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The final destination of a journey is not, after all, the last item on the agenda, but rather some understanding, however simple or provisional, of what one has seen. In these modern times, with the plethora of blood-sugar-related diseases, we need tools like GI and GL to help us understand ways to control blood sugar. The self-testing, graphic approach to food testing developed in the balance of the newsletter is a less scientific but a more dynamic way to explore postprandial (post-meal) blood glucose levels (BGLs). GI measures the blood glucose impact of foods eaten in isolation, yet we rarely consume foods this way. GI readings vary with the individual—blood sugar and insulin reactions are more extreme for diabetics, for example (See Charts 2A and 2B). GIs are calculated in the science lab as the day’s first meal after a 12-hour fast and using a fixed serving that includes 50 grams of carbohydrate.  Most of our daily calories, however, are consumed in combination and throughout the day, when our blood sugar is affected by other foods that we have eaten earlier, as well as by our level of activity. Of the following numbered charts, the first three are based upon scientific research journal articles (Charts 1, 2A, 2B), while the last four (Charts 3-6) are constructed from my own self-testing of foods4 using a simple blood glucose monitor. Chart 1:  Blood Sugar Curves of White Bread Compared to Bread with Added Fiber, Sourdough, and Vinegar. Chart 3:  Instant Oatmeal, Whole Oats (Soaked and Not Soaked), and Whole Oats Combined with a Protein and Fat. To fully appreciate the impact of two back-to-back carbohydrate breakfasts please notice that the scale used for Chart 6 is twice that of Charts 3-5. Resetting the Table–to Control Blood Sugar (For a discussion of other strategies, see April 2011).
Ramekins filled with condiments like nuts and seeds (GI=0).  Nuts and seeds provide healthy fats, fiber, vitamins, minerals, and antioxidants, while they slow digestion and curb blood sugar. Sourdough bread or whole-grain bread with whole kernels; butter from grass-fed cows and organic nut and seed butters such as tahini and pumpkin seed butter. A pitcher of water and glasses for all—sometimes we mistake hunger for what is in fact thirst.  You might flavor the water with a little lemon juice or other flavoring. Because 12-hour fasting, pre-meal blood sugar reading can vary, all data points at time zero prior to the first morning meal were indexed to zero in order to illustrate the change from a neutral starting point. I use the label “traditional” carbohydrates, just as we call unrefined fats, “traditional” fats. Sidney Kimmel Comprehensive Cancer Research Center, Department of Oncology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21287, USA. An enzyme that initiates the first reaction of glycolysis by phosphorylating glucose to produce glucose-6-phosphate. A rate-limiting enzyme of glycolysis that requires ATP to convert fructose-6-phosphate into fructose-1,6-bisphosphate. An evolutionarily conserved process in which acidic double-membrane-bound vacuoles sequester intracellular contents (such as damaged organelles and macromolecules) and target them for degradation through fusion with secondary lysosomes.
A key intermediate of the tricarboxylic acid cycle that can be derived from glutaminolysis.
Insulin resistance syndrome, or metabolic syndrome, increases your risk of diabetes and early heart disease.
OBJECTIVES: High fructose feeding induces insulin resistance and hyperinsulinemia in rats. Englisch-Deutsch-A?bersetzung fA?r insulin resistant im Online-WA¶rterbuch (DeutschwA¶rterbuch). Science, Technology and Medicine open access publisher.Publish, read and share novel research.
B Zuber, M Chami, C Houssin, J Dubochet, G Griffiths, M Daffe, Direct visualization of the outer membrane of mycobacteria and corynebacteria in their native state. M Daffe, P Draper, The envelope layers of mycobacteria with reference to their pathogenicity. A Subramoniam, D Subrahmanyam, Light-induced changes in the phospholipid composition of Mycobacterium smegmatis ATCC 607. The second factor—the postwar shift from traditional to refined carbohydrates—is largely due to the growing role of the commercial food industry and processed, convenience foods.  Convenience foods must have a long shelf-life, so food companies rely upon refined flours and oils, which do not go rancid. Visual pictures of postprandial blood sugar behavior, while less scientific than GI measurements, are nevertheless powerful learning tools, providing a real flavor for how our body reacts when we eat different kinds of foods. This chart illustrates the second meal effect– that what we eat at one meal affects postprandial blood sugar behavior at the next.
