{'fraction_non_alphanumeric': 0.03598484848484849, 'fraction_numerical': 0.013257575757575758, 'mean_word_length': 6.2465753424657535, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Caveolin‐1 negatively regulates a metalloprotease‐dependent EGF receptor transactivation by angiotensin II

The EGF receptor (EGFR) transactivation pathway via an ADAM17‐dependent ligand shedding is the key signaling step by which angiotensin II (AngII) induces vascular smooth muscle cell (VSMC) remodeling. However, the molecular mechanism of the ADAM17 regulation remains largely unclear. We hypothesized that caveolin‐1 (Cav1), the major structural protein of a membrane microdomain, caveolae, is involved in the regulation.