Tyrosine sulfation of arylsulfatase A and its peptide.
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.
Kasinathan
Chinnaswamy
C
Oral Biology, University of Medicine and Dentistry of New Jersey (UMDNJ), New Jersey Dental School, Newark, NJ 07103-2400, USA. kasinach@umdnj.edu
Jean
Smith
S
Manowitz
Paul
P
D002553:Cerebroside-Sulfatase / Q000378:metabolism*; D003470:Culture Media / Q000737:chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D005347:Fibroblasts / Q000378:metabolism; D006801:Humans; D007525:Isoelectric Focusing; D008099:Liver / Q000201:enzymology; D010446:Peptide Fragments / Q000378:metabolism; D015238:Sulfotransferases / Q000378:metabolism; D013462:Sulfur Radioisotopes; D014443:Tyrosine / Q000378:metabolism*
D003470:Culture Media; D010446:Peptide Fragments; D013462:Sulfur Radioisotopes; D014443:Tyrosine; D015238:Sulfotransferases; C039079:protein-tyrosine sulfotransferase; D002553:Cerebroside-Sulfatase