Angiotensin-Converting Enzyme, or ACE, is a critical zinc-containing metalloprotease enzyme that functions as a central component of the Renin-Angiotensin-Aldosterone System (RAAS), a major hormonal cascade regulating systemic blood pressure. This enzyme is primarily found anchored to the endothelial cells lining the blood vessels, particularly within the pulmonary circulation. Clinically, its function is essential for maintaining vascular tone, fluid balance, and overall cardiovascular homeostasis throughout the body.
Origin
The acronym ACE stands for Angiotensin-Converting Enzyme, a name that precisely describes its key biochemical function of converting a precursor peptide into its active form. The enzyme’s role was identified and characterized as part of the broader scientific elucidation of the RAAS pathway, which began with pioneering endocrinology and physiology studies focused on the mechanisms underlying essential hypertension in the mid-20th century.
Mechanism
ACE catalyzes the hydrolysis of the inactive decapeptide angiotensin I by cleaving two terminal amino acids, resulting in the formation of the highly potent octapeptide vasoconstrictor, angiotensin II. Angiotensin II then acts by binding to the AT1 receptor, triggering powerful vasoconstriction, stimulating aldosterone release from the adrenal cortex, and increasing sympathetic nervous system activity. These collective actions efficiently raise systemic blood pressure and influence sodium and water retention, illustrating a core, rapid hormonal feedback loop.
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