A common African polymorphism abolishes tyrosine sulfation of human anionic trypsinogen (PRSS2).

ABSTRACT: Human pancreatic trypsinogens undergo post-translational sulfation on Tyr(154), catalysed by the Golgi-resident enzyme tyrosylprotein sulfotransferase 2. Sequence alignments suggest that the sulfation of Tyr(154) is facilitated by a unique sequence context which is characteristically found in primate trypsinogens. In the search for genetic variants that might alter this sulfation motif, we identified a single nucleotide polymorphism (c.457G>C) in the PRSS2 (serine protease 2, human anionic trypsinogen) gene, which changed Asp(153) to a histidine residue (p.D153H). The p.D153H variant is common in subjects of African origin, with a minor allele frequency of 9.2%, whereas it is absent in subjects of European descent. We demonstrate that Asp(153) is the main determinant of tyrosine sulfation

SUBMITTER: Ronai Z 

PROVIDER: S-EPMC2700036 | biostudies-literature | 2009 Feb

REPOSITORIES: biostudies-literature