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Mitigation of Obesity: A Phytotherapeutic Approach
Published in Amit Baran Sharangi, K. V. Peter, Medicinal Plants, 2023
A.B. Sharangi, Suddhasuchi Das
Altered lipid metabolic processes together with lipogenesis and lipolysis facilitate the development of obesity (Pagliassotti et al., 1997). Synthetic moieties and surgical procedures are the universal therapy of obesity, but have detrimental side effects and likelihood of severe recurrence (Karri et al., 2019). Lipogenesis stores free fatty acids in the form of triglyceride (Mandrup and Lane, 1997); whereas in lipolysis, the stored triglyceride is metabolized to free fatty acids and glycerol (Ducharme and Bichel, 2008). Obesity is accompanied by an abnormally high concentration of lipids in blood, i.e., hyperlipidemia (Akiyama et al., 1996). The adipose tissue secretes several biologically active adipokines and thereby regulates metabolism and homeostasis (Yudkin et al., 1999). Three key transcription factors like peroxisome proliferator-activated receptor (PPAR), CCAAT/enhancer-binding protein (C/EBP) and sterol regulatory element-binding protein (SREBP) regulate the expression of these lipid-metabolizing enzymes during adipose tissue development (Freytag and Utter, 1983). 5’ AMP-activated protein kinase (AMPK) plays a major role in lipid and glucose metabolism by inactivating acetyl-CoA carboxylase (ACC) and Through up-regulating the expression of carnitine palmitoyl transferase-1 (CPT-1), PPAR, and uncoupling protein, stimulation of fatty acid oxidation is done (Kim et al., 2007).
Diabetes and Inflammation
Published in Awanish Kumar, Ashwini Kumar, Diabetes, 2020
TNF receptor 2 (TNFR2) is occasionally shed from the membrane on binding of TNF-α, giving soluble TNF receptor 2 (sTNFR2). It has been seen that in diabetic subjects, this shedding increases and concentration of sTNFR2 is negatively correlated with insulin sensitivity [10]. In insulin-resistant individuals, the mRNA level of TNF-α in skeletal muscle cells was found to be higher than in control subjects. TNF-α administration is also shown to downregulate the expression of peroxisome proliferator activated receptor-γ (PPAR-γ) and CAAT/enhancer binding protein-α (C/EBP-α) which are transcription factors related to positive insulin sensitivity. This is also one of the important mechanisms of TNF-α induced insulin resistance. This is also supported by the fact that PPAR-γ agonists, thiazolidinedione (TZDs), suppress TNF-α expression owing to the improvement of the insulin sensitivity in diabetic individuals. TNF-α administration was also found to induce the protein tyrosine phosphatase-1B (PTP-1B) activity resulting in dephosphorylation of IRS-1 protein, thus inhibiting the downstream insulin signalling [11].
Regulation of α1-Acid glycoprotein genes and Relationship to Other Type 1 Acute Phase Plasma Proteins
Published in Andrzej Mackiewicz, Irving Kushner, Heinz Baumann, Acute Phase Proteins, 2020
Heinz Baumann, Karen R. Prowse, Kwang-Ai Won, Sanja Marinkovic-Pajovic
The functional consequence of the overlapping HA (AGP/EBP or C/EBP binding site) and GRE (Figure 1) remains an unsolved issue. Two possible explanations are (1) during dexamethasone stimulation, the glucocorticoid receptor and AGP/EBP form one complex or (2) the binding of the two factors is mutually exclusive.73 In either case, the activation of the AGP gene is seen as a function of the glucocorticoid receptor, which is in agreement with the characteristic dose-dependent stimulation of the AGP gene by dexamethasone.9,12 If the glucocorticoid receptor is critical, the question arises as to why C/EBP transactivates Hep G2 cells even in the absence of steroid treatment. Alternative explanations come to mind: (1) at high concentrations of C/EBP, all three binding sites (HA, HX, and HB; Figure 1) are occupied89 and that triggers transcription or (2) an inhibitor for C/EBP, whose activity is reduced during dexamethasone treatment, is out-titrated by excess C/EBP. Since all the resources are in place, answers to these questions will be forthcoming.
