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We began analyzing https://www.ahajournals.org/doi/10.1161/ATVBAHA.116.307648, but it redirected us to https://www.ahajournals.org/doi/10.1161/ATVBAHA.116.307648. The analysis below is for the second page.

Title[redir]:
NLRP3 (Nucleotide Oligomerization Domain–Like Receptor Family, Pyrin Domain Containing 3)–Caspase-1 Inflammasome Degrades Contractile Proteins | Arteriosclerosis, Thrombosis, and Vascular Biology
Description:
Objective—Increasing evidence suggests that contractile dysfunction in smooth muscle cells (SMCs) plays a critical role in aortic biomechanical dysfunction and aortic aneurysm and dissection (AAD) development. However, the mechanisms underlying SMC contractile dysfunction in sporadic AAD are poorly understood. In this study, we examined the role of the NLRP3 (nucleotide oligomerization domain–like receptor family, pyrin domain containing 3)–caspase-1 inflammasome, a key inflammatory cascade, in SMC contractile dysfunction in AAD. Approach and Results—We observed significant SMC contractile protein degradation in aortas from patients with sporadic thoracic AAD. The contractile protein degradation was associated with activation of the NLRP3–caspase-1 inflammasome cascade. In SMCs, caspase-1 bound and directly cleaved and degraded contractile proteins, leading to contractile dysfunction. Furthermore, Nlrp3 or caspase-1 deficiency in mice significantly reduced angiotensin II–induced contractile protein degradation, biomechanical dysfunction, and AAD formation in both thoracic and abdominal aortas. Finally, blocking this cascade with the inflammasome inhibitor, glyburide (an antidiabetic medication), reduced angiotensin II–induced AAD formation. Conclusions—Inflammasome-caspase-1–mediated degradation of SMC contractile proteins may contribute to aortic biomechanical dysfunction and AAD development. This cascade may be a therapeutic target in AAD formation. In addition, glyburide may have protective effects against AAD development.

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aortic, mice, contractile, inflammasome, aad, thoracic, surgery, department, houston, sal, challenged, nlrp, medicine, dysfunction, caspase, texas, division, jsc, yhs, figure, crossref, aneurysm, nlrpcaspase, degradation, protein, cardiovascular, pubmed, cascade, google, scholar, vascular, center, dissection, smc, institute, doi, formation, university, reduced, development, sporadic, heart, patients, disease, descending, glyburide, tissues, smcs, myosin, chain,

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increasing evidence suggests aha/asa scientific statements caspase-1 inhibitor z-vad-fmk conclusions— inflammasome-caspase-1–mediated degradation footnote nonstandard abbreviations discussion recent evidence alpha-smooth muscle actin smooth muscle alpha-actin american heart association modulating nicotine-induced ferroptosis smc-specific contractile proteins nlrp3–caspase-1 inflammasome complex nlrp3–caspase-1 inflammasome complex sequential sirna-mediated knockdown nlrp3–caspase-1 inflammasome cascade smooth muscle cells early event preserved full-length tropomyosin hm-d-24-00076 crossref benjamin main content advertisement red ™ aha caspase recruitment domain]–caspase-1 nlrp3–caspase-1 inflammasome components vascular biology vol challenging c57bl/6 wild-type regulating pkm2 polymerization international users arteriosclerosis heart failure stroke submit references nested case-control analysis supplements download pdf methods materials acknowledgments highlights • obesity promotes inflammation angiotensin ii hfd contractile protein degradation article recently published inflammasome genes card8 inflammasome cascade contributes triggers cell injury provide evidence suggesting editorial support nationwide case-control study quantification studies show cell contractile function high-fat diet pa mitochondrial oxidative stress smc contractile proteins

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What causes aortic contractile protein degradation and dysfunction in sporadic AAD?

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