tailieunhanh - Báo cáo khoa học: Human metallothioneins 2 and 3 differentially affect amyloid-beta binding by transthyretin

Transthyretin (TTR), an amyloid-beta (Ab) scavenger protein, and metallo-thioneins 2 and 3 (MT2 and MT3), low molecular weight metal-binding proteins, have recognized impacts in Abmetabolism. Because TTR binds MT2, an ubiquitous isoform of the MTs, we investigated whether it also interacts with MT3, an isoform of the MTs predominantly expressed in the brain, and studied the role of MT2 and MT3 in human TTR–Abbinding. | Human metallothioneins 2 and 3 differentially affect amyloid-beta binding by transthyretin Ana Martinho1 Isabel Goncalves1 Isabel Cardoso2 Maria R. Almeida2 3 Telma Quintela1 Maria J. Saraiva2 3 and Cecilia R. A. Santos1 1 Health Sciences Research Centre CICS University of Beira Interior Covilhã Portugal 2 Molecular Neurobiology IBMC Celland Molecular Biology Institute Porto Portugal 3 ICBAS Institute of BiomedicalSciences AbelSalazar University of Porto Porto Portugal Keywords amyloid-beta metallothionein 2 metallothionein 3 protein interactions transthyretin Correspondence C. R. A. Santos Health Sciences Research Centre CICS University of Beira Interior Avenida Infante Dom Henrique 6200-506 Covilha Portugal Fax 351 275329099 Tel 351 275329048 E-mail csantos@ Received 25 February 2010 revised 9 June 2010 accepted 24 June 2010 doi Transthyretin TTR an amyloid-beta Ab scavenger protein and metallo-thioneins 2 and 3 MT2 and MT3 low molecular weight metal-binding proteins have recognized impacts in Ab metabolism. Because TTR binds MT2 an ubiquitous isoform of the MTs we investigated whether it also interacts with MT3 an isoform of the MTs predominantly expressed in the brain and studied the role of MT2 and MT3 in human TTR-Ab binding. The TTR-MT3 interaction was characterized by yeast two-hybrid assays saturation-binding assays co-immunolocalization and co-immunoprecipitation. The effect of MT2 and MT3 on TTR-Ab binding was assessed by competition-binding assays. The results obtained clearly demonstrate that TTR interacts with MT3 with a Kd of nM. Competition-binding assays demonstrated that MT2 diminishes TTR-Ab binding whereas MT3 has the opposite effect. In addition to identifying a novel ligand for TTR that improves human TTR-Ab binding the present study highlights the need to clarify whether the effects of MT2 and MT3 in human TTR-Ab binding observed in vitro have a relevant impact on Ab deposition in .

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