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• W2051238174 abstract "Background— Collectrin is an orphan member of the renin-angiotensin system and is a homolog of angiotensin-converting enzyme 2, sharing ≈50% sequence identity. Unlike angiotensin-converting enzyme 2, collectrin lacks any catalytic domain. Collectrin has been shown to function as a chaperone of amino acid transporters. In rodents, the renal expression of collectrin is increased after subtotal nephrectomy and during high-salt feeding, raising the question of whether collectrin has any direct role in blood pressure regulation. Methods and Results— Using a susceptible genetic background, we demonstrate that deletion of collectrin results in hypertension, exaggerated salt sensitivity, and impaired pressure natriuresis. Collectrin knockout mice display impaired endothelium-dependent vasorelaxation that is associated with vascular remodeling, endothelial nitric oxide synthase uncoupling, decreased nitric oxide production, and increased superoxide generation. Treatment with Tempol, a superoxide scavenger, attenuates the augmented sodium sensitivity in collectrin knockout mice. We report for the first time that collectrin is expressed in endothelial cells. Furthermore, collectrin directly regulates l -arginine uptake and plasma membrane levels of CAT1 and y + LAT1 amino acid transporters in endothelial cells. Treatment with l -arginine modestly lowers blood pressure of collectrin knockout mice. Conclusions— Collectrin is a consequential link between the transport of l -arginine and endothelial nitric oxide synthase uncoupling in hypertension." @default.
• W2051238174 created "2016-06-24" @default.
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• W2051238174 date "2013-10-15" @default.
• W2051238174 modified "2023-10-18" @default.
• W2051238174 title "Loss of Collectrin, an Angiotensin-Converting Enzyme 2 Homolog, Uncouples Endothelial Nitric Oxide Synthase and Causes Hypertension and Vascular Dysfunction" @default.
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• W2051238174 doi "https://doi.org/10.1161/circulationaha.113.003301" @default.
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