title: Recent topics in chemical and clinical research on glycated albumin.
abstract: The measuring method for glycated albumin (GA) has been developed as a new glycemic control marker since the beginning of the 21st century. Since GA has an advantage in reflecting glycemic status over a shorter period than hemoglobin A1c (HbA1c), much research and many reviews have been reported. However, so far there have been few reports on glycation sites based on the tertiary structure of human serum albumin (HSA) and the comparison of glycation rates between GA and HbA1c in detail. The present review discusses how the glycation sites of lysine residues in HSA are modified with glucose, whereas the glycation sites of lysine residues are located inside of HSA as well as the direct comparison of glycation rates between GA and HbA1c using human blood. Moreover, the most recent clinical researches on GA are described.
authors.affiliation: Diagnostics Department, Research and Development Group, Asahi Kasei Pharma Corporation, Shizuoka, Japan.
authors.forename: Yuki
authors.initials: Y
authors.lastname: Ueda
authors.affiliation: Diagnostics Department, Research and Development Group, Asahi Kasei Pharma Corporation, Shizuoka, Japan matsumoto.hb@om.asahi-kasei.co.jp.
authors.forename: Hideyuki
authors.initials: H
authors.lastname: Matsumoto
mesh_terms: D015415:Biomarkers / Q000097:blood; D003920:Diabetes Mellitus / Q000097:blood; D006442:Glycated Hemoglobin / Q000032:analysis / Q000737:chemistry; D017127:Glycation End Products, Advanced; D006801:Humans; D012709:Serum Albumin / Q000032:analysis* / Q000737:chemistry*; D000093423:Glycated Serum Albumin
chemical_list: D015415:Biomarkers; D006442:Glycated Hemoglobin; D017127:Glycation End Products, Advanced; D012709:Serum Albumin; D000093423:Glycated Serum Albumin
keywords: diabetes; enzymatic method; glycated albumin; glycation