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(Hypertension. 2005;46:1100.)
© 2005 American Heart Association, Inc.

Editorial Commentaries

Vasoconstriction Caused by the ATP Synthase Subunit–Coupling Factor 6

A New Function for a Historical Enzyme

Stephanie W. Watts

From the Department of Pharmacology and Toxicology, Michigan State University, East Lansing.

Correspondence to Stephanie W. Watts, B445 Life Sciences Building, Department of Pharmacology and Toxicology, Michigan State University, East Lansing, 48824-1317. E-mail wattss@msu.edu

An extract of the first 250 words of the full text is provided, because this article has no abstract.

	Introduction

 
Enhancement of arterial vasoconstriction and depression of endothelial cell–dependent relaxation have been reported by many investigators as characteristics of vascular dysfunction in hypertension.¹ These dysfunctions support the increase in total peripheral resistance observed in experimental and human forms of hypertension. Because arterial smooth-muscle cell hyperreactivity and reduced vasoactive function of the endothelial cell are observed in response to multiple stimuli (eg, serotonin, norepinephrine, KCl in smooth muscle; acetylcholine, bradykinin, A23187 in endothelial cell) and are thus not necessarily agonist-specific, researchers have investigated the idea that more general mechanisms of signal transduction are altered and support global changes in vascular function. These include alterations in composition and function of elements as diverse as potassium channels, calcium channels, sodium-potassium ATPase, G-proteins, membrane lipid composition, etc. In this issue of Hypertension, the study by Osanai et al² reveals a new function for a protein subunit of an enzyme that is ubiquitously expressed in all tissues, the ATP synthase.

	Historic Function of ATP Synthase

 
Figure 1 depicts our classic understanding of the ATP synthase. This ancient enzyme is present in the inner membrane of mitochondria and is responsible for generation of ATP. Synthesis of ATP is generated by the movement of hydrogen ions from the intermembrane space into the matrix of the mitochondria through the transmembrane H⁺ carrier (F_o) with subsequent movement of the F_i portion of the enzyme that coordinates the interaction of the subunits and ATP synthesis.³ This powerhouse of an enzyme can synthesize more than 100 molecules of ATP per second; this enzyme can . . . [Full Text of this Article]

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Intracellular Signaling for Vasoconstrictor Coupling Factor 6: Novel Function of ß-Subunit of ATP Synthase as Receptor

Tomohiro Osanai, Koji Magota, Makoto Tanaka, Michiko Shimada, Reiichi Murakami, Satoko Sasaki, Hirofumi Tomita, Naotaka Maeda, and Ken Okumura
Hypertension 2005 46: 1140-1146. [Abstract] [Full Text] [PDF]