Parkinson's disease (PD) is one of the most common neurodegenerative disorders. Several toxin-induced animals models simulate the motor deficits occurring in PD. Among them, the unilateral 6-hydroxydopamine (6-OHDA) model is frequently used in rats and has the advantage of presenting side-biased motor impairments. However, the behavioral consequences of a unilateral 6-OHDA-lesion have, so far, not been described in detail in mice. The aim of this study was to characterize mice with unilateral 6-OHDA-lesions placed in the median forebrain bundle using several motor behavioral tests in order to identify the most suitable predictor of nigral cell loss. Mice underwent various drug-induced (amphetamine- and apomorphine-induced rotation) and spontaneous motor tests (cylinder, rotarod, elevated body swing, and stride length test). The amphetamine-induced rotation test, the cylinder and the rotarod test were most sensitive and reliable in detecting loss of tyrosine hydroxylase-immunoreactive cells in the substantia nigra. This study demonstrates that substantial and stable unilateral 6-OHDA-induced lesions can be established in mice, and that these lesions can be functionally assessed using several different side-bias-based behavioral tests. This mouse model offers the opportunity to use transgenic mouse strains and study the interactions between genes of interest and toxins in relation to Parkinson's disease etiology in the future.

Summary.  Background: Factor H regulates the alternative pathway of complement. The protein has three heparin‐binding sites, is synthesized primarily in the liver and copurifies from platelets with thrombospondin‐1. Factor H mutations at the C‐terminus are associated with atypical hemolytic uremic syndrome, a condition in which platelets are consumed. Objectives The aim of this study was to investigate if factor H interacts with platelets. Methods: Binding of factor H, recombinant C‐ or N‐terminus constructs and a C‐terminus mutant to washed (plasma and complement‐free) platelets was analyzed by flow cytometry. Binding of factor H and constructs to thrombospondin‐1 was measured by surface plasmon resonance. Results: Factor H bound to platelets in a dose‐dependent manner. The major binding site was localized to the C‐terminus. The interaction was partially blocked by heparin. Inhibition with anti‐GPIIb/IIIa, or with fibrinogen, suggested that the platelet GPIIb/IIIa receptor is involved in factor H binding. Factor H binds to thrombospondin‐1. Addition of thrombospondin‐1 increased factor H binding to platelets. Factor H mutated at the C‐terminus also bound to platelets, albeit to a significantly lesser degree. Conclusions: This study reports a novel property of factor H, i.e. binding to platelets, either directly via the GPIIb/IIIa receptor or indirectly via thrombospondin‐1, in the absence of complement. Binding to platelets was mostly mediated by the C‐terminal region of factor H and factor H mutated at the C‐terminus exhibited reduced binding.