Clinical biochemistry · 2007
Isoenzyme pattern and partial characterization of hexosaminidases in the membrane and cytosol of human erythrocytes.
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Massaccesi Luca, Lombardo Adriana, Venerando Bruno, Tettamanti Guido, Goi Giancarlo
Аннотация
OBJECTIVES: Hexosaminidase activity is present in lysosomes, plasma membrane and cytosol of many human cells. Plasma membrane and cytosolic hexosaminidase is not well characterized, particularly as regards their isoenzyme forms and their relationship with the lysosomal ones.
DESIGN AND METHODS: Erythrocyte hexosaminidase isoforms were chromatographically separated, characterized and compared to those in the plasma of healthy individuals and in the erythrocytes of a Tay-Sachs patient.
RESULTS: Hexosaminidase isoenzymes were found in plasma membrane and cytosol and were composed of the same alpha- and beta-subunits as the lysosomal and plasma hexosaminidase A and B isoenzymes, though with some structural and kinetic differences. In addition, the cytosol contained a hexosaminidase that is a specific N-acetyl-beta-D-glucosaminidase, the one involved in the removal of N-acetylglucosamine residues O-linked to proteins, named O-GlcNAcase.
CONCLUSIONS: This work provides an additional step in the characterization of hexosaminidases helping better understand their role in non-lysosomal compartments and their involvement in physiological or pathological situations.
DESIGN AND METHODS: Erythrocyte hexosaminidase isoforms were chromatographically separated, characterized and compared to those in the plasma of healthy individuals and in the erythrocytes of a Tay-Sachs patient.
RESULTS: Hexosaminidase isoenzymes were found in plasma membrane and cytosol and were composed of the same alpha- and beta-subunits as the lysosomal and plasma hexosaminidase A and B isoenzymes, though with some structural and kinetic differences. In addition, the cytosol contained a hexosaminidase that is a specific N-acetyl-beta-D-glucosaminidase, the one involved in the removal of N-acetylglucosamine residues O-linked to proteins, named O-GlcNAcase.
CONCLUSIONS: This work provides an additional step in the characterization of hexosaminidases helping better understand their role in non-lysosomal compartments and their involvement in physiological or pathological situations.