Publications by authors named "Bernard Laurent Schneider"
Accumulation and misfolding of the alpha-synuclein protein are core mechanisms in the pathogenesis of Parkinson's disease. While the normal function of alpha-synuclein is mainly related to the control of vesicular neurotransmission, its pathogenic effects are linked to various cellular functions, which include mitochondrial activity, as well as proteasome and autophagic degradation of proteins. Remarkably, these functions are also affected when the renewal of macromolecules and organelles becomes impaired during the normal aging process.
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- α-Synuclein (α-syn) is a presynaptic protein linked to Parkinson's disease, where its overexpression in the substantia nigra causes motor impairments primarily associated with the wild-type form.
- Increased wild-type α-syn leads to reduced dopamine release in the striatum and changes at the ultrastructural level, such as fewer dopaminergic vesicles and synaptic contacts, despite some loss of dopaminergic neurons.
- The membrane-binding capabilities of α-syn are crucial, as mutant forms lacking these properties do not significantly impact dopamine release or motor function, highlighting the relationship between α-syn's structure and its effects on neurotransmission.
The present study investigates the respective roles of both the host immune response and the metabolic requirements in determining the long-term survival of erythropoietin-secreting myoblasts within encapsulating polymer membranes. Hollow-fiber capsules loaded with a high density of erythropoietin-secreting C(2)C(12) myoblasts survived poorly in the subcutaneous tissue of syngeneic mice, inducing variable hematocrit responses. To determine the role and the nature of the host response, recipients were treated with anti-inflammatory (diclofenac) and immunosuppressive (dexamethasone, FK506) agents.
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