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In vivo, the total amount of SREBP-1c in liver and adipose tissue is reduced by fasting, which suppresses insulin and increases glucagon levels, and is elevated by refeeding (32, 33). The levels of mRNA for SREBP-1c target genes parallel the changes in SREBP-1c expression. Similarly, SREBP-1c mRNA levels fall when rats are treated with streptozotocin, which abolishes insulin secretion, and rise after insulin injection (29). Overexpression of nSREBP-1c in livers of transgenic mice prevents the reduction in lipogenic mRNAs that normally follows a fall in plasma insulin levels (32). Conversely, in livers of Scap knockout mice that lack all nSREBPs in the liver (14) or knockout mice lacking either nSREBP-1c (16) or both SREBP-1 isoforms (34), there is a marked decrease in the insulin-induced stimulation of lipogenic gene expression that normally occurs after fasting/refeeding. It should be noted that insulin and glucagon also exert a posttranslational control of fatty acid synthesis though changes in the phosphorylation and activation of acetyl-CoA carboxylase. The posttranslational regulation of fatty acid synthesis persists in transgenic mice that overexpress nSREBP-1c (10). In these mice, the rates of fatty acid synthesis, as measured by [3H]water incorporation, decline after fasting even though the levels of the lipogenic mRNAs remain high (our unpublished observations).
Metformin, a biguanide drug used to treat insulin-resistant diabetes, reduces hepatic nSREBP-1 levels and dramatically lowers the lipid accumulation in livers of insulin-resistant ob/ob mice (40). Metformin stimulates AMP-activated protein kinase (AMPK), an enzyme that inhibits lipid synthesis through phosphorylation and inactivation of key lipogenic enzymes (41). In rat hepatocytes, metformin-induced activation of AMPK also leads to decreased mRNA expression of SREBP-1c and its lipogenic target genes (41), but the basis of this effect is not understood.
Human asparaginase 3 (hASNase3), which belongs to the N-terminal nucleophile hydrolase superfamily, is synthesized as a single polypeptide that is devoid of asparaginase activity. Intramolecular autoproteolytic processing releases the amino group of Thr168, a moiety required for catalyzing asparagine hydrolysis. Recombinant hASNase3 purifies as the uncleaved, asparaginase-inactive form and undergoes self-cleavage to the active form at a very slow rate. Here, we show that the free amino acid glycine selectively acts to accelerate hASNase3 cleavage both in vitro and in human cells. Other small amino acids such as alanine, serine, or the substrate asparagine are not capable of promoting autoproteolysis. Crystal structures of hASNase3 in complex with glycine in the uncleaved and cleaved enzyme states reveal the mechanism of glycine-accelerated posttranslational processing and explain why no other amino acid can substitute for glycine.
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Peroxisome proliferator-activated receptors are expressed in many tissues, including adipocytes, hepatocytes, muscles and endothelial cells; however, the affinity depends on the isoform of PPAR, and different distribution and expression profiles, which ultimately lead to different clinical outcomes. Because they play an important role in lipid and glucose homeostasis, they are called lipid and insulin sensors. Their actions are limited to specific tissue types and thus, reveal a characteristic influence on target cells. PPARα mainly influences fatty acid metabolism and its activation lowers lipid levels, while PPARγ is mostly involved in the regulation of the adipogenesis, energy balance, and lipid biosynthesis. PPARβ/δ participates in fatty acid oxidation, mostly in skeletal and cardiac muscles, but it also regulates blood glucose and cholesterol levels. Many natural and synthetic ligands influence the expression of these receptors. Synthetic ligands are widely used in the treatment of dyslipidemia (e.g. fibrates - PPARα activators) or in diabetes mellitus (e.g. thiazolidinediones - PPARγ agonists). New generation drugs - PPARα/γ dual agonists - reveal hypolipemic, hypotensive, antiatherogenic, anti-inflammatory and anticoagulant action while the overexpression of PPARβ/δ prevents the development of obesity and reduces lipid accumulation in cardiac cells, even during a high-fat diet. Precise data on the expression and function of natural PPAR agonists on glucose and lipid metabolism are still missing, mostly because the same ligand influences several receptors and a number of reports have provided conflicting results. To date, we know that PPARs have the capability to accommodate and bind a variety of natural and synthetic lipophilic acids, such as essential fatty acids, eicosanoids, phytanic acid and palmitoylethanolamide. A current understanding of the effects of PPARs, their molecular mechanisms and the role of these receptors in nutrition and therapeutic treatment are delineated in this paper.
