ArticleThe Biochemical journal2002
Glycosylation of human proteinase-activated receptor-2 (hPAR2): role in cell surface expression and signalling.
Article in The Biochemical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 116 citations in OpenAlex.
- Proteinase-activated receptor-2 mediates itch: a novel pathway for pruritus in human skin.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2003Trial
- Mechanisms of Location Bias in G Protein-Coupled Receptors.Handbook of experimental pharmacology · 2026Review
- Functional Divergence for N-Linked Glycosylation Sites in Equine Lutropin/Choriogonadotropin Receptors.Current issues in molecular biology · 2025Article
- The N-Linked Glycosylation Site N201 in eel Lutropin/Choriogonadotropin Receptor Is Uniquely Indispensable for cAMP Responsiveness and Receptor Surface Loss, but Not pERK1/2 Activity.Current issues in molecular biology · 2025Article
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- The activation fragment of PAR2 is elevated in serum from patients with rheumatoid arthritis and reduced in response to anti-IL6R treatment.Scientific reports · 2021Article
- PAR-2-activated secretion by airway gland serous cells: role for CFTR and inhibition byAmerican journal of physiology. Lung cellular and molecular physiology · 2021Article
- Post-Translational Modifications of G Protein-Coupled Receptors Control Cellular Signaling Dynamics in Space and Time.Pharmacological reviews · 2021Review
- Role of N-Linked Glycosylation in PKR2 Trafficking and Signaling.Frontiers in neuroscience · 2021Article
- Impact of naturally forming human α/β-tryptase heterotetramers in the pathogenesis of hereditary α-tryptasemia.The Journal of experimental medicine · 2019Article
- HIV-induced neuroinflammation: impact of PAR1 and PAR2 processing by Furin.Cell death and differentiation · 2019Article
- The Role of PAR2 in TGF-β1-Induced ERK Activation and Cell Motility.International journal of molecular sciences · 2017Article
- Discrepancies between human DNA, mRNA and protein reference sequences and their relation to single nucleotide variants in the human population.Database : the journal of biological databases and curation · 2016Article
- Analysis of the potential of cancer cell lines to release tissue factor-containing microvesicles: correlation with tissue factor and PAR2 expression.Thrombosis journal · 2016Article
- N-linked glycosylation of protease-activated receptor-1 at extracellular loop 2 regulates G-protein signaling bias.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Mouse mast cell protease-6 and MHC are involved in the development of experimental asthma.Journal of immunology (Baltimore, Md. : 1950) · 2014Article
- N-Glycan-dependent and -independent quality control of human δ opioid receptor N-terminal variants.The Journal of biological chemistry · 2014Article
- Article
- Evaluation of antibodies directed against human protease-activated receptor-2.Naunyn-Schmiedeberg's archives of pharmacology · 2012Article
- PR3 and elastase alter PAR1 signaling and trigger vWF release via a calcium-independent mechanism from glomerular endothelial cells.PloS one · 2012Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have analysed the role of N-linked glycosylation in regulating human proteinase-activated receptor-2 (hPAR(2)) expression and function. Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5. Western blot analysis of wt-hPAR(2) showed mature wt-hPAR(2) to have a molecular mass of 55-100 kDa, and 33-48 kDa following N -glycosidase F deglycosylation. FACS analysis and immunocytochemistry of the wt-hPAR(2) and PAR(2) mutant cell lines revealed that removal of both glycosylation sequons decreases (50% of wt-hPAR(2)) cell surface expression. Western blot analysis indicated that both N-linked sites are glycosylated. In functional studies, hPAR(2)N30A displayed a selective and significant increase in sensitivity towards tryptase. Interestingly, hPAR(2)N222A displayed a loss in sensitivity towards all PAR(2) agonists tested. However, further analysis revealed receptor sensitivity to alanine mutations in this domain, as the more conservative substitution hPAR(2)N222Q displayed no change in response to PAR(2) agonists. hPAR(2)N30A,N222Q displayed increased sensitivity towards tryptase, but a loss in sensitivity towards trypsin and the synthetic peptide SLIGRL-NH(2), although this loss in sensitivity towards trypsin and SLIGRL-NH(2) was secondary to changes in cell-surface expression. Finally, expression of sialic-acid-deficient wt-hPAR(2) in the CHO Lec2 glycosylation-deficient mutant cell line, showed a 40 kDa loss in molecular mass, in addition to a marked and selective increase in sensitivity towards tryptase. We conclude that hPAR(2) N-linked glycosylation and sialylation regulates receptor expression and/or signalling.
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