| Title | Histamine inhibits advanced glycation end products-induced adhesion molecule expression on human monocytes. | | Author(s) | Wake H, Takahashi HK, Mori S, Liu K, Yoshino T, Nishibori M | | Institution | Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences. | | Source | J Pharmacol Exp Ther 2009 Jun 30. | | Abstract | Advanced glycation end products (AGEs) are modifications of proteins/ lipids that become nonenzymatically glycated after contact with aldose sugars. Among various subtypes of AGEs, glyceraldehyde-derived AGE (AGE-2) and glycolaldehyde-derived AGE (AGE-3) are suggested to play roles in inflammation in diabetic patients. Since the engagement of intercellular adhesion molecule (ICAM)-1, B7.1, B7.2 and CD40 on monocytes with their ligands on T-cells plays roles in cytokine production, we examined the effects of AGE-2 and AGE-3 on the expression of adhesion molecules and cytokine production in human peripheral blood mononuclear cells (PBMC) and their modulation by histamine in the present study. AGE-2 and AGE-3 induced the expressions of ICAM-1, B7.1, B7.2 and CD40 on monocytes and the production of interferon (IFN)-gamma in PBMC. Histamine concentration-dependently inhibited the action of AGE-2 and AGE-3. The effects of histamine were antagonized by an H2-receptor antagonist, famotidine, and mimicked by H2/H4-receptor agonists, dimaprit and 4-methylhistamine. Histamine induced cyclic adenosine monophosphate (cAMP) production in the presence and absence of AGE-2 and AGE-3. The effects of histamine were reversed by a protein kinase A (PKA) inhibitor, H89, and mimicked by a dibutyryl cAMP (dbcAMP) and an adenylate cyclase activator, forskolin. These results as a whole indicated that histamine inhibited the AGE-2- and AGE-3-induced adhesion molecule expression and cytokine production via H2-receptors and the cAMP/PKA pathway. | | Language | ENG | | Pub Type(s) | JOURNAL ARTICLE
| | PubMed ID | 19567778 |
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