Activator Proteins for the Catabolism of Glycosphingolipids

A protein activator of glucosylceramidase (EC 3.2.1.45) has been previously identified by us in human placenta [(1985) Biochim. Biophys. Acta 836, 157–166]. In the present paper we report that its function in vitro is to stimulate the binding of the enzyme to its substrate, glucosylceramide. After the purification step which frees the enzyme of most of its activator protein (octyl‐Sepharose 4B chromatography), the capacity of glucosylceramidase to bind to the glucosylceramide micelles is dramatically decreased. The addition of the activator protein to the purified enzyme restores this binding.

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The binding of glucosylceramidase to glucosylceramide is promoted by its activator protein

Vaccaro

Muscillo

Salvioli

et al. 1987

FEBS Letters

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Specific ganglioside-cell protein interactions: A study performed with GM1 ganglioside derivative containing photoactivable azide and rat cerebellar granule cells in culture

Sonnino

Chigorno

Valsecchi

et al. 1992

Neurochemistry International

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Polyglycosylceramides, Poly-N-acetyllactosamine-Containing Glycosphingolipids: Methods of Analysis, Structure, and Presumable Biological Functions

Miller‐Podraza

2000

Chem. Rev.

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Activator Proteins for the Catabolism of Glycosphingolipids

Cited by 3 publications

References 21 publications

The binding of glucosylceramidase to glucosylceramide is promoted by its activator protein

The binding of glucosylceramidase to glucosylceramide is promoted by its activator protein

Specific ganglioside-cell protein interactions: A study performed with GM1 ganglioside derivative containing photoactivable azide and rat cerebellar granule cells in culture

Polyglycosylceramides, Poly-N-acetyllactosamine-Containing Glycosphingolipids: Methods of Analysis, Structure, and Presumable Biological Functions

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