Vascular Biology |
From the Centre de Recherches Biomédical des Cordeliers, Université Pierre et Marie Curie, Paris, France.
Correspondence to Dr Khadija El Hadri, Centre de Recherches Biomédical des Cordeliers, Université Pierre et Marie Curie, UMR 7079 CNRS, 15 rue de lEcole de Médecine, 75270 Paris Cedex 06, France. E-mail Khadija.El-Hadri{at}bhdc.jussieu.fr
Cultured vascular smooth muscle cells (VSMCs) derived from rat aortic media were used to examine semicarbazide-sensitive amine oxidase (SSAO) expression during their differentiation process. In a defined serum-free medium permissive for in vitro VSMC differentiation, there was a large increase in SSAO mRNA and protein levels and in the related enzyme activity during the course of cell culture. This pattern of expression was concomitant with that of some smooth musclespecific mRNA markers of differentiation. mRNAs in differentiated cultured VSMCs were comparable to those detected in total aorta and media. Pharmacological properties of SSAO present in VSMCs were similar to enzyme activities previously described in the aortic wall. In this model, we also demonstrated that methylamine, a physiological substrate of SSAO, activated 2-deoxyglucose transport in a time- and dose-dependent manner. This methylamine effect was reproduced by other SSAO substrates and was prevented by the SSAO inhibitor semicarbazide. It was antagonized in the presence of catalase, suggesting that SSAO-activated glucose transport was mediated through H2O2 production. In addition, methylamine promoted glucose transporter 1 accumulation at the cell surface. Thus, we demonstrate for the first time the differentiation-dependent expression of SSAO in VSMCs and its role in the regulation of VSMC glucose uptake.
Key Words: semicarbazide-sensitive amine oxidase smooth muscle cells differentiation hydrogen peroxide glucose transport
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