Abstract
Glycosyl-ation is the process of combining one or more glucose molecules (or other monosaccharides) with molecules of a different nature (which are therefore glycosyl-ated). In biochemistry, glycosyl-ation is catalyzed by several specific enzymes, and assumes considerable importance since it occurs mainly at the expense of proteins and phospho-lipids which are thus transformed into glycoproteins and glycolipids. Conversely, in diabetes and aging, glycation of proteins is a phenomenon of non-enzymatic nature and thus not easily controlled. Glycation of collagen distorts its structure, renders the extracellular matrix stiff and brittle and at the same time lowers the degradation susceptibility thereby preventing renewal. Based on models detailed in this paper and with parameters determined from experimental data, we describe the glycation of type 1 collagen in bovine pericardium derived bio-tissues, upon incubation in glucose and ribose. With arginine and lysine/hy-droxy-lysine amino acids as the primary sites of glycation and assuming that the topological polar surface area of the sugar molecules determines the glycation rates, we modelled the glycation as a function of time and determined the glycation rate and thus the progression of glycation as well as the resulting volume increase.
Highlights
Diabetes mellitus (DM) is a pathological condition characterized by a high blood glucose and insulin concentration for a long period of time
When it increases to 126 mg dlÀ1 the condition is defined as impaired fasting glucose (IFG) which develops into DM for blood glucose concentrations over 126 mg dlÀ1 (American Diabetes Association, 2016)
Decellularized bovine pericardia have been used as collagen tissue and kept in a water solution mixed with sugars at increasing concentration from 0 to 40 mg mlÀ1 for different incubation times, from 0 to 90 days (Giannini et al, 2019, 2021), and for different type of sugars: ribose, glucose and galactose
Summary
Diabetes mellitus (DM) is a pathological condition characterized by a high blood glucose (hyperglycemia) and insulin concentration for a long period of time. Among the complication of diabetes are alterations of micro and macro circulation, inducing multiple organ dysfunctions, and activation of proinflammatory pathways The link between these pathological conditions and hyperglycemia are the advanced glycation endproducts (AGEs) formed by the non-enzymatic crosslink reaction between small sugars, in particular glucose, fructose and ribose, and lipids and proteins. 8, 1024–1034 research papers group of reducing sugars with the free amino groups of the amino acid side chains such as lysine, hydroxylysine or arginine During this first step, a non-stable Schiff base is formed (adduct) and is subsequently stabilized in ketoamine, known as Amadori’s product. The glucosepane (Sell et al, 2005) is the most abundant and relevant AGE in collagen-rich tissues, as it was found to increase by 1000 times in diabetics with respect to non-pathological tissues It is a characteristic crosslink between lysine, glucose and arginine. Mentally, for example, using the tissue model system on which the experimental part of this study is based
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
