We are analyzing https://link.springer.com/article/10.1007/s00395-016-0596-8.

Title:
Calpain 1 cleaves and inactivates prostacyclin synthase in mesenteric arteries from diabetic mice | Basic Research in Cardiology
Description:
Diabetes is associated with a number of co-morbidities including an increased risk of developing cardiovascular diseases. The activation of Ca2+-activated proteases of the calpain family has been implicated in platelet activation associated with diabetes and this study aimed to determine the role of calpain activation in the development of endothelial dysfunction. Diabetes induction in mice attenuated acetylcholine-induced relaxation of mesenteric artery rings, an effect prevented in mice receiving a calpain inhibitor. A nitric oxide-independent but diclofenac-sensitive component of the relaxation–response was altered and correlated with a loss of prostacyclin (PGI2) generation and reduced vascular levels of PGI2 synthase. Calpain inhibition was also able to restore PGI2 synthase levels and PGI2 generation in arteries from diabetic animals. The effects of diabetes were reproduced in vitro by a combination of high glucose and palmitate, which elicited calpain activation, PGI2 synthase cleavage and inactivation as well as endothelial dysfunction in mesenteric arteries from wild-type mice. PGI2 cleavage was not observed in arteries from calpain 1−/− mice or mice overexpressing the endogenous calpain inhibitor calpastatin. Finally, proteomic analyses revealed that calpain 1 cleaved the C-terminal domain of PGI2 synthase close to the catalytic site of the enzyme. These data demonstrate that diabetes leads to the activation of calpain 1 in mesenteric arteries and can initiate endothelial dysfunction by cleaving and inactivating the PGI2 synthase. Given that calpain inhibition prevented diabetes-induced endothelial dysfunction in mesenteric arteries, calpains represent an interesting therapeutic target for the prevention of cardiovascular complication of diabetes.
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Keywords {🔍}

pubmed, article, google, scholar, cas, calpain, diabetes, synthase, prostacyclin, endothelial, arteries, diabetic, mice, activation, central, mesenteric, dysfunction, vascular, randriamboavonjy, fleming, platelet, nitric, pgi, role, pharmacol, oxide, research, access, res, physiol, privacy, cookies, content, main, elgheznawy, mechanism, tyrosine, data, publish, search, basic, december, voahanginirina, kyselova, ingrid, inhibitor, inhibition, cleavage, moncada, prostaglandin,

Topics {✒️}

mice attenuated acetylcholine-induced relaxation acetylcholine-induced endothelium-dependent contractions month download article/chapter streptozotocin-induced diabetic rats platelet-derived calpain cleaves cyclooxygenase-1-mediated prostacyclin synthesis established streptozotocin-diabetic rats article basic research shear-stress-induced activation thromboxane a2 full article pdf nitric oxide synthase related subjects endothelium-dependent contractions nitric oxide-independent privacy choices/manage cookies ca2+-activated proteases initiate endothelial dysfunction potentiate endothelial dysfunction �-calpain activity arterial walls generate endothelial cell calpain rat resistance arteries calpain inhibition stabilizes ca2+-independent activation calpain cleavage prediction article randriamboavonjy diabetic complications vascular endothelial cells tandem mass spectrometry sven zukunft relaxation–response wild-type mice aged 3xtgad mice kim-kaneyama jr pgi2 synthase cleavage inhibits platelet aggregation calpain inhibitor european economic area diclofenac-sensitive component proteomic analyses revealed c-terminal domain interesting therapeutic target kca channel opener haymann jp ve-cadherin disorganization wan sulaiman wa zaharil mat sa ghulam rasool ah expert technical assistance

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         description:Diabetes is associated with a number of co-morbidities including an increased risk of developing cardiovascular diseases. The activation of Ca2+-activated proteases of the calpain family has been implicated in platelet activation associated with diabetes and this study aimed to determine the role of calpain activation in the development of endothelial dysfunction. Diabetes induction in mice attenuated acetylcholine-induced relaxation of mesenteric artery rings, an effect prevented in mice receiving a calpain inhibitor. A nitric oxide-independent but diclofenac-sensitive component of the relaxation–response was altered and correlated with a loss of prostacyclin (PGI2) generation and reduced vascular levels of PGI2 synthase. Calpain inhibition was also able to restore PGI2 synthase levels and PGI2 generation in arteries from diabetic animals. The effects of diabetes were reproduced in vitro by a combination of high glucose and palmitate, which elicited calpain activation, PGI2 synthase cleavage and inactivation as well as endothelial dysfunction in mesenteric arteries from wild-type mice. PGI2 cleavage was not observed in arteries from calpain 1−/− mice or mice overexpressing the endogenous calpain inhibitor calpastatin. Finally, proteomic analyses revealed that calpain 1 cleaved the C-terminal domain of PGI2 synthase close to the catalytic site of the enzyme. These data demonstrate that diabetes leads to the activation of calpain 1 in mesenteric arteries and can initiate endothelial dysfunction by cleaving and inactivating the PGI2 synthase. Given that calpain inhibition prevented diabetes-induced endothelial dysfunction in mesenteric arteries, calpains represent an interesting therapeutic target for the prevention of cardiovascular complication of diabetes.
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      description:Diabetes is associated with a number of co-morbidities including an increased risk of developing cardiovascular diseases. The activation of Ca2+-activated proteases of the calpain family has been implicated in platelet activation associated with diabetes and this study aimed to determine the role of calpain activation in the development of endothelial dysfunction. Diabetes induction in mice attenuated acetylcholine-induced relaxation of mesenteric artery rings, an effect prevented in mice receiving a calpain inhibitor. A nitric oxide-independent but diclofenac-sensitive component of the relaxation–response was altered and correlated with a loss of prostacyclin (PGI2) generation and reduced vascular levels of PGI2 synthase. Calpain inhibition was also able to restore PGI2 synthase levels and PGI2 generation in arteries from diabetic animals. The effects of diabetes were reproduced in vitro by a combination of high glucose and palmitate, which elicited calpain activation, PGI2 synthase cleavage and inactivation as well as endothelial dysfunction in mesenteric arteries from wild-type mice. PGI2 cleavage was not observed in arteries from calpain 1−/− mice or mice overexpressing the endogenous calpain inhibitor calpastatin. Finally, proteomic analyses revealed that calpain 1 cleaved the C-terminal domain of PGI2 synthase close to the catalytic site of the enzyme. These data demonstrate that diabetes leads to the activation of calpain 1 in mesenteric arteries and can initiate endothelial dysfunction by cleaving and inactivating the PGI2 synthase. Given that calpain inhibition prevented diabetes-induced endothelial dysfunction in mesenteric arteries, calpains represent an interesting therapeutic target for the prevention of cardiovascular complication of diabetes.
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