Ionic strength and calcium regulate membrane interactions of myelin basic protein and the cytoplasmic domain of myelin protein zero
نویسندگان
چکیده
منابع مشابه
Serum and Saliva Myelin Basic Protein as Multiple Sclerosis Biomarker
Objective: Multiple sclerosis (MS) is presented with motor and sensory function loss. It is caused by demyelination and following axonal lesion. As myelin basic protein (MBP) is one of the key elements of the myelin cover, we examined the level of MBP in serum, stimulated, and unstimulated saliva as a suitable biomarker for detecting MS. Methods: A case-control study was performed in 29 health...
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The surface forces apparatus and atomic force microscope were used to study the effects of lipid composition and concentrations of myelin basic protein (MBP) on the structure of model lipid bilayers, as well as the interaction forces and adhesion between them. The lipid bilayers had a lipid composition characteristic of the cytoplasmic leaflets of myelin from "normal" (healthy) and "disease-lik...
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Multiple sclerosis (MS) is an inflammatory disease of the central nervous system of presumed autoimmune etiology. One of the best animal models of demyelinating diseases is experimental autoimmune encephalomyelitis (EAE), which can be induced in a variety of animals by injection of a target antigen such as myelin basic protein (MBP). The immune responses against the target amino acids caus...
متن کاملDesigning, Optimization and Construction of Myelin Basic Protein Coding Sequence Binding to the Immunogenic Subunit of Cholera Toxin
Abstract Background and Objectives: Multiple sclerosis (MS) is a chronic inflammatory autoimmune disease. Mucosal feeding of myelin basic protein binding to the cholera toxin B subunit can reduce the intensity of the immune response in MS patients. Expression system, the domain composition of the fusion protein, accessibility of two domains, codon adaptation index (CAI) and GC contents are v...
متن کاملThe cytoplasmic domain of the myelin P0 protein influences the adhesive interactions of its extracellular domain
The extracellular domain of the myelin P0 protein is believed to engage in adhesive interactions and thus hold the myelin membrane compact. We have previously shown that P0 can behave as a homophilic adhesion molecule through interactions of its extracellular domains (Filbin, M. T., F. S. Walsh, B. D. Trapp, J. A. Pizzey, and G. I. Tennekoon. 1990. Nature (Lond.) 344:871-872). To determine if t...
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ژورنال
عنوان ژورنال: Biochemical and Biophysical Research Communications
سال: 2019
ISSN: 0006-291X
DOI: 10.1016/j.bbrc.2019.02.025