Acid sphingomyelinase possesses a domain homologous to its activator proteins: Saposins B and D
- 1 February 1994
- journal article
- research article
- Published by Wiley in Protein Science
- Vol. 3 (2) , 359-361
- https://doi.org/10.1002/pro.5560030219
Abstract
An N‐terminal region of the acid sphingomyelinase sequence (residues 89‐165) is shown to be homologous to saposintype sequences. By analogy with the known functions of saposins, this sphingomyelinase saposin‐type domain may possess lipid‐binding and/or sphingomyelinase‐activator properties. This finding may prove to be important in the understanding of Niemann‐Pick disease, which results from sphingomyelinase deficiency.Keywords
This publication has 33 references indexed in Scilit:
- A Function of Lung Surfactant Protein SP-BScience, 1993
- Identification of a 3′ acceptor splice site mutation (g2610c) in the acid sphingomyelinase gene of patients with Niemann - Pick diseaseHuman Molecular Genetics, 1993
- ALSCRIPT: a tool to format multiple sequence alignmentsProtein Engineering, Design and Selection, 1993
- Human surfactant polypeptide SP‐B Disulfide bridges, C‐terminal end, and peptide analysis of the airway formFEBS Letters, 1992
- Expression and characterization of recombinant human acyloxyacyl hydrolase, a leukocyte enzyme that deacylates bacterial lipopolysaccharidesBiochemistry, 1991
- Surfactant protein B: disulfide bridges, structural properties and kringle similaritiesBiochemistry, 1991
- Mutation in the sphingolipid activator protein 2 in a patient with a variant of Gaucher diseaseFEBS Letters, 1991
- Detection of a point mutation in sphingolipid activator protein-1 mRNA in patients with a variant form of metachromatic leukodystrophyBiochemical and Biophysical Research Communications, 1990
- Saposin D: A sphingomyelinase activatorBiochemical and Biophysical Research Communications, 1988
- Acid sphingomyelinase from human urine: purification and characterizationBiochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1987