What we do to our children when we give them a sugary cereal or a Pop-tart for breakfast extends beyond this first meal to affect their blood sugar, hunger, concentration, and desire to overeat throughout the rest of the day. One of the best herbs and spices to moderate blood sugar.  It can be sprinkled on hot cereals and desserts such as puddings, custards, and stewed fruits. A unidirectional transporter that facilitates the transport of glucose across the plasma membrane.
An enzyme that phosphorylates and inactivates pyruvate dehydrogenase, thereby inhibiting the catalysis of pyruvate to acetyl-CoA and preventing the initiation of the tricarboxylic acid cycle.
Well over 60,000 searches are done online each and every month for the term insulin resistance.
Read about insulin resistance is causes, symptoms, treatment (like diet), risk factors and more. Explains how insulin resistance develops and offers natural symptom relief for women who are insulin resistant. Certain food groups have been shown in reliable studies to decrease the risk of various conditions. M Plitzko, H Engelhardt, Disclosure of the mycobacterial outer membrane: cryo-electron tomography and vitreous sections reveal the lipid bilayer structure.
T Cole, R Brosch, J Parkhill, T Garnier, C Churcher, D Harris, et alDeciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. K Nandedkar, Comparative study of the lipid composition of particular pathogenic and nonpathogenic species of Mycobacterium. K Khuller, R Taneja, N Nath, Effect of fatty acid supplementation on the lipid composition of Mycobacterium smegmatis ATCC 607, grown at 27 degrees and 37 degrees C.
This, in turn, leads to the expression of multiple cytokines, chemokines and cell surface receptors, all of which promote T cell activation and proliferation3. CPT1A catalyses the transfer of the acyl group of long-chain fatty acids to acylcarnitine, which allows for its transport from the cytosol to the mitochondria.
Some pathways such as TAG and PE biosynthesis (shown as green arrows) do not occur in corynebacteria while some others (shown as blue arrows) are known to occur only in corynebacteria. Morita2[1] Australian Research Council Centre of Excellence in Structural and Functional Microbial Genomics, Department of Microbiology, Monash University, Australia[2] Department of Microbiology, University of Massachusetts, Amherst, USA1. This is why diabetes and obesity often go hand-in-hand (90% of diabetics are either overweight or obese). David Ludwig regarding high-glycemic foods and overeating, cited in the Recommended Reading section at the conclusion of this newsletter. Fortunately there is one condition that will always improve with dietary and lifestyle modifications, and that is Insulin Resistance, a common condition which is estimated to affect at least one in four people! IntroductionBacteria of the Corynebacterineae, a suborder of the Actinobacteria, comprise Mycobacterium, Corynebacterium, Nocardia, Rhodococcus and other genera.
Dashed lines indicate that some of the fatty acid products are further utilized for mycolic acid production. A progression from PIM1 to AcPIM2 via AcPIM1 can also occur but is sub-optimal in mycobacteria.
This suborder of high GC gram-positive bacteria includes a number of important human pathogens, such as Mycobacterium tuberculosis, Mycobacterium leprae and Corynebacterium diphtheriae, the causative agents of tuberculosis, leprosy and diphtheria, respectively.

As shown for CD4+ T cells, interleukin-12 (IL-12), IL-4 and IL-6 activate signal transducer and activator of transcription 4 (STAT4), STAT6 and STAT3, respectively. Powell is a professor in the Division of Immunology and the Department of Oncology at Johns Hopkins University School of Medicine, Maryland, USA.
His laboratory studies the role of mammalian target of rapamycin (mTOR) in integrating signals from the immune microenvironment to guide T cell differentiation and function.Contact Jonathan D. The Corynebacterineae also includes non-pathogenic species such as Mycobacterium smegmatis, a saprophytic species, and Corynebacterium glutamicum, an industrial workhorse for the production of amino acids and other useful compounds. These long chain ?-branched, ?-hydroxylated fatty acids are covalently linked to the arabinogalactan polysaccharide layer.
Intermediates representing Gl-Y and Gl-Z have been detected in very recent studies (Rainczuk et al, submitted).
This mycolic acid layer is complemented by a glycolipid layer to form an outer “mycomembrane” analogous to the outer membrane of Gram-negative bacteria.
