Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0011849 (diabetes)
 277,896 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Diabetes, is a metabolic disorder characterised by chronic hyperglycaemia, hypertension, dyslipidaemia, microalbuminuria and inflammation. Moreover, there are a number of complications associated with this condition including retinopathy, neuropathy and nephropathy. Diabetic nephropathy, is the major cause of end-stage renal disease in Western societies affecting a substantial proportion (25-40%) of patients with diabetes. Advanced glycation end products (AGEs) have been identified as important modulators of the development and progression of diabetic nephropathy, through both receptor dependant and independent interactions. AGEs elicit their receptor mediated effects via their engagement with numerous receptors and binding proteins which are broadly thought to be either inflammatory (RAGE and AGE-R2) or clearance receptors (AGE-R1, AGE-R3, CD36, Scr-II, FEEL-1 and FEEL-2). Modulation of AGE receptor expression is an important potential therapeutic approach worth consideration as a treatment for diabetic nephropathy and likely applicable to other vascular complications.
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PMID:Interactions between advanced glycation end-products (AGE) and their receptors in the development and progression of diabetic nephropathy - are these receptors valid therapeutic targets. 1914 35

The scavenger receptor FEEL-1/stabilin-1 is known as the marker of alternatively activated macrophage and sinusoidal endothelial cell. FEEL-1/stabilin-1 is a multifunctional transmembrane glycoprotein that is implicated in bacterial infection, diabetes, atherosclerosis, wound healing, and innate immunity. In the current study, we have identified the phox-homology domain containing protein SNX17 as a novel interaction partner of FEEL-1/stabilin-1 in endothelial cells. SNX17 directly interacts with FEEL-1/stabilin-1 and regulates its trafficking. Studies using the cytoplasmic domain of truncated or mutant FEEL-1/stabilin-1 suggest that the NPxF motif of the FEEL-1/stabilin-1 cytoplasmic tail is required for its interaction with SNX17. By transfecting cells with small interfering RNA targeting SNX17, total cellular FEEL-1/stabilin-1 expression and FEEL-1/stabilin-1-mediated ligand uptake were significantly decreased due to the enhancement of FEEL-1/stabilin-1 protein degradation. Our results identify SNX17 as a novel interaction partner of FEEL-1/stabilin-1 in endothelial cells.
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PMID:Adaptor protein sorting nexin 17 interacts with the scavenger receptor FEEL-1/stabilin-1 and modulates its expression on the cell surface. 2022 21