christopher J, Hannun Yusuf A

Abstract excerpt

Acid sphingomyelinase (aSMase) catalyzes the hydrolysis of sphingomyelin (SM) to form the bioactive lipid ceramide (Cer). Notably, aSMase exists in two forms: a zinc (Zn(2+))-independent lysosomal aSMase (L-SMase) and a Zn(2+)-dependent secreted aSMase (S-SMase) that arise from alternative traffi...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 21098024
DOI: 10.1074/jbc.M110.155234
PMCID: PMC3030379

Genes

LAMP1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-21098024-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

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