Key result
Arg2 modification in Ang II eliminates ACE2 competition and alters cellular signaling compared to wild-type.
Why the study?
The mechanistic role of arginine at position 2 of angiotensin II in ACE2 recognition and the functional consequences of its oxidant-mediated modification were unclear.
Comparison
Wild-type Ang II versus Arg2-modified Ang II peptides
Design
Experimental study with mass spectrometry and gene expression analyses
Authors
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Arg2-modified Ang II variants evade ACE2 and elicit unique signals; hypothesis-generating for redox Ang II roles in cardiovascular disease.
The Arg2 residue of Angiotensin II is critical for ACE2 recognition, and its oxidant-mediated conversion generates peptides with distinct biological functions.
Suzuki et al. (2026) studied this question. Modification of Arg2 in Angiotensin II (Arg2Glu and Arg2Pro) vs. Wild-type Angiotensin II was evaluated on ACE2 activity and cellular signaling responses. Modification of the Arg2 residue in Angiotensin II to Glu or Pro eliminated its ability to compete for ACE2 and elicited distinct cellular signaling responses compared to wild-type Ang II.
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