The family of peroxisome proliferation-activated receptors comprises three isoforms: PPARα, PPARβ/δ and PPARγ [1]. These three isotypes differ from each other in terms of their tissue distributions, ligand specificities and physiological roles. Each of them either activates or suppresses different genes with only partial overlap in activity (Figure 3) [5]. All isoforms participate in lipid homeostasis and glucose regulation (energy balance), and, until recently, their actions were thought to be limited to specific tissue types (Figure 4) [5, 11]. PPARα is highly expressed in metabolically active tissues, such as liver, heart, skeletal muscle, intestinal mucosa and brown adipose tissue. This receptor is implicated in fatty acid metabolism and its activation lowers lipid levels [12-15].
The least known isoform is PPARβ/δ, which has not been so intensely studied as PPARα and PPARγ. PPARβ/δ is expressed ubiquitously in virtually all tissues; however, it is particularly abundant in the liver, intestine, kidney, abdominal adipose tissue, and skeletal muscle, all of which are involved in lipid metabolism. It participates in fatty acid oxidation, mainly in skeletal and cardiac muscles, regulates blood cholesterol concentrations and glucose levels [1, 13, 19, 20].
Many natural and synthetic agonists of PPARs are used in the treatment of glucose and lipid disorders. PPARs perform different activities, mainly via endogenous ligands produced in the metabolic pathways of fatty acids; and therefore, they are called lipid sensors. PPAR agonists have different properties and specificities for individual PPAR receptors, different absorption/distribution profiles, and distinctive gene expression profiles, which ultimately lead to different clinical outcomes [1, 5, 17, 22, 23].
The characteristic feature of the PPAR ligand binding cavity is its size, which is 3-4 times larger than that of the other nuclear receptors. Thus, PPARs have the capability to accommodate and bind a variety of natural and synthetic lipophilic acids, such as essential fatty acids (EFA) (Figure 5). These acids act as PPAR agonists that transcript the genes involved in glucose and lipid homeostasis [12, 22, 24]. They include docosahexaenoic acid and eicosapentaenoic acid used in the prevention and treatment of cardiovascular and metabolic diseases [25]. Not only EFA but also eicosanoids are natural ligands of PPARs - e.g. leukotriene B4 stimulates PPARα, and prostaglandin PGJ2 activates PPARγ [22]. However, both EFA and eicosanoids are required in relatively high concentrations (approximately 100 μM) for PPAR activation [24]. Also, synthetic ligands are widely used in clinical practice - for example, fibrates (PPARα ligands) are recommended in the dyslipidemic state (hypertriglyceridemia) and thiazolidinediones (PPARγ agonists) are used in the treatment of diabetes mellitus [26-29].
As mentioned above, PPARα is expressed mainly in tissues with a high capacity for fatty acid oxidation, e.g. the liver, heart, and skeletal muscle. It also plays a role in glucose homeostasis and insulin resistance development (Figure 6) [29]. Natural or pharmacological ligands (fatty acids and fibrates, respectively) primarily control the expression of genes involved in lipid metabolism. If the concentration of fatty acids increases, PPARα is activated and uptakes oxidized forms of these acids [30, 31]. Oxidation of fatty acids is mainly present in the liver and it prevents steatosis in the case of starvation/fasting. During the influx of fatty acids, transcription of PPARα-regulated genes is stimulated and the oxidation systems (microsomal omega-oxidation system, and mitochondrial and peroxisomal beta-oxidation) are activated (Figure 7) [21, 32]. This activation and increased PPARα sensing in the liver result in increased energy burning and reduced fat storage. Conversely, ineffective PPARα sensing or decreased fatty acid oxidation causes a reduction in energy burning that results in hepatic steatosis and steatohepatitis (especially during overnight or prolonged fasting) [32, 33]. The diminished effectiveness of oxidation systems is caused by genetic or toxic factors (including drug related ones), and metabolic disturbances. In animal models, inefficient PPARα sensing (characteristic for PPARα_/_ mice) enables the oxidation of the influxed fatty acids and leads to severe hepatic steatosis development. Administration of PPARα agonists prevents these processes and even reverses hepatic fibrosis (in animal models) [34]. Thus, PPARα functions as a lipid sensor and it controls energy combustion. It also plays also a prominent role in the pathogenesis of fatty liver disease (FLD) and ligands of this receptor might be effective in the reduction of hepatic staetosis by increasing energy utilization [32, 33]. 2b1af7f3a8
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