Carboxyl-Terminal Disulfide Bond of Acid Sphingomyelinase Is Critical for Its Secretion and Enzymatic Function

Author:

Lee Ching Yin1,Tamura Taku1,Rabah Nadia1,Lee Dong-Young Donna1,Ruel Isabelle1,Hafiane Anouar1,Iatan Iulia1,Nyholt Dana1,Laporte Frédéric1,Lazure Claude1,Wada Ikuo1,Krimbou Larbi1,Genest Jacques1

Affiliation:

1. Cardiovascular Genetics Laboratory, Cardiology Division, McGill University Health Center/Royal Victoria Hospital, Montréal, Québec H3A 1A1, Canada, Department of Cell Science, Institute of Biomedical Sciences, Fukushima Medical University School of Medicine, Fukushima, Japan, Laboratory of Structure and Metabolism of Neuropeptides, Institut de recherches cliniques de Montreal, Montréal, Canada, and Cell Map Laboratory, McGill University, Montréal, Canada

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Reference58 articles.

1. Scriver, C. R., Beaudet, A. L., Sly, W. S., Valle, D., Childs, B., Kinzler, K. W., and Vogelstein, B., Eds. (2001)The Metabolic & Molecular Bases of Inherited Disease, Vol. III, 8th ed., pp 3371−3894, McGraw-Hill, New York.

2. Zn2+-stimulated Sphingomyelinase Is Secreted by Many Cell Types and Is a Product of the Acid Sphingomyelinase Gene

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