The outer leaflet of the mycomembrane is composed of a variety of lipids including trehalose dimycolates (TDMs), glycopeptidolipids (GPLs), phthiocerol dimycocerosates (PDIMs), sulfolipids, phenolic glycolipids (PGLs), and lipooligosaccharides. Some of these lipids are widely distributed while others are restricted to particular species. For example, TDMs and their structural equivalents are found in both mycobacteria and corynebacteria, while PDIMs and PGLs are restricted to a subset of mycobacteria. The structure and hydrophobic properties of the cell wall make it a potent permeability barrier that is responsible for intrinsic resistance of mycobacteria to an array of host microbiocidal processes, many antibiotics and sterilization conditions [3, 4]. Many of the cell wall components of pathogenic mycobacterial species are essential for pathogenesis and in vitro growth, hampering efforts to characterize the function of individual proteins in their assembly. Studies on mycobacteria and corynebacteria provide a unique opportunity to illustrate the complexity and diversity of lipid metabolic pathways in bacteria. They have a significantly higher lipid content than other bacteria with cell wall lipids comprising ~40% of the dry cell mass.
It has devoted a significant proportion of its coding capacity to lipid metabolism and produces about 250 enzymes dedicated to fatty acid metabolism, which is around five times the number produced by Escherichia coli [5].
Lipid biosynthesis places a significant metabolic burden on the organism but is ultimately advantageous, allowing M. While capable of de novo synthesis, these bacteria also scavenge and degrade host cell membrane lipids to acetyl-CoA, via broad families of ?-oxidation and other catabolic enzymes, for incorporation into their own metabolic pathways and to fuel cellular processes.
While some lipid metabolic reactions take place in the cytoplasm or cell wall, the plasma membrane is the pivotal site for the metabolism of lipids. Studies on how these metabolic and cellular processes might be organized within bacterial plasma membranes are in their infancy. Understanding the homeostasis of the plasma membrane is particularly important in Corynebacterineae organisms because this structure must support the high biosynthetic demands of sustaining such a lipid-rich cell wall.
In this chapter, we focus our discussion on processes of lipid metabolism that are critical for the biogenesis and maintenance of the plasma membrane, and illustrate the recent progress on our understanding of plasma membrane biogenesis in mycobacteria and corynebacteria.2. Functions of plasma membrane lipids in mycobacteria and corynebacteriaIn this section we will describe the functions of plasma membrane lipids.
Lastly, we will discuss the functions of neutral lipids because their biosynthesis is closely linked to phospholipid metabolism and neutral lipid storage is a critical part of plasma membrane homeostasis. Structural lipidsMajor structural components of the mycobacterial plasma membrane are phospholipids such as cardiolipin (CL), phosphatidylethanolamine (PE), phosphatidylinositol (PI), and glycosylated PIs (i.e. The ratio of these phospholipids may vary depending on the species and growth conditions [6-8].
Phosphatidylglycerol (PG), which is abundant in other bacteria, is a relatively minor species in mycobacteria. In corynebacteria, major species of phospholipids are PI, PG, CL, and acylphosphatidylglycerol (APG) [13], and PE appears to be absent. Nonyl acridine orange (NAO) is a fluorescent dye which is proposed to bind the hydrophobic surface created by the CL cluster [14], allowing microscopic visualization of CL domains. Indeed, using NAO, CLs were found to be enriched in septa and poles of actively dividing M. CL has a non-bilayer structure [17, 18], and carries a small partially immobilized head group that is more exposed to the aqueous environment than those of other glycerophospholipids [19]. Although the physiological function of CL is unclear, its physical properties may indicate that it provides a platform for membrane-protein interactions.
Indeed, some mycobacterial enzymes require CL for activity [20-22], although the molecular basis for these observations has not been clarified. However, a large proportion of CL is also found to be associated with the outer membrane [24], suggesting that some of these phospholipids are exported to the outer membrane in corynebacteria. It has been suggested that lyso-CL may influence host immune responses during infection.PE is another major class of glycerophospholipids in mycobacteria.
Although PE is generally found in all organisms, it is particularly abundant in bacterial plasma membranes [26]. Mycobacteria are no exception [20], but corynebacteria apparently lack the capacity to synthesize PE [27]. Indeed, PE biosynthetic enzymes, such as PS synthetase and PS decarboxylase, appear to be absent in corynebacterial genomes.
