alexa Amadori-modified glycated albumin predominantly induces E-selectin expression on human umbilical vein endothelial cells through NADPH oxidase activation.
Oncology

Oncology

Journal of Integrative Oncology

Author(s): Higai K

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BACKGROUND: Protein glycation is closely linked to endothelial-cell dysfunction and vascular complications in diabetes. Glycated albumin is reported to induce cellular signaling similar to advanced glycation endoproducts (AGEs), however, cellular signaling remains obscure.
METHOD: We stimulated human umbilical vein endothelial cells (HUVECs) by glycated human serum albumin (Glc-HSA), determined E-selectin expression by real-time PCR and immunometric methods, and estimated cellular signaling by using various signaling molecule inhibitors and confocal microscopy.
RESULTS: Glc-HSA-induced E-selectin expression was 10 or 20 times more than that induced with 3 kinds of AGEs-HSAs, which was not suppressed by anti-receptor for AGEs (RAGE) antibody. Glc-HSA-induced E-selectin expression was completely suppressed by the NADPH oxidase inhibitor diphenylene iodonium chloride and the reactive oxygen species (ROS) scavenger N-acetyl-L-cysteine. Confocal microscopic analysis also revealed intracellular accumulation of ROS. Glc-HSA-induced E-selectin expression was suppressed by the phosphatidylinositol 3 kinase (PI3K) inhibitors wortmannin and LY294002, the protein kinase B (PKB) inhibitor ML-9, the IkappaB kinase (IKK) inhibitor BAY117082, and the Jun N-terminal kinase (JNK) inhibitor SP600125, On the other hand, the protein kinase C inhibitors calphostin C and H-7 did not suppress Glc-HSA-induced E-selectin expression.
CONCLUSION: Glc-HSA induces activation of NADPH oxidase, PKB-IKK and JNK, then E-selectin gene transcription is upregulated by nuclear-translocated NF-kappaB and AP-1.

This article was published in Clin Chim Acta and referenced in Journal of Integrative Oncology

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