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Saposin D: a sphingomyelinase activator.

S Morimoto¹, B M Martin, Y Kishimoto

¹Department of Neurosciences, School of Medicine, University of California, San Diego, La Jolla 92093.

Biochemical and Biophysical Research Communications

|October 14, 1988

Summary

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Saposin D, a heat-stable glycoprotein, was isolated and purified. This protein specifically stimulates acid sphingomyelinase, an enzyme crucial for lipid metabolism.

Area of Science:

Biochemistry
Glycoprotein Research
Enzyme Stimulation

Background:

Gaucher disease involves lipid accumulation due to enzyme deficiency.
Saposin proteins are activators of lysosomal hydrolases.
Saposin D is a newly identified member of the saposin family.

Purpose of the Study:

To isolate and characterize Saposin D.
To determine the enzymatic activity of Saposin D.
To elucidate the role of Saposin D in sphingolipid metabolism.

Main Methods:

Isolation and purification of Saposin D from Gaucher spleen.
Chemical sequencing of Saposin D.
Enzyme assays to test Saposin D's effect on hydrolases.

Related Experiment Videos

Main Results:

Saposin D was purified to homogeneity as a heat-stable 10 kDa glycoprotein.
Amino acid sequencing confirmed Saposin D as the fourth domain of prosaposin.
Saposin D specifically stimulated acid sphingomyelinase activity.

Conclusions:

Saposin D is a functional domain of prosaposin.
Saposin D plays a specific role in activating acid sphingomyelinase.
Further research into Saposin D's function may offer therapeutic insights for lysosomal storage disorders.