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Science 24 March 2006:
Vol. 311. no. 5768, p. 1677
DOI: 10.1126/science.311.5768.1677c
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The pathogenesis of hypertension--a risk factor for heart disease, kidney disease, and stroke--is complex and poorly understood. Zacchigna et al. find that mice lacking elastin microfibril interface-located protein 1 (Emilin1), a secreted extracellular matrix protein expressed in the cardiovascular system, had high blood pressure in conjunction with decreased blood vessel diameter and increased peripheral resistance. Emilin1 contains a cysteine-rich domain, as do other proteins involved in the regulation of growth factor signaling, leading the authors to investigate the relationship between Emilin1 and transforming growth factor-beta (TGF-beta), which plays a critical role in vascular development and pathophysiology. Emilin1 blocked TGF-beta signaling upstream of receptor activation and did not interfere with ligand/receptor binding or signaling in response to mature TGF-beta1. Rather, Emilin1 bound to proTGF-beta1, preventing its proteolytic processing and the production of biologically active TGF-beta1. TGF-beta signaling was enhanced in the aortic wall of the mice lacking Emilin1, and inactivation of one TGF-beta1 allele in Emilin1 knockout mice restored normal blood vessel diameter and blood pressure. Thus, the authors conclude that Emilin1 acts to regulate blood pressure by modulating TGF-beta processing and thus the availability of the biologically active form. -- EMA

Cell 124, 929 (2006).




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