Corynebacterium aquaticum has been reported to possess PE [28], but this species was later reclassified as Leifsonia aquatica [29], which belongs to the suborder Micrococcineae of the order Actinomycetales. The functions of PE remain elusive at the molecular level, but it appears to play important roles as a component of the plasma membrane. PIs are an important class of phospholipids, and are known to be further modified by extensive glycosylation. The resultant lipoglycans, termed PIMs, LM, and LAM, are essential structural components of mycobacterial and corynebacterial cell walls. Furthermore, in pathogenic species, they have been suggested to perform additional roles in the modulation of host immune responses in favor of the pathogen through myriad effects on macrophages including cytokine production, inhibition of phagosome maturation and apoptosis [31-34]. It remains controversial if these glycolipids are embedded in the plasma membrane or exported to the outer membrane. For example, a pimE-deletion mutant that cannot produce mature PIM6 species (see below) is viable, but shows severe plasma membrane abnormalities [36], suggesting that higher order PIMs may be involved in the maintenance of plasma membrane integrity. APG is an acylated form of PG which is widespread in corynebacteria [37-40], and is a major phospholipid species in Corynebacterium amycolatum.
Therefore, APG and API are likely to be components of the plasma membrane, and are suggested to play structural roles. Very little is known about their biosynthesis, and acyltransferases responsible for their synthesis remain to be identified for both lipid species. Functional lipidsThere are some examples of lipids that appear to play no structural roles in the plasma membrane.
Two well-studied examples are polyprenol phosphomannose (PPM) and decaprenol phosphoarabinose (DPA). These molecules are the donors of mannose and arabinose, respectively, and their biosynthesis will be discussed in a later section. It accumulates only transiently upon stimulation by high concentrations of salt, and behaves as if it is involved in a signaling cascade.
However, whether PI 3-phosphate represents a mediator of stress responses remains to be addressed. The synthesis of lysinylated PG is mediated by LysX and a lysX deletion mutant showed altered phospholipid metabolism and membrane integrity [16, 44], suggesting a regulatory role of lysinylated PG in plasma membrane homeostasis. Carotenoids are photo-protective pigments and serve to scavenge free radicals or harvest light [45].

Several mycobacterial species are known to produce carotenoids with the notable exception of M. Lipid storage for energy and carbonNeutral lipids are an important reservoir of stored energy and carbon, and their metabolism is closely linked to plasma membrane phospholipid metabolism. Unlike many other bacteria which use polyhydroxyalkanoates as a lipid storage material [47], Actinobacteria use triacylglycerides (TAGs) as a major form of lipid storage, and the presence of TAGs has been reported in Mycobacterium, Streptomyces, Rhodococcus and Nocardia [48-52]. Interestingly, corynebacteria seem to lack the capacity to synthesize TAG, indicating that some lineages of Actinobacteria have eliminated this capacity at some point in their evolution.
Nevertheless, a mutant defective in accumulating TAG remained viable under in vitro dormancy-inducing conditions [54].
These somewhat contradictory observations suggest that our understanding of TAG metabolism in mycobacteria is far from complete.
As we illustrate later, there appear to be several redundant genes involved in the final step of TAG synthesis, suggesting that it is an important regulatory step of lipid metabolism in these bacteria.
Cholesterol has recently been suggested to be an alternative form of lipid storage in mycobacteria. Cholesterol catabolism is critical in the chronic phase of animal infection, and a fully functional catabolic pathway is encoded by the M. Furthermore, cholesterol appears to accumulate in the mycobacterial cell envelope, and this might represent a potential form of lipid storage for M. Although the authors of this study suggested that cholesterol accumulates in the outer membrane, it remains possible that the plasma membrane is the true site of accumulation. Metabolized propionyl-CoA is in part incorporated into TAG [63], and it has been suggested that TAG functions as a sink for reducing equivalents in addition to being a source of carbon and energy. Structure and metabolism of plasma membrane lipids in mycobacteria and corynebacteriaIn this section, we will describe the structure and metabolism of various lipids found in the plasma membrane of mycobacteria and corynebacteria in more detail. Lipids are categorized into the following four classes based on their key structural features. Fatty acid metabolism is essential for intracellular survival of the pathogen since it forms the precursors of key membrane components such as plasma membrane phospholipids and outer membrane glycolipids. In particular, mycolic acids, which are very long chain ?-alkyl ?-hydroxy fatty acids, form the hydrophobic, protective mycomembrane described earlier. The key elongation unit is malonyl-CoA, which is produced by acetyl-CoA carboxylase (ACCase) and the M.
De novo synthesis by FAS-ISurprisingly, members of the Corynebacterineae use a eukaryote-like FAS-I system for de novo fatty acid synthesis.
