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Tropical Herbs and Spices as Functional Foods with Antidiabetic Activities
Published in Megh R. Goyal, Arijit Nath, Rasul Hafiz Ansar Suleria, Plant-Based Functional Foods and Phytochemicals, 2021
Arnia Sari Mukaromah, Fitria Susilowati
Acetone extract of nutmeg seed contains 28.16% of sabinene, 10.26% of βpinene, 9.72% of α-pinene, 4.30% of myristicin, 2.72% of isoeu-genol, 1.81% of p-cymene, 1.54% of carvacrol, 0.89% of eugenol and 0.82% of β-caryophyllene with antimicrobial and antioxidant activities [36]. Furthermore, AMP-activated protein kinase (AMPK) enzyme can be induced by nutmeg extract. Bioactive components of nutmeg extract include tetrahydrofuroguaiacin B, nectandrin B, and galbacin, which offer strong AMPK stimulation in mouse C2C12 skeletal my oblast. Therefore, nutmeg, and its active components have become popular as a T2DM therapeutic agent and to develop obesity medication [70].
Anti-Inflammatory Properties of Bioactive Compounds from Medicinal Plants
Published in Hafiz Ansar Rasul Suleria, Megh R. Goyal, Health Benefits of Secondary Phytocompounds from Plant and Marine Sources, 2021
Muhammad Imran, Abdur Rauf, Anees Ahmed Khalil, Saud Bawazeer, Seema Patel, Zafar Ali Shah
Colchicine reduced the transcoronary (coronary sinus-arterial) gradients for IL-1β, IL-18, and IL-6 [29]. AMPK (AMP-activated protein kinase: a metabolic bio-sensor) having anti-inflammatory characteristics. MSU (mono-sodium urate) inhibited phosphorylated AMPK-α in bone marrow-derived macrophage production (BMDMs). According to in vitro and in vivo studies, colchicine at low concentration (10 nM) confirmed AMPKα phosphorylation, polarization of macrophage M2, decreased caspase-1 activation, and release of IL-1β and CXCL1 due to MSU crystals in BMDMs [30].
Pharmacologic Ascorbate Influences Multiple Cellular Pathways Preferentially in Cancer Cells
Published in Qi Chen, Margreet C.M. Vissers, Cancer and Vitamin C, 2020
Qi Chen, Kishore Polireddy, Ping Chen, Ramesh Balusu, Tao Wang, Ruochen Dong
More mechanistic details have been revealed after ATP drop in ascorbate-treated cancer cells. AMP-activated protein kinase (AMPK) is the main sensor of cellular energy status and is activated when cellular AMP:ATP and ADP:ATP ratio is increased. AMPK activation restores the energy balance by inhibiting the anabolic process, which utilizes ATP (protein synthesis, fatty acid synthesis, sterol synthesis), while promoting catabolic processes that generate ATP (fatty acid oxidation, glucose uptake, glycolysis, autophagy) [38]. Ascorbate treatment resulted in activation of AMPK as evidenced by increased phosphorylation of the catalytic subunit of AMPK, AMPK-α. Activation of AMPK in cancer cells led to the inhibition of protein synthesis and cell growth by inhibiting mTOR (Figure 3.2), which is a central regulator of many biosynthetic pathways, especially protein translation [4]. Currently, it has been proposed, but efforts have not been made to discover the other signaling networks altered by AMPK when cells are treated with pharmacologic ascorbate.
Research progress of p38 as a new therapeutic target against morphine tolerance and the current status of therapy of morphine tolerance
Published in Journal of Drug Targeting, 2023
Metformin is an activator of adenosine 5′-monophosphate (AMP)-activated protein kinase (AMPK). The activation of AMPK is related to the inhibition of inflammatory nociceptive sensation, so metformin has potential anti-inflammatory effects [140]. Some studies have found that metformin can alleviate morphine tolerance [141]. Metformin was given before morphine injection. It was found that morphine-induced phosphorylation of p38MAPK, the release of proinflammatory cytokines and increased mRNA expression of Toll-like receptor 4 (TLR4), IL-1142]. Metformin is very effective in improving morphine tolerance, but there is a lack of more experimental data [143]. Further in vivo studies are needed to examine the adverse reactions of long-term use of metformin and its effects on opioid tolerance.
Research progress on related mechanisms of uric acid activating NLRP3 inflammasome in chronic kidney disease
Published in Renal Failure, 2022
Miao Wang, Xin Lin, Xiaoming Yang, Yanlang Yang
AMPK (AMP-activated protein kinase) is a key regulatory pathway of cell energy metabolism. Serum uric acid can regulate AMPK-mTOR (mammalian target of rapamycin)-mitochondrial reactive oxygen species, and the HIF-1α (hypoxia inducible factor-1α) pathway mediates the enhancement of the inflammatory process [59]. A decrease in uric acid levels will lead to the activation of AMPK to reduce inflammation [60]. Hyperuricemia will further cause inflammation, autophagy, and mitochondrial dysfunction through damage to sodium-potassium pump signal transduction and eventually lead to cell damage. The AMPK-mTOR pathway is abundant in renal tubular epithelial cells [52]. Hyperuricemia can stimulate the activation of AMPK in proximal tubular epithelial cells, in this study, they found that UA stimulates AMPK activity as a protective mechanism; however, soon AMPK activity decreases, leading to the impairment of Na+-K+-ATPase signaling, which further triggers inflammation autophagy, and mitochondrial dysfunction and leads to cell injury. Sustained treatment with an AMPK activator significantly alleviated UA-induced alterations [61].
Therapeutic perspectives on the metabolism of lymphocytes in patients with rheumatoid arthritis and systemic lupus erythematosus
Published in Expert Review of Clinical Immunology, 2021
The glycolytic system is the major metabolic process involved in generating energy in immune cells. When T cells are exposed to specific antigens, co-stimulatory molecules activate PI3K and upregulate the expression of glucose transporter 1 (GLUT1), resulting in enhanced glucose uptake [26]. AMP-activated protein kinase (AMPK) plays an important role in the regulation of glucose metabolism. Activation of AMPK enhances glycolysis by increasing the expression of GULT and promoting glucose utilization [27]. Furthermore, the glycolytic system is more enhanced in the Th1, Th17, Tfh, and CD8+ cells compared to that in the quiescent cells [28,29] and is particularly important for Th1 and Th17 cell differentiation [29,30]. Overexpression of the GLUT1 gene in mouse T cells leads to increased glucose uptake and production of IL-2 and IFN-γ [31]. Deletion of GLUT1 decreases the utilization of glucose in the CD4 + T cells and suppresses their differentiation into effector T cells [32]. Blockade of the glycolytic system promotes Treg cell differentiation [29]. High expression of Glut1 is associated with Th cell activation and production of IL-17, which is associated with the disease severity of active SLE [33,34]. HIF1α is activated by mTOR and is involved in the differentiation of Th1, Th17, and CD8+ cells via enhanced glucose metabolism. HIF1α activity is promoted to induce Th1 and Th17 cell differentiation via glucolysis downstream of TCR signaling [35,36].