Publications by authors named "Sayed Modinur Rahaman"

Methods enabling rapid and on-site detection of pathogenic bacteria are a prerequisite for public health assurance, medical diagnostics, ensuring food safety and security, and research. Many current bacteria detection technologies are inconvenient and time-consuming, making them unsuitable for field detection. New technology based on the CRISPR/Cas system has the potential to fill the existing gaps in detection.

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Background: The World Health Organization (WHO) estimated that the number of cancer-related deaths was 9.6 million in 2018 and 2.09 million deaths occurred by lung cancer.

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The role of angiotensin II in regulating Na+/K(+)-ATPase activity has been investigated in bovine pulmonary artery smooth muscle cells (BPASMCs). Our study reveals that angiotensin II inhibits the Na+/K+ATPase activity via glutathionylation of the pump with the involvement of an increase in NADPH oxidase-derived O2*-. Additionally, angiotensin II treatment to the cells increases the inhibitory potency of the 15.

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Article Synopsis
  • - A new low molecular weight protein (15.6 kDa) that inhibits Na(+)/K(+)-ATPase was discovered in the cytosol of bovine pulmonary artery smooth muscle cells.
  • - This inhibitor shows different binding strengths to the two isozymes of the enzyme—α₂β₁ is more affected than α₁β₁.
  • - It binds reversibly to the E1 site of Na(+)/K(+)-ATPase, preventing the formation of a phosphorylated intermediate and altering the enzyme's structure.
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Treatment of bovine pulmonary smooth muscle cells with U46619 inhibited the Na(+)/K(+) ATPase activity in two parallel pathways: one of which is mediated via glutathionylation of the pump and the other by augmenting the inhibitory activity of the 70kDa inhibitor protein of Na(+)/K(+) ATPase. Although phospholemman deglutathionylates the pump leading to its activation, the inhibitor is responsible for irreversible inhibition of Na(+)/K(+) ATPase in an isoform specific manner during treatment of the cells with U46619.

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