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Noninvasive Sensing of Serum sRAGE and Glycated Hemoglobin by Skin UV-Induced Fluorescence
Published in Andrey V. Dunaev, Valery V. Tuchin, Biomedical Photonics for Diabetes Research, 2023
Vladimir V. Salmin, Tatyana E. Taranushenko, Natalya G. Kiseleva, Alla B. Salmina
It is known that in type 1 diabetes mellitus, there is an increased content of advanced glycation end products (AGEs), which are the result of non-enzymatic glycation of cell proteins. The accumulation of AGE in the vascular wall leads to the disruption of its structure and functioning and plays a key role in the occurrence of vascular complications. According to the literature, increased accumulation of AGEs in the vessel wall in diabetes is associated with changes in the functional activity of endothelial cells, macrophages, and smooth muscle cells, and leads to the development of endothelial dysfunction, thickening of the basement membrane, and impaired vasoconstriction and vasodilation. Specific AGE receptors are RAGE (Receptors for Advanced Glycation End Products) that belong to the immunoglobulin superfamily. When AGE binds to RAGE, “metabolic memory” is formed as the leading mechanism of the pathogenesis of specific vascular complications. It is important that AGE and RAGE levels are independent of current blood glucose levels and are markers of chronic hyperglycemia over the previous several months [1].
The positional information grid in development and regeneration
Published in David M. Gardiner, Regenerative Engineering and Developmental Biology, 2017
Susan V. Bryant, David M. Gardiner
A number of causes for regenerative decline are being actively investigated (e.g., depletion of the pool of adult stem cells and/or changes in the stem cell niche). In the context of this chapter, we note that any age-associated modifications to the PI grid would result in changes in the way the behavior of regeneration-competent cells is regulated during regeneration. One such modification is the accumulation of advanced glycation end products (AGEs) with age, which is accelerated in association with diseases of aging (e.g., diabetes). The AGEs are protein modifications that occur during metabolism by the non-enzymatic glycation resulting from reactions between glucose and the amino groups of proteins. By incorporating the observation of increasing accumulation of AGEs with aging, along with what we know about the role of the ECM in contributing to and regulating the PI grid, it is possible that the active sites of the PI grid are progressively altered over time. Presumably, glycation of the PI grid would lead to progressive regenerative failure, and thus, therapies to reverse glycation would restore PI grid’s function. The thinking here is that over time, the PI grid needs to be cleaned up, which would lead to the long-sought goal of rejuvenation.
Changes in bioactive components, biological activities and starch digestibility of soymilk residues as affected by far-infrared radiation combined with hot-air and hot-air drying
Published in Drying Technology, 2022
Ekkarat Tangkhawanit, Naret Meeso, Sirithon Siriamornpun
Advanced glycation end products (AGEs) are damaging compounds that are formed when protein or fat combine with sugar in the bloodstream. The high levels of AGEs have been shown to cause oxidative stress and inflammation. Moreover, these compounds are involved the development of many diseases, including diabetes, heart disease, kidney failure, and Alzheimer’s, as well as premature aging.[12] The relevant assay determines the capacity of antioxidant compounds from soy and soymilk residues to inhibit the AGE formation in a glucose-mediated protein glycation system. The percentage of the inhibition of AGEs by sample extracts is presented in Table 5. For the free phenolic fraction, the highest AGE inhibition value was observed for the dried SI-FIR followed by WSB, SI (untreated residue), and dried SI-HA, respectively. Moreover, the AGE inhibition of bound phenolic fractions ranged from 30 to 31% for WSB and SI samples, 14 to 46% for dried SI-HA, and 36 to 42% for dried SI-FIR residues. Bound phenolic extracts of SI-HA 60 had the highest AGE inhibition, followed by dried SI-HA 70 and 80, respectively. Whilst, the AGE inhibition values of free and bound dried SI-FIR at three levels drying temperature were not significantly.