This very large protein elongates acetyl groups by 2-carbon (acetate) units using acetyl-CoA and malonyl-CoA. Early rounds of elongation yield C16 to C18-CoA products that are used for synthesis of membrane phospholipids or to feed into the FAS-II system. More extensive elongation yields C24-C26 products that ultimately form the ?-branch of mycolic acids.
Elongation by FAS-IIThe FAS-II system is commonly found in bacteria and plants and, unlike FAS-I, is composed of a series of separate enzymes, each performing one step in the pathway.
FAS-II elongates medium chain fatty acids derived from FAS-I using malonyl-CoA, producing C18-C30 fatty acids [68]. AcpM is a mycobacterial acyl carrier protein (ACP) and plays a key role in transferring acyl groups between the various enzyme components [70]. Further elongation and processing of the products of FAS-II produces the precursors of the long meromycolate chains that are condensed with the ?-branches derived from FAS-I by the large polyketide synthase Pks13 [72]. Their biosynthesis is overlapping and 1,2-diacyl-sn-glycerol 3-phosphate, commonly known as phosphatidic acid (PA), is an important intermediate at the branch point (Fig. In this section, we focus our discussion on the biosynthesis of PA and its conversion to non-polar lipids. Non-polar lipids are generally divided into three different classes depending on the number of fatty acids attached to glycerol: monoacylglycerol (MAG), diacylglycerol (DAG) and TAG. TAG is a glycerol carrying three fatty acyl chains, and its biosynthesis diverges from phospholipid synthesis after the synthesis of PA. How TAG is made in the plasma membrane and incorporated into lipid droplets remains largely unclear. Biosynthesis of PAThe first step of PA biosynthesis is mediated by glycerol phosphate acyltransferase (GPAT) transferring an acyl chain from acyl-CoA to glycerol-3-phosphate, forming acyl-glycerol 3-phosphate. However, mycobacteria are unusual in that 2-acyl-sn-glycerol 3-phosphate is used as the main intermediate for the production of PA [75]. Another unusual feature is that oleic acid, an unsaturated fatty acid often found at the sn-2 positions of glycerolipids, is found at the sn-1 position in mycobacteria. Instead, palmitic acid, a saturated fatty acid, is the preferred fatty acid attached to the sn-2 position in mycobacteria [75, 76]. In the second step, acylglycerol phosphate acyltransferase (AGPAT) further transfers a fatty acid from acyl-CoA to 2-acyl-sn-glycerol 3-phosphate, producing PA. PA can be diverted to TAG synthesis, or activated to form cytidine diphosphate-diacylglycerol (CDP-DAG), which is the precursor for the synthesis of phospholipids.
Therefore, PA represents an important branch point for the synthesis of TAG and phospholipids [74]. An alternative pathway for PA synthesis is phosphorylation of DAG by DAG kinase, and Rv2252 has been suggested to be involved in this reaction [77].
Disruption of this enzyme results in altered PIM biosynthesis, but precise functions of this metabolic pathway remain unclear. First, PA is dephosphorylated to become DAG, and this reaction is mediated by phosphatidic acid phosphatase (PAP). PAP was discovered from animal tissues in 1957 by the group of Eugene Kennedy [78], and the gene encoding this activity was recently identified in Saccharomyces cerevisiae [79]. In the second step, diacylglycerol acyltransferase (DGAT) catalyzes the addition of a fatty acyl-CoA to DAG to form TAG.
Until recently, little was known about the genes involved in this final step of TAG synthesis in mycobacteria. Analysis of this final step is complicated because there are multiple genes encoding TAG synthetase in mycobacteria and corynebacteria.
Despite the redundancies, recent studies reported that some of these tgs genes are critical for TAG synthesis in M. Specifically, TAG synthetases encoded by Rv3130c (tgs1), Rv3734c (tgs2), Rv3234c (tgs3), and Rv3088 (tgs4) have been shown to have TAG synthetase activities [53].
Furthermore, Tgs1 has been demonstrated to be the main contributor to TAG synthesis and lipid droplet formation in M.
More recently, Ag85A, which is known as a mycolyltransferase involved in TDM biosynthesis, was shown to possess DGAT activity [81]. Ag85A is not homologous to other tgs genes, and may represent a novel class of TAG biosynthetic enzymes. TAG not only forms a lipid droplet in the cytoplasm, but also accumulates in the cell wall of mycobacteria [82]. Therefore, Ag85A located in the cell wall might be involved in the production of surface-exposed TAGs.
Utilization of TAGUnder starvation conditions where stored TAG needs to be mobilized for energy production, TAG is catabolized by lipases.

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