Abstract

Purified human liver arylsulfatase A (ASA) as well as an ASA peptide (residues 28-39) were sulfated by tyrosyl protein sulfotransferase in vitro. The media, but not the cell lysate, of normal human fibroblasts contained a tyrosine sulfated protein (pI = 4.5-5.5). This protein was not present in either media or cell lysate of human fibroblasts lacking ASA protein. These results suggest that tyrosine sulfation facilitates secretion of ASA and that this may have pathophysiological consequences.

Keywords: Tyrosine sulfation, cellular regulation, protein secretion, arylsulfatase A