Sandbox Reserved 1652: Difference between revisions
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'''Phosphorylation''' of the TRPV1 receptor leads to its sensitization | '''Phosphorylation''' of the TRPV1 receptor leads to its sensitization | ||
(the process regulates TRPV1 its functionality). Phosphorylations are either caused by '''PKC''' ([https://en.wikipedia.org/wiki/Inositol_trisphosphate IP3 signalling]), by '''PKA''' ([https://fr.wikipedia.org/wiki/Adénylate_cyclase AMPc signalling]), or by '''CamKII'' | (the process regulates TRPV1 its functionality). Phosphorylations are either caused by '''PKC''' ([https://en.wikipedia.org/wiki/Inositol_trisphosphate IP3 signalling]), by '''PKA''' ([https://fr.wikipedia.org/wiki/Adénylate_cyclase AMPc signalling]), or by '''CamKII'' activation by inflammatory mediators. <ref>K. W. Ho, N. J. Ward, et D. J. Calkins, « TRPV1: a stress response protein in the central nervous system », Am. J. Neurodegener. Dis., vol. 1, no 1, p. 1‑14, avr. 2012.</ref><ref name="Integrating TRPV1 Receptor Function with Capsaicin Psychophysics"> Depending on the target residu, the impact on the receptor will be different as various activation pathways are impacted. Phosphorylation improves the efficiency of the receptor and because it regulates the function, it is a target to treat [https://en.wikipedia.org/wiki/Hyperalgesia]. <ref name="Phosphorylation of TRPV1 S801 Contributes to Modality-Specific Hyperalgesia in Mice"> <ref>John Joseph, L. Qu, S. Wang, M. Kim, D. Bennett, J. Ro, M. J. Caterina and MK. Chung, Journal of Neuroscience 11 December 2019, 39 (50) 9954-9966. https://www.jneurosci.org/content/39/50/9954 (Consulté le: déc. 23, 2021). [En ligne].</ref>. PKA phosphorylates <scene name='86/868185/S502_t370/1'>T370 and S502</scene>, PKC and CaMKII phosphorylate <scene name='86/868185/Ser502_thr704/1'>S502 and T704</scene>. | ||
The phosphorylation of TRPV1 lead to an '''over-expression ''' of TRPV1 at the membrane surface.<ref>K. W. Ho, N. J. Ward, et D. J. Calkins, « TRPV1: a stress response protein in the central nervous system », Am. J. Neurodegener. Dis., vol. 1, no 1, p. 1‑14, avr. 2012.</ref> Moreover, phosphorylated TRPV1 would have a reduced channel opening threshold.<ref>G. Bhave et al., « Protein kinase C phosphorylation sensitizes but does not activate the capsaicin receptor transient receptor potential vanilloid 1 (TRPV1) », Proc. Natl. Acad. Sci., vol. 100, no 21, p. 12480‑12485, oct. 2003, doi: 10.1073/pnas.2032100100.</ref>. As a result phosphorylated TRPV1 are more responsive to agonist and the resulting pain sensation is higher. | The phosphorylation of TRPV1 lead to an '''over-expression ''' of TRPV1 at the membrane surface.<ref>K. W. Ho, N. J. Ward, et D. J. Calkins, « TRPV1: a stress response protein in the central nervous system », Am. J. Neurodegener. Dis., vol. 1, no 1, p. 1‑14, avr. 2012.</ref> Moreover, phosphorylated TRPV1 would have a reduced channel opening threshold.<ref>G. Bhave et al., « Protein kinase C phosphorylation sensitizes but does not activate the capsaicin receptor transient receptor potential vanilloid 1 (TRPV1) », Proc. Natl. Acad. Sci., vol. 100, no 21, p. 12480‑12485, oct. 2003, doi: 10.1073/pnas.2032100100.</ref>. As a result phosphorylated TRPV1 are more responsive to agonist and the resulting pain sensation is higher. | ||