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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.
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
The AGE-Reader medical analyzer of end products of glycation [37] is a diagnostic device that noninvasively measures the content of AGEs in tissues as a parameter of UV-induced autofluorescence in the real-time mode. It includes a spectrometer, fiber probe, and UV fluorescent lamp with the emission range of 300–420 nm. The measurement of radiation is carried out in the area of the patient’s forearm; the result reflects the ratio of the intensity of autofluorescence (420–600 nm) to the intensity of the reflected exciting radiation (300–420 nm). In the clinical practice, this device is used to assess the risk of cardiovascular complications in patients with diabetes mellitus.
Marine Algae in Diabetes and Its Complications
Published in Se-Kwon Kim, Marine Biochemistry, 2023
Proteins or lipids are modified by glycosylation non-enzymatically in hyperglycemia to form AGEs and are subsequently oxidized. Schiff bases and Amadori products are formed due to early oxidation and glycation processes. Persistent glycation leads to molecular rearrangements that aids in AGE formation (Schmidt et al., 1994). Glycated products generate reactive oxygen species (ROS), engage receptors on the cell surface, and cross-link them. Important factors critical to AGE formation incorporate the rate of turnover of proteins for glycoxidation, the extent of hyperglycemia, and oxidative stress in the milieu (Figure 2.1). If these conditions prevail, glycation and oxidation of both intracellular and extracellular proteins are certain. The AGE formation (by the Maillard reaction) happens due to the reaction between Schiff bases and Amadori product with the -NH2 moieties of biomolecules (Giovino et al., 2020). During Amadori reorganization, these intermediary carbonyl groups that are highly reactive accumulate and are known as α-dicarbonyls or oxoaldehyde. These are the products of 3-deoxyglucosone and methylglyoxal. Such accumulation is called “carbonyl stress”. The α-dicarbonyls react with -SH, -NH2, and guanidine functional groups resulting in browning, cross-linking, and denaturation of the target proteins. They also react with arginine and lysine to form stable, non-fluorescent AGE products such as N-α-(carboxymethyl)lysine (CML). Protein glycation increases free radical activity that brings forth bimolecular damage in diabetes. AGEs act as initiators of a lot of abnormal cellular and tissue responses, such as the illicit expression of growth factors, extracellular matrix accumulation, and induction of cell death (Suzuki et al., 1999).[
Noninvasive diagnosis of type 2 diabetes mellitus by hair analysis using laser-induced breakdown spectroscopy (LIBS)
Published in Instrumentation Science & Technology, 2023
Imen Cherni, Mohamed Nakkach, Hassen Ghalila, Rihem Nouir, Mehdi Somai, Fatma Daoued, Imen Rachdi, Fatma Boussema, Nejmeddine Jaidane, Sami Hamzaoui
Type 2 diabetes mellitus is a major worldwide public health problem today.[1,2] The number of diabetics were estimated to increase from 171 million in 2000 to 366 million in 2030 according to World Health Organization and up to 700 million in 2045 according to recent International Diabetes Federation.[3–6] Diabetes leads to degenerative microvascular and macrovascular complications, with an ever-increasing incidence. The accumulation of advanced glycation end-products (AGEs) in the organism and glycosylation of several proteins induce these diabetes-related complications.[7–9] As consequences of these degenerative complications, diabetes leads to many modifications in the organism on the systemic, tissular, molecular, and atomic levels. According to the literature,[10–18] diabetes is linked to the modifications of several elemental concentrations, including Ca, Na, Mg, Zn, Cu, Cr, Fe, Mn, V, and Se. These changes have been noted on several types of biological samples such as plasma, urine, skin, fingernails, and hair.[19–24]
A review on artificial pancreas and regenerative medicine used in the management of Type 1 diabetes mellitus
Published in Journal of Medical Engineering & Technology, 2022
Pallavi Sachdeva, Ashrit R. M., Rahul Shukla, Ashish Sahani
Type 1 diabetes mellitus (often abbreviated as T1D or T1DM) affects nearly 15 in 100,000 people around the world, with the same number being met in Asia. It predominantly affects people under the age of 20 (nearly 85% of cases) and shows a strong genetic link [1–3]. Multiple studies have confirmed the long-standing suspicion that the chronic disease is true of autoimmune nature [4]. The beta cells in the pancreas responsible for insulin production are destroyed by defunct immunogenic agents resulting in an absolute insulin deficiency (the aetiology and pathogenesis are what contrasts it from type 2 diabetes where there is an increased insulin resistance compounds low insulin secretion leading to hyperglycaemia) [5]. Typical manifestations of the disease resulting from hyperglycaemia include frequent urination, excessive hunger and decreased wound healing [6]. The condition chronic hyperglycaemia and genetic variability causes the production of advanced glycation end products (AGEs), the creation of proinflammatory microenvironment, and the induction of oxidative substances which lead to the development of vascular complications. Effects on small blood vessels cause microvascular complications, such as diabetic neuropathy nephropathy and retinopathy and effect on larger blood vessels to cause macrovascular complication, such as ischaemic heart disease, peripheral vascular disease, and cerebrovascular disease [7,8]. The condition of diabetes (both type 1 and type2) increases the risk of stroke by five times [9].
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.