Accessible Requires Authentication Published by De Gruyter May 20, 2015

High β-glucosidase (GBA) activity not attributable to GBA1 and GBA2 in live normal and enzyme-deficient fibroblasts may emphasise the role of additional GBAs

Klaus Harzer and Yildiz Yildiz
From the journal Biological Chemistry


Beta-glucosidases (GBA) include GBA1, GBA2 and other β-glucosidases (non-GBA1-2). GBA1 is a lysosomal and GBA2 an extra-lysosomal enzyme. GBA1- and GBA2-deficient genetic conditions, with different phenotypes, are glucosylceramide (GC; the main GBA substrate) accumulating diseases. To study the activity profile of GBA, live fibroblasts were loaded with radioactive GC. The GC metabolism was measured in wild-type, GBA1-deficient (Gaucher disease) and GBA2-deficient (Gba2-/- mouse) cells. The differences found allowed the prediction of marked proportions of GBA1, GBA2, and particularly non-GBA1-2 (probably including GBA3, a cytosolic β-glucosidase) activity for wild-type cells. The high proportion of non-GBA1-2 suggests an important role of these enzymes.

Corresponding author: Klaus Harzer, Neurometabolic Laboratory, Children’s Hospital, University of Tübingen, Hoppe-Seyler-Str. 1, D-72076 Tübingen, Germany, e-mail:


The work was supported by Deutsche Forschungsgemeinschaft Grants DFG YI 100/1 and SFB 645. We thank Dr. B. Kustermann-Kuhn, G. Merkel and M. Pechan, Neurometabolic Laboratory, Children’s Hospital, University of Tübingen, Germany, for help with cell cultures; and Dr. A. Rolfs, Department of Neurology, University of Rostock, Germany, for gene analysis of patients 2GD1, 3GD1 and 4GD1.


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Received: 2015-3-21
Accepted: 2015-5-12
Published Online: 2015-5-20
Published in Print: 2015-11-1

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