Tyrosine sulfation of arylsulfatase A and its peptide

Research output: Contribution to journalArticlepeer-review

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 languageEnglish (US)
Pages (from-to)357-361
Number of pages5
JournalProtein and Peptide Letters
Volume13
Issue number4
DOIs
StatePublished - Apr 2006

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biochemistry

Keywords

  • Arylsulfatase A
  • Cellular regulation
  • Protein secretion
  • Tyrosine sulfation

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