Mammalian cells contain a second nucleocytoplasmic hexosaminidase.

The Biochemical journal (2008-12-02)
Martin Gutternigg, Dubravko Rendić, Regina Voglauer, Thomas Iskratsch, Iain B H Wilson
ABSTRACT

Some thirty years ago, work on mammalian tissues suggested the presence of two cytosolic hexosaminidases in mammalian cells; one of these has been more recently characterized in a recombinant form and has an important role in cellular function due to its ability to cleave beta-N-acetylglucosamine residues from a variety of nuclear and cytoplasmic proteins. However, the molecular nature of the second cytosolic hexosaminidase, named hexosaminidase D, has remained obscure. In the present study, we molecularly characterize for the first time the human and murine recombinant forms of enzymes, encoded by HEXDC genes, which appear to correspond to hexosaminidase D in terms of substrate specificity, pH dependency and temperature stability. Furthermore, a Myc-tagged form of this novel hexosaminidase displays a nucleocytoplasmic localization. Transcripts of the corresponding gene are expressed in a number of murine tissues. On the basis of its sequence, this enzyme represents, along with the lysosomal hexosaminidase subunits encoded by the HEXA and HEXB genes, the third class 20 glycosidase to be identified from mammalian sources.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Total Protein Kit, Micro Lowry, Peterson′s Modification
Sigma-Aldrich
Anti-HEXDC antibody produced in mouse, purified immunoglobulin, buffered aqueous solution
Sigma-Aldrich
Anti-HEXDC antibody produced in rabbit, Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution, Ab1
Sigma-Aldrich
Anti-HEXDC antibody produced in rabbit, Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution, Ab2