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Saposin D solubilizes anionic phospholipid-containing membranes.

F Ciaffoni¹, R Salvioli, M Tatti

¹Department of Metabolism and Pathological Biochemistry, Istituto Superiore Sanita', Viale Regina Elena 299, 00161 Rome, Italy.

The Journal of Biological Chemistry

|June 15, 2001

Summary

Saposin D, a lysosomal protein, interacts with anionic phospholipid membranes in acidic environments. This interaction causes membrane solubilization, breaking down vesicles into smaller particles.

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Area of Science:

Biochemistry
Cell Biology
Molecular Biology

Background:

Saposin D (Sap D) is a lysosomal protein derived from prosaposin.
Its physiological function and mechanism of action remain largely unknown.
Sap B and Sap C have known roles in sphingolipid hydrolysis.

Purpose of the Study:

To elucidate the mechanism of Sap D interaction with membranes.
To investigate the functional role of Sap D in the late endosomal/lysosomal environment.

Main Methods:

Gel filtration
Density gradient centrifugation
Negative staining electron microscopy
Vesicle turbidity assays

Main Results:

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Sap D's superficial hydrophobicity increases at low pH, triggering interaction with anionic phospholipid vesicles.
Sap D solubilizes membranes by transforming large vesicles into smaller particles.
Sap D's activity is dependent on pH, lipid/saposin ratio, and anionic phospholipids.

Conclusions:

Sap D mediates a complex membrane interaction process.
Anionic phospholipids attract Sap D, leading to membrane breakdown into smaller, lipid-enriched particles.
Sap D may play a general role in solubilizing intralysosomal/late endosomal membranes, beyond sphingolipid degradation.