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J Biol Chem, Vol. 274, Issue 6, 3651-3658, February 5, 1999
From the Christian Albrechts Universität zu Kiel,
Biochemisches Institut, Olshausenstrasse 40, D-24098 Kiel, Germany
The critical step in lysosomal targeting of
soluble lysosomal enzymes is the recognition by an
UDP-N-acetylglucosamine:lysosomal enzyme-N-acetylglucosamine-1-phosphotransferase. The
structure of the determinant common to all lysosomal enzymes for proper recognition by the phosphotransferase is not completely understood. Our
current knowledge is largely based on the introduction of targeted
amino acid substitutions into lysosomal enzymes and analysis of their
effects on phosphotransferase recognition. We have investigated the
effect of eight anti-arylsulfatase A monoclonal antibodies on the
interaction of arylsulfatase A with the lysosomal enzyme phosphotransferase in vitro. We also show that a
lysine-rich surface area of arylsulfatases A and B is essential for
proper recognition by the phosphotransferase. Monoclonal antibodies
bind to at least six different epitopes at different locations on the
surface of arylsulfatase A. All antibodies bind outside the lysine-rich
recognition area, but nevertheless Fab fragments of these antibodies
prevent interaction of arylsulfatase A with the phosphotransferase. Our data support a model in which binding of arylsulfatase A to the phosphotransferase is not restricted to a limited surface area but
involves the simultaneous recognition of large parts of arylsulfatase A.
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