Cloning and expression of human arylsulfatase A.
Cloning and expression of human arylsulfatase A.
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发表时间：
1989-01
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通讯作者：
C. Stein;V. Gieselmann;J. Kreysing;Bernhard Schmidt;R. Pohlmann;Abdul Waheed;Helmut E. Meyer;J. O'brien;K. Figura
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作者：
C. Stein;V. Gieselmann;J. Kreysing;Bernhard Schmidt;R. Pohlmann;Abdul Waheed;Helmut E. Meyer;J. O'brien;K. Figura
A full length cDNA for human arylsulfatase A was cloned and sequenced. The predicted amino acid sequence comprises 507 residues. A putative signal peptide of 18 residues is followed by the NH2-terminal sequence of placental arylsulfatase A. One of the arylsulfatase A peptides ends 3 residues ahead of the predicted COOH terminus. This indicates that proteolytic processing of arylsulfatase A is confined to the cleavage of the signal peptide. The predicted sequence contains three potential N-glycosylation sites, two of which are likely to be utilized. The sequence shows no homology to any of the known sequences of lysosomal enzymes but a 35% identity to human steroid sulfatase. Transfection of monkey and baby hamster kidney cells resulted in an up to 200-fold increase of the arylsulfatase A activity. The arylsulfatase A was located in lysosome-like structures and transported to dense lysosomes in a mannose 6-phosphate receptor-dependent manner. The arylsulfatase A cDNA hybridizes to 2.0- and 3.9-kilobase species in RNA from human fibroblasts and human liver. RNA species of similar size were detected in metachromatic leukodystrophy fibroblasts of two patients, in which synthesis of arylsulfatase A polypeptides was either detectable or absent.
