Sulfoconjugation: role in neurotransmitter and secretory protein activity

A variety of endogenous biogically active substances can undergo sulfate conjugation in vivo. The physiologically consequence of this reaction is clearly dependent on the particular molecule which is esterified. Sulfation of small molecules sych as the catecholamine neurotransmitter generally leads to inactivation of the biologically active species and probably facilitates the excretion of these endogenous amines in the urine. Sulfoconjugation of the tyrosyl residue of small secretory peptides and other larger proteins appears to be a ubiquitous process and may constitute a significant post-translational modification, in vivo. In this article, Jerome Roth presents some of the recent findings demonstrating the importance and potential role of sulfoconjugation in regulating the function of endogenous biologically active agents in vivo.