The products of the nonenzymatic glycation and oxidation of proteins, lipids and nucleic acids,
the advanced glycation end-products (AGEs), accumulate in various pathological conditions, such as diabetes, inflammation,
renal failure, and aging. AGEs accumulate at site of microvascular injury in diabetes, including the kidney, the retina,
and within the vasculature. The enhanced formation of AGEs also exists in various disease, such as atherosclerosis, Alzheimer’s
disease, end-stage renal disease (ESRD), rheumatoid arthritis and liver cirrhosis.
AGEs can arise not only from glucose,
but also from dicarbonyl compounds, short chain-reducing sugars and other metabolic pathways of glucose.
Methylglyoxal (MG) increases in diabetes and can modify proteins rapidly and form AGE-4. It has been showed that exogenously
added MG has a strong synergistic effect on TNF-induced cell death and AGE-4 is formed during TNF-induced cell in death mouse
L929 cell, and that increased MG and AGE-4 levels induce apoptosis in mycobacterial-infected macrophages. It also has been
demonstrated that MG rapidly modifies the PTP covalently and stabilizes the PTP in the closed conformation in rat liver
mitochondria. Moreover, it has been showed that an increase in intracellular MG concentration inhibit the insulin signaling
pathway and leads to an insulin-resistant state in L6 muscle cells.
This antibody is specific to AGE-4 and will be
useful to research for diabetes, chromic diseases associated with aging and diabetic complications, cell death
Takeuchi M, et al
., Mol Med. 2000 Feb;6(2):114-25.
Takeuchi M, et al
., Mol Med. 2001 Nov;7(11):783-91.
Van Herreweghe F, et al
., Proc Natl Acad Sci U S A. 2002 Jan 22;99(2):949-54. Epub 2002 Jan 15.
Speer O, et al
., J Biol Chem. 2003 Sep 12;278(37):34757-63. Epub 2003 Jun 18.
Riboulet-Chavey A, et al
., Diabetes. 2006 May;55(5):1289-99.
Rachman H, et al
., PLoS One. 2006 Dec 20;1:e29.
This product is generated from GANP mice