N-linked glycosylation is a post-translational modification that enables the cell to regulate protein function without recourse to the genome. The Proteinase-Activated Receptors (PAR) each possesses a number of N-linked glycosylation sites on their extracellular domains. However, little is currently known about the relative glycosylation status of each family member and about the influence that glycosylation may confer on receptor function. Interestingly, each PAR possesses an N-linked glycosylation site in close proximity to the cleavage/activation site on the receptor N-terminus. Recent studies focusing on PAR(2) have pointed out a role for glycosylation on the N-terminus in influencing receptor activation. Consequently, shifts in tissue and/or cell glycosylation patterns in health and disease could play an important role in regulating PAR function. (C) 2003 Wiley-Liss, Inc.