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Fucosidosis
Published in William L. Nyhan, Georg F. Hoffmann, Aida I. Al-Aqeel, Bruce A. Barshop, Atlas of Inherited Metabolic Diseases, 2020
Fucose is a deoxysugar, an aldohexose in which the terminal CH2OH is replaced by a methyl group (Figure 95.1). It occurs in glycoproteins and glycolipids as a terminal oligosaccharide linked to galactose or N-acetylglucosamine (Figure 95.2). The degradation of glycoproteins takes place sequentially in the lysosomes. Fucosidosis is a glycoprotein storage disease in which patients have impaired degradation of fucose-containing glycoproteins.
Insights into the Recent Scientific Evidences of Natural Therapeutic Treasures as Diuretic Agents
Published in Debarshi Kar Mahapatra, Cristóbal Noé Aguilar, A. K. Haghi, Applied Pharmaceutical Practice and Nutraceuticals, 2021
Vaibhav Shende, Sameer Hedaoo, Debarshi Kar Mahapatra
The whole organic processes of filtering the fluid happen by diffusion process.18 Since the produced capillary vessel filtrate is actually isoosmotic, it largely depends on the metal organic process to form the associate diffusion gradient.19 Once the formation of a plasma ultrafiltrate within the capillary occur, the fluid enters the proximal convoluted tube-shaped structure, where specific transporters absorb metal, chloride, hydrogen carbonate, aldohexose, and amino acids.20 Concerning the amount of water and most of the organic solutes, they are again reabsorbed within the proximal tube-shaped structure.21 At the boundary between the inner and outer stripes of the outer medulla, the skinny dropping limb of Henle activity reabsorbs both sodium and chlorine from the lumen (about 3/5th of the filtered sodium).22 However, the conditions are not like the proximal tube and therefore the dropping limb is nearly impermeable to the water.23 The sodium chloride resorption occur within the thick ascending limb effectively, which dilutes the fluid, therefore this section is termed the “diluting segment.”24 The loop of Henle also acts in producing a countercurrent regarding the formation of a gradient of hyperosmolarity within the medullary interstitium.25 The distal convoluted tube-shaped structure connects the diluting section, where around 100% of the filtered common salt is reabsorbed.26 Just like the thick ascending limb, the membrane is comparatively tight to water, therefore ensues more dilution.27
Sirtuins as therapeutic targets for improving delayed wound healing in diabetes
Published in Journal of Drug Targeting, 2022
Fathima Beegum, Anuranjana P. V., Krupa Thankam George, Divya K. P., Farmiza Begum, Nandakumar Krishnadas, Rekha R. Shenoy
A number of studies have emphasised that SIRT 3 expression is less in diabetes. Low levels of SIRT 3 have been observed in diabetic patients. Wound macrophages have diminished SIRT 3 levels due to fatty acid-binding protein-4 activation. Inadequate SIRT 3 expression is one of the vital reasons for delayed diabetic wound healing [104]. The studies in SIRT 3 knockout mice suggested that high aldohexose content attenuated the proliferation and migration of skin fibroblasts, hence produced oxidative stress [104]. Even though an acceptable amount of free radical aids in wound healing, the excess quantity will negatively influence the healing process by suppressing proliferation, migration of repairing cells, and ECM synthesis. Impairment of the antioxidant system by weakening free radicals scavenging and increasing macromolecule peroxidation is found in diabetes. SIRT 3 protects excessive ROS and regulates the repair process [113]. Hyperglycaemia with SIRT 3 deficiency ends up in severe oxidative stress and reduced VEGF expression which limits angiogenic response and quick wound repair in diabetic patients. The SIRT 3 deficiency can damage mitochondrial structure and performance, increase ROS production and induce necroptosis [71]. SIRT 3 can be a potential target for delayed wound healing in diabetes.
Clot activators and anticoagulant additives for blood collection. A critical review on behalf of COLABIOCLI WG-PRE-LATAM
Published in Critical Reviews in Clinical Laboratory Sciences, 2021
G. Lima-Oliveira, L. M. Brennan-Bourdon, B. Varela, M. E. Arredondo, E. Aranda, S. Flores, P. Ochoa
The additives, sodium fluoride and iodoacetate, are used to improve the accuracy of glucose determination by reducing glycolysis in vitro [147] (Figure 9). However, these additives should be used in combination with an anticoagulant additive – EDTA, oxalate, or heparin – with or without mannose. It should be noted that at least 3 h are required to stabilize the glucose in blood samples [148,149]. Mannose is a C-2 epimer of glucose and a sugar monomer of the aldohexose series of carbohydrates, differing structurally from glucose in the configuration around just one carbon atom [150]. Thus, in vitro mannose is a competitive inhibitor of hexokinase with a short half-life (4 h) [151]. While fluoride is able to move rapidly across the erythrocyte membrane [152], the additives, fluoride and oxalate, do not completely prevent the in vitro decrease of glucose [153,154]. Sodium fluoride inhibits enolase [155,156] in the presence of inorganic phosphate; the fluorophosphate ion is the inhibitory species, which, when bound to magnesium, forms a complex with enolase and inactivates the enzyme [157]. It is noteworthy that samples collected with fluoride and oxalate show hemolysis [158], making the samples unsuitable for other assays.
Intra-site differential inhibition of multi-specific enzymes
Published in Journal of Enzyme Inhibition and Medicinal Chemistry, 2020
Mario Cappiello, Francesco Balestri, Roberta Moschini, Umberto Mura, Antonella Del-Corso
Although a “complete” intra-site differential inhibitor as defined above has not as yet been envisaged for AKR1B1, molecules able to differentially inhibit aldoses reduction and/or GSHNE reduction versus HNE reduction have been proposed. The typical basic conditions to illustrate in vitro the differential inhibition of AKR1B1 mimic those occurring in a hyperglycaemic status, with the aldose substrates kept at the mM level, and the toxic aldehydes (i.e., HNE) or their glutathionyl-derivatives (i.e., GSHNE) kept at the µM level. D,L-glyceraldehyde, the most common substrate used in AKR1B1 inhibition studies, was also utilised as a substrate in differential inhibition studies. However, the evidence of incomplete inhibitory action exerted on the enzyme activity by aldose hemiacetals51,52, which cannot take place with a triose, suggested the use of an aldohexose as the substrate. Thus, L-idose, an epimer of D-glucose at C5, with a free aldehyde form approximately 80 times higher than what was observed for glucose, was chosen as elective substrate for inhibition studies53. Finally, the problem of poor solubility of molecules often encountered in inhibition studies of AKR1B1 was overcome by using a proper aqueous cocktail of either methanol or dimethyl sulfoxide, after evaluating the limits of their suitability for the enzyme assay20. In these conditions, supported by kinetic analysis of the inhibitory action towards the different substrates, a number of molecules, coming both from organic synthesis and from natural sources, were identified as having differential inhibitory abilities.