Correction to: protease-activated receptors (PARs): mechanisms of action and potential therapeutic modulators in PAR-driven inflammatory diseases

Abstract

Activates Microglia by Inducing the Expressions of Matrix Metalloproteinases and the Subsequent Activation of Protease-Activated Receptor-1. J Immunol. 2010, ji_0903480. For further clarification, this sentence should read as follows: "Similarly, MMP-2 cleaves human PAR1 and enhances platelet activation [91], and MMP-3, MMP-8, and MMP-9 were shown to cleave and activate PAR1 peptide at thrombin cleavage site R41 [92]."

Macrophage TLR4 and PAR2 Signaling: Role in Regulating Vascular Inflammatory Injury and Repair

“…For example, PAR1 is cleaved by proteases such as thrombin, factor Xa, plasmin, MMP1 and MMP13 (121). Originally, PAR2 was thought to be cleaved only by trypsin, tryptase, factor VIIa, factor Xa and elastase (28,29). However, recent studies show that thrombin can also cleave PAR2, albeit at higher concentrations (30,31).…”

“…Protease activated receptors (PARs), PAR1, PAR2, and PAR3 encoded by the genes F2R, F2RL1, F2RL2, and F2RL3, respectively are also expressed on the MΦ cell-surface. As the name indicates, PARs are activated by several different proteases, including those involved in the coagulation pathway ( 26 , 28 , 120 ). While each of these receptors can be cleaved by their specific proteases, several common proteases can also cleave various PARs because of their sequence homology.…”

“…Inflammation is also known to activate the coagulation cascade, which in turn affects inflammatory processes by generating a further suite of proteases such as trypsin, thrombin, elastases, FVIIa and FXa (26,27). Protease activated receptors (PAR) such as PAR2, are known to ligate trypsin, tryptase, factor VIIa, factor Xa, and elastase (28,29). Interestingly, recent studies suggest that thrombin also ligates PAR2 (30,31).…”

Deciphering the Role of the Coagulation Cascade and Autophagy in Cancer-Related Thrombosis and Metastasis

“…These receptors belong to the G protein-coupled receptor (GPCR) family and become activated upon proteolytic cleavage of their N-terminal domain by extracellular proteases. PAR signaling has been implicated in several inflammatory diseases, including cancer (10,11). Mammalian genomes contain four PARs that are ubiquitous within the body.…”

“…Upon activation, PARs are rapidly uncoupled from heterotrimeric G proteins through internalization to endosomes and then sorted to lysosomes and degraded. However, recent studies indicate that activated internalized PARs signal from endosomes through the recruitment of b-arrestins and potentially other pathways [reviewed in (10,22)]. Interestingly, crosstalk between PAR signaling and autophagy has been described in different cell types (23)(24)(25), the physiological and pathophysiological role of this crosstalk still is an open field for investigation and discussion.…”