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Citations to this article

Apolipoprotein C-III-1 activates lysosomal sphingomyelinase in vitro.
A J Alpert, A L Beaudet
A J Alpert, A L Beaudet
Published December 1, 1981
Citation Information: J Clin Invest. 1981;68(6):1592-1596. https://doi.org/10.1172/JCI110414.
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Research Article

Apolipoprotein C-III-1 activates lysosomal sphingomyelinase in vitro.

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Abstract

Apolipoprotein (apo)C-III-1 from human very low density lipoprotein stimulates 14-fold the activity of lysosomal sphingomyelinase from human fibroblasts. At the sphingomyelin concentrations tested, maximal stimulation was obtained with 5 microM apoC-III-1 or apoC mixture. Apolipoproteins A-I, A-II, B, and C-I conferred little or no stimulation. Sphingomyelinase was stimulated 20-fold by lysophosphatidylcholine with an optimum concentration of 70 microM using 0.3 mM substrate. Sphingomyelinase activity was inhibited by concentrations of apoC-III-1 and lysophosphatidylcholine three- to fivefold above stimulatory levels. Triton X-100 activated sphingomyelinase 300-fold with a pH optimum of 5.0, while the pH optimum with the biological activators was 4.0. These results raise the possibility of an in vivo activity for the biological activators. The proteins that enter lysosomes as part of a lipoprotein complex may activate lysosomal enzymes that degrade the lipid components.

Authors

A J Alpert, A L Beaudet

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Total citations by year

Year: 2021 2004 1999 1996 1991 1988 1987 1986 1983 Total
Citations: 1 1 1 1 1 2 1 2 1 11
Citation information
This citation data is accumulated from CrossRef, which receives citation information from participating publishers, including this journal. Not all publishers participate in CrossRef, so this information is not comprehensive. Additionally, data may not reflect the most current citations to this article, and the data may differ from citation information available from other sources (for example, Google Scholar, Web of Science, and Scopus).

Citations to this article (11)

Title and authors Publication Year
Recent advances in 1,8-naphthalimide-based small-molecule fluorescent probes for organelles imaging and tracking in living cells
H Yu, Y Guo, W Zhu, K Havener, X Zheng
Coordination Chemistry Reviews 2021
Acid and neutral sphingomyelinases: roles and mechanisms of regulation
N Marchesini, YA Hannun
Biochemistry and Cell Biology 2004
Semi-Automated Rapid Isoelectric Focusing of Apolipoproteins C from Human Plasma Using PhastSystem™ and Immunofixation
B Noll, R Hackler, M Pelzer, S Pelzer, P Nusser, B Maisch, JR Schaefer, A Steinmetz
Clinical Chemistry and Laboratory Medicine 1999
Biology of the Lysosome
JB Lloyd, RW Mason
1996
Human Placental Sphingomyelinase. Purification to Homogeneity, Antigenic Properties and Partial Amino-Acid Sequences of the Enzyme
J KURTH, W STOFFEL
Biological Chemistry Hoppe-Seyler 1991
Analysis of the multiple forms of Gaucher spleen sphingolipid activator protein 2
BC Paton, A Poulos
Biochemical Journal 1988
Der Internist
E Buchborn, M Classen, W Dölle, R Gross, J van de Loo, G Riecker, PC Scriba, W Siegenthaler, P von Wichert
Der Internist 1988
Polymorphism of human plasma apolipoprotein C-III at birth and in early neonatal life
WJ McConathy, MA McCaffree, DM Lane
Journal of lipid research 1987
Human lysosomal sphingomyelinase: substrate efficacy of apolipoprotein/sphingomyelin complexes
TY Ahmad, AL Beaudet, JT Sparrow, JD Morrisett
Biochemistry 1986
Apolipoprotein C-III/sphingomyelin recombinants: formation, isolation, and characterization
TY Ahmad, JR Guyton, JT Sparrow, JD Morrisett
Biochemistry 1986
Concentrations of an activator protein for sphingolipid hydrolysis in liver and brain samples from patients with lysosomal storage diseases
K Inui, DA Wenger
Journal of Clinical Investigation 1983

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