Cloning and expression of human arylsulfatase A

J Biol Chem. 1989 Jan 15;264(2):1252-9.

Abstract

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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Cerebroside-Sulfatase / genetics*
  • Cloning, Molecular*
  • DNA / genetics
  • DNA Probes
  • Female
  • Genes*
  • Humans
  • Molecular Sequence Data
  • Placenta / enzymology
  • Plasmids
  • Pregnancy
  • Restriction Mapping
  • Sequence Homology, Nucleic Acid
  • Transfection

Substances

  • DNA Probes
  • DNA
  • Cerebroside-Sulfatase

Associated data

  • GENBANK/J04442
  • GENBANK/J04593