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Supramolecular assemblies from lysosomal matrix proteins and complex lipids

M Jadot¹, F Dubois, S Wattiaux-De Coninck

¹Laboratoire de Chimie Physiologique, Facultés Universitaires Notre-Dame de la Paix, Namur, Belgium. michel.jadot@fundp.ac.be

European Journal of Biochemistry

|December 12, 1997

Summary

Lysosomal proteins, including lysosome-associated membrane protein-II, aggregate at acidic pH, forming complexes with lipids. This intralysosomal matrix formation may impact organelle function.

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Area of Science:

Cell Biology
Biochemistry
Lysosome Biology

Background:

Lysosomal hydrolases are typically soluble enzymes.
Lysosome-associated membrane protein-II (Lamp-II) is a key lysosomal membrane protein.

Purpose of the Study:

To investigate the aggregation of lysosomal molecules, particularly lysosomal enzymes and Lamp-II.
To understand the role of intralysosomal pH and lipids in protein aggregation within lysosomes.

Main Methods:

Studied aggregation of lysosomal marker enzymes and Lamp-II at varying pH.
Investigated the pH-dependent solubility of Lamp-II using lysosome extracts.
Analyzed complex formation between proteins and lysosomal lipids.
Fractionated lysosome extracts and reconstituted assemblies in vitro.

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Main Results:

Lysosomal enzymes and Lamp-II showed optimal aggregation at intralysosomal pH (around pH 5.0).
Lamp-II aggregation and loss of solubility were dependent on lysosome extract components.
Mild acidic pH induced the formation of complexes between lysosomal proteins and lipids.
Specific lipids like phosphatidylcholine, sphingomyelin, and phosphatidylethanolamine were effective in binding lysosomal proteins.

Conclusions:

Supramolecular assemblies of lysosomal proteins and lipids form within the lysosome at acidic pH.
This intralysosomal matrix formation, driven by pH and lipid interactions, may influence lysosomal function.