Publications by authors named "Saja Kamalamma"

Objectives: Sesamol, a polyphenolic compound isolated from roasted sesame seeds exhibits significant anti-inflammatory effect, but the molecular mechanism is poorly understood. Peritoneal macrophages play a pivotal role in the control of infections and inflammatory pathologies and are also found in injured tissues along with resident macrophages. The present study aimed to examine the anti-inflammatory effect of sesamol and the molecular mechanisms involved, particularly the role of sesamol in modulating SIRT1- and SIRT1-mediated deacetylation of NF-κB p65 using in vivo activated peritoneal macrophages.

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Background And Aims: ADAMTS-4 is a protease enzyme involved in vascular remodeling and atherosclerosis. It was found to be upregulated in macrophages seen in atherosclerotic lesions. This study aimed to investigate the expression and regulation of ADAMTS-4 in oxidized LDL-induced human monocytes/macrophages system.

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Hypothermic conditions enhance the incidence of cardiovascular diseases due to increased blood pressure. Cold-induced adaptive thermogenesis increased mitochondrial biogenesis and function in skeletal muscles and adipocytes. Here, we studied the effect of intermittent cold exposure on the regulators of cardiac mitochondrial biogenesis, function, and its regulation by SIRT-3.

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Sirt-1 is one of the most extensively studied mammalian Sirtuins that deacetylates histones and several non-histone proteins critical to cellular homeostasis. As a key sensor of cellular metabolism, it is regulated at multiple levels including transcriptional and post translational levels. As an allosteric enzyme, its activity is also modulated by ligands and certain endogenous proteins.

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Mitochondrial ATP synthase catalyzes the coupling of oxidative phosphorylation. Under pathological conditions, ATP synthase hydrolyzes ATP to replenish protons from the matrix into the intermembrane space, sustaining mitochondrial membrane potential. ATPase inhibitory factor 1 (IF1) is a nuclear-encoded, ATP synthase-interacting protein that selectively inhibits the hydrolysis activity of ATP synthase, which may render the protective role of IF1 in ischemic hearts.

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