Murine arylsulfatase C: evidence for two isozymes

Area of Science:

• Biochemistry
• Genetics
• Enzymology

Background:

• Sulfatase enzymes play crucial roles in various biological processes.
• Significant variations in sulfatase activities exist between different mouse strains.
• Arylsulfatase C (ASC) exhibits distinct biochemical properties and subcellular localization.

Purpose of the Study:

• To investigate the genetic basis for interstrain differences in sulfatase activities in mice.
• To characterize the biochemical properties and distributions of murine ASC isozymes.
• To determine the relationship between ASC isozymes and steroid sulfatase activity.

Main Methods:

• Comparative analysis of arylsulfatase C, estrone sulfatase, and dehydroepiandrosterone sulfatase activities in SWR/J and A/J mice.
• Biochemical characterization of hydrophobic and hydrophilic ASC isozymes.
• Assessment of subcellular distribution of ASC isozymes in different tissues.

Main Results:

• SWR/J mice exhibit significantly higher ASC, estrone sulfatase, and dehydroepiandrosterone sulfatase activities than A/J mice.
• Murine ASC exists as hydrophobic and hydrophilic isozymes with distinct properties and distributions.
• The hydrophobic ASC isozyme is identical to steroid sulfatase, while the hydrophilic form lacks this activity.
• A single autosomal gene appears to regulate the activity of both ASC isozymes.

Conclusions:

• Interstrain differences in sulfatase activities are genetically determined by at least one autosomal gene.
• The gene(s) influencing sulfatase activity affect both hydrophobic and hydrophilic ASC isozymes.
• Understanding these genetic variations provides insights into sulfatase enzyme regulation and function.