Activator proteins and topology of lysosomal sphingolipid catabolism

W Fürst; K Sandhoff

doi:10.1016/0005-2760(92)90210-m

Activator proteins and topology of lysosomal sphingolipid catabolism

Biochim Biophys Acta. 1992 Jun 5;1126(1):1-16. doi: 10.1016/0005-2760(92)90210-m.

Authors

W Fürst¹, K Sandhoff

Affiliation

¹ Institute for Organic Chemistry and Biochemistry, University of Bonn, Germany.

PMID: 1606169
DOI: 10.1016/0005-2760(92)90210-m

Abstract

The lysosomal degradation of several sphingolipids by acid hydrolases is dependent on small non-enzymic cofactors, called sphingolipid activator proteins some of which have been identified as sphingolipid binding proteins. This review summarizes the information available on the structure, function, biosynthesis, gene organization and pathobiochemistry of the known sphingolipid activator proteins. It also offers models for their mode of action and for the topology of lysosomal digestion of glycolipids.

Publication types

Research Support, Non-U.S. Gov't
Review

MeSH terms

Animals
Carbohydrate Sequence
G(M2) Activator Protein
Gene Expression Regulation
Glycoproteins / chemistry
Glycoproteins / genetics
Glycoproteins / metabolism*
Humans
Lysosomes / metabolism*
Models, Biological
Molecular Sequence Data
Protein Precursors / genetics
Protein Precursors / metabolism*
Proteins / metabolism*
Saposins
Sphingolipid Activator Proteins
Sphingolipids / chemistry
Sphingolipids / metabolism*

Substances

G(M2) Activator Protein
Glycoproteins
PSAP protein, human
Protein Precursors
Proteins
Saposins
Sphingolipid Activator Proteins
Sphingolipids