Sulfation of tyrosine residues does not influence secretion of alpha 2-antiplasmin or C4.
Sulfation of tyrosine residues is a biosynthetic modification of many secretory proteins. The function of this modification is not known, but it has been proposed that tyrosine sulfate residues may act as sorting signals to direct proteins along the secretory pathway. We tested this hypothesis by examining the effect of sulfation inhibitors on the kinetics of secretion of proteins by HepG2 cells. The inhibitors induced no change in the rate of secretion of alpha 2-antiplasmin and C4 (fourth component of complement), both of which contain tyrosine sulfate residues. Sulfation of tyrosine residues does not contribute to secretion of these proteins.
D002460:Cell Line; D002704:Chlorates / Q000494:pharmacology; D003181:Complement C4 / Q000378:metabolism*; D003470:Culture Media; D006139:Guaiacol / Q000494:pharmacology; D007118:Immunoassay; D013431:Sulfates / Q000378:metabolism*; D014443:Tyrosine / Q000378:metabolism*; D000979:alpha-2-Antiplasmin / Q000378:metabolism*
D002704:Chlorates; D003181:Complement C4; D003470:Culture Media; D013431:Sulfates; D000979:alpha-2-Antiplasmin; D014443:Tyrosine; D006139:Guaiacol; C032706:sodium chlorate