Trypsin Cleavage of the Β1-Adrenergic Receptor
American journal of physiology Heart and circulatory physiology(2022)
Abstract
Current concepts regarding the molecular basis for β1AR responses derive from literature predicated on the assumption that β1ARs signal exclusively as full-length receptor proteins. However, we recently showed that β1ARs accumulate as both full-length and N-terminally truncated forms in cardiomyocytes and other cell types and that these distinct β1AR species evoke distinct signaling responses. This manuscript provides novel evidence that β1-adrenergic receptors can be cleaved by trypsin (and presumably other inflammatory serine proteases) and that cell surface β1AR cleavage constitutes a heretofore unrecognized mechanism to alter catecholamine-dependent signaling responses.
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Key words
&beta, ,1-adrenergic receptors,cardiomyocytes,trypsin
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