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Vascular protein disulfide isomerase A1 mediates endothelial dysfunction induced by angiotensin II in mice.

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Title: Vascular protein disulfide isomerase A1 mediates endothelial dysfunction induced by angiotensin II in mice.
Authors: Kij, Agnieszka (AUTHOR), Bar, Anna (AUTHOR), Czyzynska‐Cichon, Izabela (AUTHOR), Przyborowski, Kamil (AUTHOR), Proniewski, Bartosz (AUTHOR), Mateuszuk, Lukasz (AUTHOR), Kurylowicz, Zuzanna (AUTHOR), Jasztal, Agnieszka (AUTHOR), Buczek, Elzbieta (AUTHOR), Kurpinska, Anna (AUTHOR), Suraj‐Prazmowska, Joanna (AUTHOR), Marczyk, Brygida (AUTHOR), Matyjaszczyk‐Gwarda, Karolina (AUTHOR), Daiber, Andreas (AUTHOR), Oelze, Matthias (AUTHOR), Walczak, Maria (AUTHOR), Chlopicki, Stefan (AUTHOR)
Source: Acta Physiologica. Apr2024, Vol. 240 Issue 4, p1-18. 18p.
Subjects: Protein disulfide isomerase, Angiotensin II, Endothelium diseases, Pulse wave analysis, Electron paramagnetic resonance
Abstract: Aim: Protein disulfide isomerases (PDIs) are involved in platelet aggregation and intravascular thrombosis, but their role in regulating endothelial function is unclear. Here, we characterized the involvement of vascular PDIA1 in angiotensin II (Ang II)‐induced endothelial dysfunction in mice. Methods: Endothelial dysfunction was induced in C57BL/6JCmd male mice via Ang II subcutaneous infusion, and PDIA1 was inhibited with bepristat. Endothelial function was assessed in vivo with magnetic resonance imaging and ex vivo with a myography, while arterial stiffness was measured as pulse wave velocity. Nitric oxide (NO) bioavailability was measured in the aorta (spin‐trapping electron paramagnetic resonance) and plasma (NO2− and NO3− levels). Oxidative stress, eNOS uncoupling (DHE‐based aorta staining), and thrombin activity (thrombin–antithrombin complex; calibrated automated thrombography) were evaluated. Results: The inhibition of PDIA1 by bepristat in Ang II‐treated mice prevented the impairment of NO‐dependent vasodilation in the aorta as evidenced by the response to acetylcholine in vivo, increased systemic NO bioavailability and the aortic NO production, and decreased vascular stiffness. Bepristat's effect on NO‐dependent function was recapitulated ex vivo in Ang II‐induced endothelial dysfunction in isolated aorta. Furthermore, bepristat diminished the Ang II‐induced eNOS uncoupling and overproduction of ROS without affecting thrombin activity. Conclusion: In Ang II‐treated mice, the inhibition of PDIA1 normalized the NO‐ROS balance, prevented endothelial eNOS uncoupling, and, thereby, improved vascular function. These results indicate the importance of vascular PDIA1 in regulating endothelial function, but further studies are needed to elucidate the details of the mechanisms involved. [ABSTRACT FROM AUTHOR]
Copyright of Acta Physiologica is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Psychology and Behavioral Sciences Collection
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  Data: Vascular protein disulfide isomerase A1 mediates endothelial dysfunction induced by angiotensin II in mice.
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  Data: <searchLink fieldCode="AR" term="%22Kij%2C+Agnieszka%22">Kij, Agnieszka</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Bar%2C+Anna%22">Bar, Anna</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Czyzynska‐Cichon%2C+Izabela%22">Czyzynska‐Cichon, Izabela</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Przyborowski%2C+Kamil%22">Przyborowski, Kamil</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Proniewski%2C+Bartosz%22">Proniewski, Bartosz</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Mateuszuk%2C+Lukasz%22">Mateuszuk, Lukasz</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Kurylowicz%2C+Zuzanna%22">Kurylowicz, Zuzanna</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Jasztal%2C+Agnieszka%22">Jasztal, Agnieszka</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Buczek%2C+Elzbieta%22">Buczek, Elzbieta</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Kurpinska%2C+Anna%22">Kurpinska, Anna</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Suraj‐Prazmowska%2C+Joanna%22">Suraj‐Prazmowska, Joanna</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Marczyk%2C+Brygida%22">Marczyk, Brygida</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Matyjaszczyk‐Gwarda%2C+Karolina%22">Matyjaszczyk‐Gwarda, Karolina</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Daiber%2C+Andreas%22">Daiber, Andreas</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Oelze%2C+Matthias%22">Oelze, Matthias</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Walczak%2C+Maria%22">Walczak, Maria</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Chlopicki%2C+Stefan%22">Chlopicki, Stefan</searchLink> (AUTHOR)
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  Data: <searchLink fieldCode="JN" term="%22Acta+Physiologica%22">Acta Physiologica</searchLink>. Apr2024, Vol. 240 Issue 4, p1-18. 18p.
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  Data: <searchLink fieldCode="DE" term="%22Protein+disulfide+isomerase%22">Protein disulfide isomerase</searchLink><br /><searchLink fieldCode="DE" term="%22Angiotensin+II%22">Angiotensin II</searchLink><br /><searchLink fieldCode="DE" term="%22Endothelium+diseases%22">Endothelium diseases</searchLink><br /><searchLink fieldCode="DE" term="%22Pulse+wave+analysis%22">Pulse wave analysis</searchLink><br /><searchLink fieldCode="DE" term="%22Electron+paramagnetic+resonance%22">Electron paramagnetic resonance</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: Aim: Protein disulfide isomerases (PDIs) are involved in platelet aggregation and intravascular thrombosis, but their role in regulating endothelial function is unclear. Here, we characterized the involvement of vascular PDIA1 in angiotensin II (Ang II)‐induced endothelial dysfunction in mice. Methods: Endothelial dysfunction was induced in C57BL/6JCmd male mice via Ang II subcutaneous infusion, and PDIA1 was inhibited with bepristat. Endothelial function was assessed in vivo with magnetic resonance imaging and ex vivo with a myography, while arterial stiffness was measured as pulse wave velocity. Nitric oxide (NO) bioavailability was measured in the aorta (spin‐trapping electron paramagnetic resonance) and plasma (NO2− and NO3− levels). Oxidative stress, eNOS uncoupling (DHE‐based aorta staining), and thrombin activity (thrombin–antithrombin complex; calibrated automated thrombography) were evaluated. Results: The inhibition of PDIA1 by bepristat in Ang II‐treated mice prevented the impairment of NO‐dependent vasodilation in the aorta as evidenced by the response to acetylcholine in vivo, increased systemic NO bioavailability and the aortic NO production, and decreased vascular stiffness. Bepristat's effect on NO‐dependent function was recapitulated ex vivo in Ang II‐induced endothelial dysfunction in isolated aorta. Furthermore, bepristat diminished the Ang II‐induced eNOS uncoupling and overproduction of ROS without affecting thrombin activity. Conclusion: In Ang II‐treated mice, the inhibition of PDIA1 normalized the NO‐ROS balance, prevented endothelial eNOS uncoupling, and, thereby, improved vascular function. These results indicate the importance of vascular PDIA1 in regulating endothelial function, but further studies are needed to elucidate the details of the mechanisms involved. [ABSTRACT FROM AUTHOR]
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  Data: <i>Copyright of Acta Physiologica is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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        Value: 10.1111/apha.14116
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        Text: English
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      – SubjectFull: Angiotensin II
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      – SubjectFull: Endothelium diseases
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