Acta Med Hist Adriat
January 2024
The Šibenik Foundling House was an institution that cared for abandoned children before their adoption. The paper analysed the accommodation capacities of the foundling house from 1886 to 1900, using registers of baptisms and deaths from the provincial hospital in Šibenik as the basis for the analysis. An analysis of the received children was conducted based on how they arrived at the site and the level of knowledge about their origin or identity.
View Article and Find Full Text PDFThe Spanish flu is a pandemic that was neglected even though it killed more people than World War I. At the end of 1918, newspaper reports are scarce due to war events, press cen-sorships, and burst political events. For decades after the epidemic was over, the Spanish flu was not the subject of scientific research.
View Article and Find Full Text PDFBackground: Advanced glycation endproducts (AGE) are a family of heterogeneous chemical structures formed on the host protein in the conditions of carbonyl or oxidative stress. Among AGE precursors, methylglyoxal (MG) is considered one of the key intermediates.
Methods: In the current study, we describe and evaluate a solid phase time-resolved fluoroimmunoassay (DELFIA) based on the competitive reaction between MG-AGE antibody and competitive antigen for detecting MG-adducts in serum and urine.
Advanced glycation endproducts (AGE) accumulate over proteins as a consequence of diabetic hyperglycemia, and thus contribute to the pathogenesis of diabetic complications. To improve the understanding of the pathology of diabetic neuropathy, AGE accumulation was analyzed in sural and/or femoral nerves obtained under spinal anesthesia from 8 type 2 diabetic patients with both distal symmetrical polyneuropathy and proximal neuropathy. Pronounced AGE immunoreactivity was detected on axons and myelin sheaths in 90% of diabetic peripheral nerves but not in the control specimen.
View Article and Find Full Text PDFCollagenous proteins are especially prone to nonenzymatic glycation, because they contain several dibasic amino acid residues with free amino groups, have a very slow turnover rate, and are exposed to ambient levels of glucose. The aim of this study was to determine the time-dependent course of advanced glycation process in diabetic rats in relation to glycemic control and duration of diabetes, compared to age-matched controls. Immunochemical assay with antibodies to advanced glycation end products (AGE) was first developed to qualitatively detect and quantify the AGE formed in rat tendon and aortic collagen.
View Article and Find Full Text PDFIn an attempt to shed more light on the relation between the glycation process and structural protein alterations, we followed the formation of glycated products in the lenses of hyperglycaemic Wistar rats during a period of 5 months following alloxan diabetes inducement. The study groups included non-diabetic (control), untreated diabetic rats (D), and diabetic rats receiving insulin alone or in combination with phlorizin, an inhibitor of renal tubular glucose transport. Lenses were removed at 4 and 20 weeks, and advanced glycation products in alkalisoluble lens proteins were determined by their characteristic spectrofluorescence (emission at 385 nm with excitation of 335 nm).
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