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keywords cathelicidin-related antimicrobial peptide cathepsin pi3k/akt/m-tor pathway cathelicidin-related antimicrobial peptide ctsl cathelicidin-related antimicrobial peptide month download article/chapter cathelicidins prime platelets regulating endothelial-mesenchymal transition cardiac ischemia-reperfusion injury myocardial ischemia/reperfusion injury regulating igfr1/pi3k/akt cdp/cux transcription factor perk regulating eif2α/chop perk/atf4/chac1 axis antimicrobial peptide cathelicidin article basic research antimicrobial peptide ll-37 cathelicidin peptide ll-37 full article pdf antimicrobial peptide combined myocardial ischemia/reperfusion pdia4 confers resistance related subjects privacy choices/manage cookies attenuates cardiac dysfunction signal peptide localizes cowland jb tlr9/ampkα ferroptosis-related genes extracellular milieu contribute induces cellular senescence osteoarthritis cartilage s1063–4584 infarcted cardiac tissues improved cardiac function regulates oxidative stress shuo miao attenuate cardiac dysfunction infarcted myocardial tissues natural science foundation renal cell carcinoma holds exclusive rights levels caused pdia4 basic res cardiol cramp inhibited ferroptosis myocardial infarction contributes european economic area original contribution published cathelin/pro-bactenecin positive feedback loop muratore-schroeder tl reduces infarct size

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         headline:Antimicrobial peptide CRAMP/LL-37 mediates ferroptosis resistance in cardiomyocytes by inhibiting cathepsin L
         description:Ferroptosis is an important cause of cardiomyocyte loss and cardiac dysfunction. Cathelicidin-related antimicrobial peptide (CRAMP) is an endogenous polypeptide that regulates oxidative stress in the body and is involved in ferroptosis. However, its specific role and mechanism in ferroptosis are unclear. To analyze the role of CRAMP in ferroptosis, we first analyzed its expression in infarcted myocardial tissues, and verified its role in ferroptosis in vitro through overexpression and knock-down techniques. The activity and expression of cathepsin L (CTSL) and its effect on ferroptosis were analyzed to verify whether CTSL participated in ferroptosis as a downstream of CRAMP. Protein disulfide isomerase family A member 4 (PDIA4) was screened as an interacting protein of CTSL by using the database, and the role of PDIA4 in ferroptosis was analyzed by gene knockdown and overexpression. Finally, the regulatory mechanism of CRAMP in ferroptosis was verified in vivo by mouse myocardial infarction model. CRAMP levels were reduced in both infarcted cardiac tissues and cardiomyocytes exposed to ferroptosis inducers. The overexpression of CRAMP or pretreatment of LL-37 alleviated cardiomyocyte ferroptosis, whereas CRAMP knockdown exacerbated cell death. Under ferroptotic stress, the expression of CTSL was elevated. CRAMP inhibited ferroptosis by antagonizing the CTSL activity. Abnormal increase in CTSL activity and levels caused PDIA4 to decrease. Overexpression of PDIA4 inhibited ferroptosis induced by CTSL, while knocking down PDIA4 counteracted the protection of CRAMP. In vivo, both CRAMP overexpression and administration of CRAMP peptide significantly ameliorated myocardial injury and improved cardiac function. CRAMP increases PDIA4 levels by inhibiting the activity of CTSL and antagonizes ferroptosis in cardiomyocytes. Targeting CRAMP offers innovative therapeutic strategies and insights for the prevention and management of myocardial injury.
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            Cathelicidin-related antimicrobial peptide
            Cathepsin L
            Protein disulfide isomerase family A member 4
            Ferroptosis
            Myocardial injury
            Cardiology
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      headline:Antimicrobial peptide CRAMP/LL-37 mediates ferroptosis resistance in cardiomyocytes by inhibiting cathepsin L
      description:Ferroptosis is an important cause of cardiomyocyte loss and cardiac dysfunction. Cathelicidin-related antimicrobial peptide (CRAMP) is an endogenous polypeptide that regulates oxidative stress in the body and is involved in ferroptosis. However, its specific role and mechanism in ferroptosis are unclear. To analyze the role of CRAMP in ferroptosis, we first analyzed its expression in infarcted myocardial tissues, and verified its role in ferroptosis in vitro through overexpression and knock-down techniques. The activity and expression of cathepsin L (CTSL) and its effect on ferroptosis were analyzed to verify whether CTSL participated in ferroptosis as a downstream of CRAMP. Protein disulfide isomerase family A member 4 (PDIA4) was screened as an interacting protein of CTSL by using the database, and the role of PDIA4 in ferroptosis was analyzed by gene knockdown and overexpression. Finally, the regulatory mechanism of CRAMP in ferroptosis was verified in vivo by mouse myocardial infarction model. CRAMP levels were reduced in both infarcted cardiac tissues and cardiomyocytes exposed to ferroptosis inducers. The overexpression of CRAMP or pretreatment of LL-37 alleviated cardiomyocyte ferroptosis, whereas CRAMP knockdown exacerbated cell death. Under ferroptotic stress, the expression of CTSL was elevated. CRAMP inhibited ferroptosis by antagonizing the CTSL activity. Abnormal increase in CTSL activity and levels caused PDIA4 to decrease. Overexpression of PDIA4 inhibited ferroptosis induced by CTSL, while knocking down PDIA4 counteracted the protection of CRAMP. In vivo, both CRAMP overexpression and administration of CRAMP peptide significantly ameliorated myocardial injury and improved cardiac function. CRAMP increases PDIA4 levels by inhibiting the activity of CTSL and antagonizes ferroptosis in cardiomyocytes. Targeting CRAMP offers innovative therapeutic strategies and insights for the prevention and management of myocardial injury.
      datePublished:2025-06-15T00:00:00Z
      dateModified:2025-06-15T00:00:00Z
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         Cathelicidin-related antimicrobial peptide
         Cathepsin L
         Protein disulfide isomerase family A member 4
         Ferroptosis
         Myocardial injury
         Cardiology
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