Glycated albumin (Amadori product) induces activation of MAP kinases in monocyte-like MonoMac 6 cells

被引:13
作者
Brandt, Rowena [1 ]
Krantz, Sven [1 ]
机构
[1] Ernst Moritz Arndt Univ Greifswald, Inst Med Biochem & Mol Biol, Klinikum Greifswald, D-17487 Greifswald, Germany
来源
BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS | 2006年 / 1760卷 / 11期
关键词
glycated albumin; fructoselysine; receptor; signal transduction; MonoMac; 6;
D O I
10.1016/j.bbagen.2006.09.004
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 [生物化学与分子生物学]; 081704 [应用化学];
摘要
Increased levels of glycated, Amadori-modified albumin are a risk factor for diabetic vascular disorders. Glycated albumin binds to specific receptors and induces cellular signaling pathways, the complexity of which is largely unknown. Binding of glycated albumin to MonoMac 6 cells leads to an activation of MAPK p44/42 (ERK1/2) and p38 with subsequent translocation of NF-kappa B into the nucleus. The activation of MAPK is in part mediated by protein kinase C activation, but a PKC-independent pathway via MEK-1 is also involved. Protein tyrosine kinases do not play a role in the activation of NF-kappa B. The results may have pathophysiological significance, because the MonoMac 6 cell line is not greatly different from blood monocytes. (c) 2006 Elsevier B.V. All rights reserved.
引用
收藏
页码:1749 / 1753
页数:5
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