Attenuation of obesity related inflammation in RAW 264.7 macrophages and 3T3-L1 adipocytes by varanadi kashayam and identification of potential bioactive molecules by UHPLC-Q-Orbitrap HRMS
Published in Archives of Physiology and Biochemistry, 2023
J. U. Chinchu, Mohind C. Mohan, B. Prakash Kumar
Obesity is a major health problem characterised by excessive body fat accumulation through an imbalance between energy intake and consumption and is responsible for developing type 2 diabetes, coronary heart disease and certain cancers (Guyenet and Schwartz 2012). Obesity is mainly associated with an increase in white adipose tissue mass through activation of adipogenesis and increased deposition of cytoplasmic triglycerides (Frigolet et al. 2008). Adipogenesis is a highly regulated process in which undifferentiated fibroblasts (preadipocytes) become mature adipocytes and is regulated by an elaborate network of transcription factors including CCAAT/enhancer-binding protein (C/EBP) and peroxisome proliferator-activated receptor-γ (PPAR-γ) (Yu et al. 2014). C/EBP-α and PPAR-γ work cooperatively in inducing the adipocyte differentiation process and promote the expression of fatty acid synthase (FAS) to trigger the synthesis and accumulation of triglyceride (TG) in mature adipocyte (Farmer 2006). Therefore, adipogenesis inhibition by downregulating adipogenic transcriptional factor expressions is critical for achieving an anti-obesity effect.
High-fat diet exacerbates cognitive and metabolic abnormalities in neuronal BACE1 knock-in mice – partial prevention by Fenretinide
Published in Nutritional Neuroscience, 2022
Kaja Plucińska, Nimesh Mody, Ruta Dekeryte, Kirsty Shearer, George D. Mcilroy, Mirela Delibegovic, Bettina Platt
Because the diabetic phenotype in PLB4 mice was associated with increased expression of ER stress markers, such as eukaryotic translation-initiation factor 2α (eIF2α) and C/EBP homologous protein (CHOP), we next investigated whether HFD feeding in WT caused similar pathology. Quantification of phospho/total eIF2α ratio (Figure 4(F)), revealed that HFD+/− Fen elevated the total levels of active eIF2α three to five-fold in WT (p < 0.001) and PLB4 forebrains (p < 0.001), respectively. We were unable to replicate the increase in p-eIF2α expression in this cohort of PLB4 mice fed chow diet (1.3-fold increase compared to WT; F < 1, p > 0.05), but the cerebral levels of CHOP protein, a down-stream target of eIF2α was elevated 2.2-fold in PLB4 mice on normal chow diet (genotype effect: F(1,18) = 20.5, p < 0.001; Figure 4(G)) as observed before. Surprisingly, HFD down-regulated neuronal CHOP levels both in WT and PLB4 mice independently of Fenretinide treatment (effect of diet: F(2,18) = 26.5, p < 0.001; effect of drug: p < 0.001). Overall, these data indicate differential effects of HFD on central p-eIF2α and CHOP protein levels in mice.
From a basic to a functional approach for developing a blood stage vaccine against Plasmodium vivax
Published in Expert Review of Vaccines, 2020
Manuel Alfonso Patarroyo, Gabriela Arévalo-Pinzón, Darwin A. Moreno-Pérez
In-depth knowledge of which fragments are essential in parasite–cell interaction must first be obtained before beginning studies in animal models. Functional restriction analysis has been shown to be useful for identifying essential regions for reticulocyte binding which the parasite protects by using highly antigenic but polymorphic regions as smoke screens. This must be followed by roughly identifying protein regions having binding activity through protein–cell interaction trials, as has been done with PvEBP, PvGAMA, PvRBSA, PvAMA1, PvRON2, and PvRON4. CD71+ reticulocyte enriched samples (UCB) and/or other sources (JK-1 cells or ejRBC) must be used for functionally characterizing the molecules mediating parasite–cell interaction and determining the significance of such protein interactions.