The DOI matches its Crossref record; 15 of the 15 references it cites were found in a registry or an index.
Characterization of Protease-activated Receptor-2 Immunoreactivity in Normal Human Tissues
Abstract
PAR-2 is a second member of a novel family of G-protein-coupled receptors characterized by a proteolytic cleavage of the amino terminus, thus exposing a tethered peptide ligand that autoactivates the receptor. The physiological and/or pathological role(s) of PAR-2 are still unknown. This study provides tissue-specific cellular localization of PAR-2 in normal human tissues by immunohistochemical techniques. A polyclonal antibody, PAR-2C, was raised against a peptide corresponding to the amino terminal sequence SLIGKVDGTSHVTGKGV of human PAR-2. Significant PAR-2 immunoreactivity was detected in smooth muscle of vascular and nonvascular origin and stromal cells from a variety of tissues. PAR-2 was also present in endothelial and epithelial cells independent of tissue type. Strong immunolabeling was observed throughout the gastrointestinal tract, indicating a possible function for PAR-2 in this system. In the CNS, PAR-2 was localized to many astrocytes and neurons, suggesting involvement of PAR-2 in neuronal function. A role for PAR-2 in the skin was further supported by its immunolocalization in the epidermis. PAR-2C antibody exemplifies an important tool to address the physiological role(s) of PAR-2.
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Cites
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Interactions of Mast Cell Tryptase with Thrombin Receptors and PAR-2
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Self-citationMolecular cloning, expression and potential functions of the human proteinase-activated receptor-2
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Cited by
D'Andrea, M. R., Nagele, R. G., Wang, H., Peterson, P. A., & Lee, D. H. S. (2001) · Histopathology · doi:10.1046/j.1365-2559.2001.01082.x · Cited by 390
Self-citationPotential Mechanisms Underlying Centralized Pain and Emerging Therapeutic Interventions
Eller-Smith, O. C., Nicol, A. L., & Christianson, J. A. (2018) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2018.00035 · Cited by 227
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Dulon, S., Leduc, D., Cottrell, G. S., D'Alayer, J., Hansen, K. K., Bunnett, N. W., Hollenberg, M. D., Pidard, D., & Chignard, M. (2005) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2004-0274oc · Cited by 139
Protease-activated receptors in health and disease
Peach, C. J., Edgington-Mitchell, L. E., Bunnett, N. W., & Schmidt, B. L. (2023) · Physiological Reviews · doi:10.1152/physrev.00044.2021 · Cited by 116
Metadata
- Authors
- R. D'Andrea, M., Derian, C. K., Leturcq, D., Baker, S. M., Brunmark, A., Ling, P., Darrow, A. L., Santulli, R. J., Brass, L. F., & Andrade–Gordon, P.
- Venue
- Journal of Histochemistry & Cytochemistry
- Publisher
- SAGE Publications
- Published
- 1998-02
- Volume
- 46
- Issue
- 2
- Pages
- 157-164
- ISSN
- 0022-1554 (ISSN-L)
- 1551-5044
- OpenAlex
- W2031843235
- Cited by
- 320
- References
- 15
- FWCI
- 12.39
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Characterization of Protease-activated Receptor-2 Immunoreactivity in Normal Human Tissues. https://app.cochat.ai/papers/10.1177/002215549804600204
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- R. D'Andrea, M., Derian, C. K., Leturcq, D., Baker, S. M., Brunmark, A., Ling, P., Darrow, A. L., Santulli, R. J., Brass, L. F., & Andrade–Gordon, P. (1998). Characterization of Protease-activated Receptor-2 Immunoreactivity in Normal Human Tissues. Journal of Histochemistry & Cytochemistry. https://doi.org/10.1177/002215549804600204
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
