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.
Original language | English (US) |
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Pages (from-to) | 357-361 |
Number of pages | 5 |
Journal | Protein and Peptide Letters |
Volume | 13 |
Issue number | 4 |
DOIs | |
State | Published - Apr 2006 |
All Science Journal Classification (ASJC) codes
- Structural Biology
- Biochemistry
Keywords
- Arylsulfatase A
- Cellular regulation
- Protein secretion
- Tyrosine sulfation