Unveiling the molecular mechanisms underpinning biorecognition of early-glycated human serum albumin and receptor for advanced glycation end products

A Tramarin, M Naldi, G Degani, L Lupu… - Analytical and …, 2020 - Springer
Serum levels of early-glycated albumin are significantly increased in patients with diabetes
mellitus and may play a role in worsening inflammatory status and sustaining diabetes …

[HTML][HTML] A capture method based on the VC1 domain reveals new binding properties of the human receptor for advanced glycation end products (RAGE)

G Degani, AA Altomare, M Colzani, C Martino… - Redox Biology, 2017 - Elsevier
Abstract The Advanced Glycation and Lipoxidation End products (AGEs and ALEs) are a
heterogeneous class of compounds derived from the non-enzymatic glycation or protein …

Binding of receptor for advanced glycation end products (RAGE) ligands is not sufficient to induce inflammatory signals: lack of activity of endotoxin-free albumin …

JV Valencia, M Mone, C Koehne, J Rediske… - Diabetologia, 2004 - Springer
Aims/hypothesis Activation of the receptor for advanced glycation end products (RAGE)
reportedly triggers cellular responses implicated in the pathogenesis of diabetes, such as …

Non-enzymatic glycation mediated structure–function changes in proteins: case of serum albumin

S Awasthi, NT Saraswathi - RSC advances, 2016 - pubs.rsc.org
Albumin, a major plasma protein with extraordinary ligand binding properties, transports
various ligands ranging from drugs, hormones, fatty acids, and toxins to different tissues and …

Moderate glycation of serum albumin affects folding, stability, and ligand binding

SW Vetter, VSK Indurthi - Clinica Chimica Acta, 2011 - Elsevier
BACKGROUND: Serum protein glycation and formation of advanced glycation endproducts
(AGE) correlates with diabetic complications. Highly AGE-modified albumin is frequently …

Impaired drug-binding capacities of in vitro and in vivo glycated albumin

J Baraka-Vidot, A Guerin-Dubourg, E Bourdon… - Biochimie, 2012 - Elsevier
Albumin, the major circulating protein in blood, can undergo increased glycation in diabetes.
One of the main properties of this plasma protein is its strong affinity to bind many …

Glycated serum albumin and AGE receptors

SW Vetter - Advances in Clinical Chemistry, 2015 - Elsevier
In vivo modification of proteins by molecules with reactive carbonyl groups leads to
intermediate and advanced glycation end products (AGE). Glucose is a significant glycation …

Solution Structure of the Variable-Type Domain of the Receptor for Advanced Glycation End Products: New Insight into AGE−RAGE Interaction,

S Matsumoto, T Yoshida, H Murata, S Harada… - Biochemistry, 2008 - ACS Publications
Diabetes is defined by chronic hyperglycemia due to deficiency in insulin action. It has been
found that the amount of advanced glycation end products (AGE) from the Maillard reaction …

Nonenzymatic glycosylation of human serum albumin and its effect on antibodies profile in patients with diabetes mellitus

A Raghav, J Ahmad, K Alam - PLoS One, 2017 - journals.plos.org
Background Albumin glycation and subsequent formation of advanced glycation end
products (AGEs) correlate with diabetes and associated complications. Methods Human …

Expression and characterization of recombinant C-terminal biotinylated extracellular domain of human receptor for advanced glycation end products (hsRAGE) in …

M Kumano-Kuramochi, Q Xie, Y Sakakibara… - Journal of …, 2008 - academic.oup.com
The receptor for advanced glycation end products (RAGE) is a multi-ligand receptor involved
in the development of diabetic complications. Using an Escherichia coli expression system …