They transport organic cations, zwitterions, and some uncharged compounds and operate as facilitated diffusion systems and/or antiporters. The organic cation transporters (OCTs) OCT1, OCT2, OCT3, novel OCT (OCTN)1, OCTN2, multidrug and toxin exclusion (MATE)1, and MATE kidney-specific 2 are polyspecific transporters exhibiting broadly overlapping substrate selectivities. On the basis of these results, we propose that IRIP regulates the activity of a variety of transporters under normal and We measured transport kinetics of OCT2-mediated uptake and demonstrated that IRIP overexpression significantly decreased RNA or antisense RNA increased MPP+ uptake. Conversely, inhibition of IRIP expression by small interfering (OAT1), and monoamine transporters were also inhibited by IRIP. The activities of exogenous organic cation transporters (OCT2 and OCT3), organic anion transporter IRIP overexpression inhibited endogenous 1-methyl-4-phenylpyridinium (MPP+) uptake activity in HeLa cells. Transporter activity was subsequently investigated. Interaction between IRIP and RS1 was further confirmed in coimmunoprecipitation assays. The transporter regulator RS1 was identified as an IRIP-interacting protein in yeast two-hybrid screening. Besides ischemia/reperfusion, endotoxemia also activated the expression of IRIP in the liver, lung,Īnd spleen. Mouse IRIP mRNA was expressed in all tissues tested, the highest level being in the testis, secretory,Īnd endocrine organs. IRIP cDNA was isolated in a differential display analysis of an ischemia/reperfusion-treated We report the identification and characterization of a new ischemia/reperfusion-inducible protein (IRIP), which belongs to
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