Isolation and characterization of two binding proteins for advanced glycosylation end products from bovine lung which are present on the endothelial cell surface.

Schmidt, AM; Vianna, Mônica Ryff Moreira Roca; Gerlach, Marlene L.; Brett, Jerold; Ryan, J; Kao, J; Esposito, Ciro; Hegarty, H.M.; Hurley, W.L.; Clauss, Matthias

doi:10.1016/s0021-9258(18)42137-0

Cited by 735 publications

(90 citation statements)

References 32 publications

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“…AGEs are ligands for the receptor for advanced glycation endproducts (RAGE), a membrane-bound receptor of the immunoglobulin family (303,304). Originally discovered in 1992 as an AGE-binding receptor (305), several additional ligands have been identified including S100/calgranulins, amyloid fibrils, amphoterins, and Mac-1. RAGE can thus be viewed as a relatively promiscuous pro-inflammatory pattern recognition receptor (303,304).…”

Section: Effects Mediated Through the Receptor For Advanced Glycation Endproductsmentioning

confidence: 99%

“…This leads predominantly to sustained activation of NF-κB-and STAT-dependent gene transcription (304,(308)(309)(310). As, typically, studies have been performed using soluble and globular glycated proteins such as serum albumin or ovalbumin (305,(311)(312)(313), it is not entirely clear whether "AGEd" collagen is capable of inducing these pathways. Studies using glycated collagen have established a RAGE-dependent link between "AGEd" collagen and apoptosis of mesenchymal cells.…”

Section: Effects Mediated Through the Receptor For Advanced Glycation Endproductsmentioning

confidence: 99%

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Collagen Biosynthesis, Processing, and Maturation in Lung Ageing

et al. 2021

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In addition to providing a macromolecular scaffold, the extracellular matrix (ECM) is a critical regulator of cell function by virtue of specific physical, biochemical, and mechanical properties. Collagen is the main ECM component and hence plays an essential role in the pathogenesis and progression of chronic lung disease. It is well-established that many chronic lung diseases, e.g., chronic obstructive pulmonary disease (COPD) and idiopathic pulmonary fibrosis (IPF) primarily manifest in the elderly, suggesting increased susceptibility of the aged lung or accumulated alterations in lung structure over time that favour disease. Here, we review the main steps of collagen biosynthesis, processing, and turnover and summarise what is currently known about alterations upon lung ageing, including changes in collagen composition, modification, and crosslinking. Recent proteomic data on mouse lung ageing indicates that, while the ER-resident machinery of collagen biosynthesis, modification and triple helix formation appears largely unchanged, there are specific changes in levels of type IV and type VI as well as the two fibril-associated collagens with interrupted triple helices (FACIT), namely type XIV and type XVI collagens. In addition, levels of the extracellular collagen crosslinking enzyme lysyl oxidase are decreased, indicating less enzymatically mediated collagen crosslinking upon ageing. The latter contrasts with the ageing-associated increase in collagen crosslinking by advanced glycation endproducts (AGEs), a result of spontaneous reactions of protein amino groups with reactive carbonyls, e.g., from monosaccharides or reactive dicarbonyls like methylglyoxal. Given the slow turnover of extracellular collagen such modifications accumulate even more in ageing tissues. In summary, the collective evidence points mainly toward age-induced alterations in collagen composition and drastic changes in the molecular nature of collagen crosslinks. Future work addressing the consequences of these changes may provide important clues for prevention of lung disease and for lung bioengineering and ultimately pave the way to novel targeted approaches in lung regenerative medicine.

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Section: Effects Mediated Through the Receptor For Advanced Glycation Endproductsmentioning

confidence: 99%

Section: Effects Mediated Through the Receptor For Advanced Glycation Endproductsmentioning

confidence: 99%

Collagen Biosynthesis, Processing, and Maturation in Lung Ageing

et al. 2021

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“…Hyperglycemia enhances the formation of AGEs, which are formed by the nonenzymatic reaction of glucose and other glycating compounds with proteins [21][22][23]. Plasma proteins modified by AGEs precursors bind to RAGE on cells such as macrophages, vascular endothelial cells, and vascular smooth muscle cells [24,25]. This induces the production of reactive oxygen species, and activation of nuclear factor -B, causing multiple inflammatory cascades in gene expression [26][27][28][29][30].…”

Section: Role Of Ages-rage System For Fibrosis Developmentmentioning

confidence: 99%

Angiotensin II type 1 receptor blocker attenuates diabetes-induced atrial structural remodeling

Kato

Yamashita

Sekiguchi

et al. 2011

Journal of Cardiology

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“…13 AGE-induced effects are also due to their ability to interact, as specific ligands, with the membrane-bound receptor for advanced glycation endproducts (RAGE), isolated and characterized in 1992. 14 The AGE-RAGE interaction leads to a number of adverse phenomena, such as the generation of an excess of intracellular reactive oxygen species (ROS) [15][16][17] or to the enhanced transcription and production of a number of cytokines 18 and pro-inflammatory mediators via the nuclear factor-kB (NF-kB) pathway, 19,20 e.g. the intercellular adhesion molecule-1 (ICAM-1), the vascular cell adhesion molecule (VCAM-1), E-selectin, the tumor necrosis factor-a (TNF-a), interleukin-1 (IL-1), interleukin-6 (IL-6) and cyclo-oxygenase-2 (COX-2).…”

Section: Introductionmentioning

confidence: 99%

Human recombinant lysozyme downregulates advanced glycation endproduct-induced interleukin-6 production and release in an in-vitro model of human proximal tubular epithelial cells

Gallo¹,

Cocchietto²,

Masat

et al. 2014

Exp Biol Med (Maywood)

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Diabetic nephropathy is the leading cause of chronic renal disease and one of the major causes of cardiovascular mortality. Evidence suggests that its progression is due to the chronic hyperglycemia consequent to the production and accumulation of advanced glycation endproducts (AGEs). Lysozyme was shown to posses AGE-sequestering properties and the capacity to reduce the severity of the early stage manifestations of the diabetic nephropathy. This study was aimed to contribute to the understanding the molecular mechanisms of lysozyme effectiveness in the diabetic nephropathy, using an in-vitro cellular model, represented by the HK-2 cells, human proximal tubular epithelial cells. Lysozyme significantly reduced the AGE-induced IL-6 mRNA and an ELISA assay showed also a decreased release of the functional protein with a dose-dependent trend. In addition, lysozyme prevented macrophage recruitment, suggesting its capacity to elicit an anti-inflammatory action. We may conclude that the protective action of lysozyme on the nephrotoxic effects of AGE may depend, at least in part, on its ability to prevent the production and release of inflammatory mediators, such as IL-6 and to reduce macrophage recruitment in the inflammatory sites.

show abstract

Isolation and characterization of two binding proteins for advanced glycosylation end products from bovine lung which are present on the endothelial cell surface.

Cited by 735 publications

References 32 publications

Collagen Biosynthesis, Processing, and Maturation in Lung Ageing

Collagen Biosynthesis, Processing, and Maturation in Lung Ageing

Angiotensin II type 1 receptor blocker attenuates diabetes-induced atrial structural remodeling

Human recombinant lysozyme downregulates advanced glycation endproduct-induced interleukin-6 production and release in an in-vitro model of human proximal tubular epithelial cells

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