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G alpha q Is the Specific Mediator of PAR-1 Transactivation of Kinase Receptors in Vascular Smooth Muscle Cells
Journal article   Open access   Peer reviewed

G alpha q Is the Specific Mediator of PAR-1 Transactivation of Kinase Receptors in Vascular Smooth Muscle Cells

Danielle Kamato, Mai Gabr, Hirushi Kumarapperuma, Zheng J. Chia, Wenhua Zheng, Suowen Xu, Narin Osman and Peter J. Little
International Journal of Molecular Sciences, Vol.23(22), pp.1-13
2022
PMCID: PMC9692893
PMID: 36430902
pdf
ijms-23-144251.40 MBDownloadView
Published Version Open Access CC BY V4.0
url
https://doi.org/10.3390/ijms232214425View
Published Version

Abstract

epidermal growth factor receptor transforming growth factor type I receptor transactivation dependent thrombin GPCR proteoglycans
Aims: G protein-coupled receptor (GPCR) transactivation of kinase receptors greatly expands the actions attributable to GPCRs. Thrombin, via its cognate GPCR, protease-activated receptor (PAR)-1, transactivates tyrosine and serine/threonine kinase receptors, specifically the epidermal growth factor receptor and transforming growth factor-beta receptor, respectively. PAR-1 transactivation-dependent signalling leads to the modification of lipid-binding proteoglycans involved in the retention of lipids and the development of atherosclerosis. The mechanisms of GPCR transactivation of kinase receptors are distinct. We aimed to investigate the role of proximal G proteins in transactivation-dependent signalling. Main Methods: Using pharmacological and molecular approaches, we studied the role of the G alpha subunits, G alpha q and G alpha 11, in the context of PAR-1 transactivation-dependent signalling leading to proteoglycan modifications. Key Findings: Pan G alpha q subunit inhibitor UBO-QIC/FR900359 inhibited PAR-1 transactivation of kinase receptors and proteoglycans modification. The G alpha q/11 inhibitor YM254890 did not affect PAR-1 transactivation pathways. Molecular approaches revealed that of the two highly homogenous G alpha q members, G alpha q and G alpha 11, only the G alpha q was involved in regulating PAR-1 mediated proteoglycan modification. Although G alpha q and G alpha 11 share approximately 90% homology at the protein level, we show that the two isoforms exhibit different functional roles. Significance: Our findings may be extrapolated to other GPCRs involved in vascular pathology and highlight the need for novel pharmacological tools to assess the role of G proteins in GPCR signalling to expand the preeminent position of GPCRs in human therapeutics.

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Chemistry, Multidisciplinary

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