Cellular localization of soluble and membrane-bound forms of arylsulfatase in rat brain

Brain Res. 1987 Sep 1;419(1-2):141-6. doi: 10.1016/0006-8993(87)90577-4.

Abstract

The cellular localization of the soluble and membrane-bound forms of the enzyme, arylsulfatase (ArS), in rat brain was investigated by measuring their activities in rat striatum after unilateral lesioning with the neurotoxin, kainic acid. Membrane-bound ArS (C form of ArS) activity was found to increase after lesioning and the increase paralleled that of the astroglial marker enzyme, glutamine synthetase. Total soluble ArS (A and B forms of ArS) was shown to decrease on day 2 after the kainic acid injection but rapidly increase thereafter. When the two soluble forms of arylsulfatase were measured separately, the activity associated with the A form was found to initially decrease followed by a rapid increase in activity, whereas the activity of the B form of the enzyme increased over the entire duration of the experiment. These data suggest that the ArS-C and B form of arylsulfatase predominate in proliferating astroglial cells, whereas the A form of arylsulfatase is present both in neuronal cell bodies and astroglia associated with the rat striatum.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Arylsulfatases / metabolism*
  • Cerebroside-Sulfatase / metabolism*
  • Chondro-4-Sulfatase / metabolism*
  • Corpus Striatum / enzymology*
  • Kainic Acid
  • Male
  • Membrane Proteins / metabolism*
  • Rats
  • Rats, Inbred Strains
  • Solubility
  • Steryl-Sulfatase
  • Sulfatases / metabolism*
  • Time Factors

Substances

  • Membrane Proteins
  • Sulfatases
  • Arylsulfatases
  • Steryl-Sulfatase
  • Cerebroside-Sulfatase
  • Chondro-4-Sulfatase
  • Kainic Acid