Myelin Basic Protein inhibits the calcium response to phytohaemagglutinin in human lymphocytes

1990 ◽  
Vol 10 (1) ◽  
pp. 55-59
Author(s):  
Tiziana Bellini ◽  
Diana Degani ◽  
Maurizio Matteuzzi ◽  
Franco Dallocchio
Keyword(s):  
Myelin Basic Protein ◽  
Protein Concentration ◽  
Basic Protein ◽  
Human Lymphocytes ◽  
Cytosolic Calcium ◽  
Free Calcium ◽  
Cellular Activation ◽  
The Central Nervous System ◽  
Pre Treatment ◽  
Preincubation Time

Myelin Basic Protein, one of the major membrane protein component of the central nervous system, was used to probe the molecular mechanism of cellular activation by phytohaemagglutinin. Pre-treatment of human lymphocytes with myelin basic protein results in a lower rising of cytosolic concentration of free calcium after stimulation with phytohaemagglutinin. This effect is dependent on myelin basic protein concentration and on the preincubation time of the protein with the cells. It is not due to a interaction between myelin basic protein and phytohaemagglutinin, but appears to be a consequence of the binding of the protein to the cell surface. The reduction of the rise of cytosolic calcium induced by phytohaemagglutinin is specific for the myelin basic protein because other proteins like albumin and protamine have no effect.

Effect of 17 β-estradiol on calcium response to phytohaemagglutinin in human lymphocytes

1990 ◽  
Vol 10 (1) ◽  
pp. 73-78 ◽  
Author(s):  
Tiziana Bellini ◽  
Diana Degani ◽  
Maurizio Matteuzzi ◽  
Franco Dallocchio
Keyword(s):  
Cell Surface ◽  
Steroid Hormones ◽  
Human Lymphocytes ◽  
Cytosolic Calcium ◽  
Free Calcium ◽  
Cytosolic Free Calcium ◽  
Calcium Response ◽  
Pre Treatment ◽  
Preincubation Time ◽  
Estradiol Concentration

Pre-treatment of human lymphocytes with 17 β-estradiol diminishes the increase in concentration of cytosolic free calcium after stimulation with phytohaemagglutinin. The effect is dependent on 17 β-estradiol concentration and on the preincubation time. The effect is not due to an interaction between 17 β-estradiol and phytohaemagglutinin, but appears to be a consequence of the binding of the hormone to the cell surface. The effect is specific for 17 β-estradiol, since the α isomer and other steroid hormones (progesterone, testosterone, diethylstilbestrol and 5α-androstan), have no effect. Since the effect of the 17 β-estradiol can be suppressed by treatment of lymphocytes with ouabain, it appears that the effect of estradiol on the rise of cytosolic calcium induced by phytohaemagglutinin is mediated by the (Na, K)-ATPase.

scholarly journals Fuzzy complexes of myelin basic protein: NMR spectroscopic investigations of a polymorphic organizational linker of the central nervous systemThis paper is one of a selection of papers published in this special issue entitled “Canadian Society of Biochemistry, Molecular & Cellular Biology 52nd Annual Meeting — Protein Folding: Principles and Diseases” and has undergone the Journal's usual peer review process.

2010 ◽  
Vol 88 (2) ◽  
pp. 143-155 ◽  
Author(s):  
David S. Libich ◽  
Mumdooh A.M. Ahmed ◽  
Ligang Zhong ◽  
Vladimir V. Bamm ◽  
Vladimir Ladizhansky ◽  
...  
Keyword(s):  
Solid State ◽  
Myelin Basic Protein ◽  
Solid State Nmr ◽  
Basic Protein ◽  
Peer Review Process ◽  
Protein Nmr ◽  
Spectroscopic Studies ◽  
Intrinsically Disordered ◽  
The Central Nervous System ◽  
Structural Homeostasis

The classic 18.5 kDa isoform of myelin basic protein (MBP) is central to maintaining the structural homeostasis of the myelin sheath of the central nervous system. It is an intrinsically disordered, promiscuous, multifunctional, peripheral membrane protein, whose conformation adapts to its particular environment. Its study requires the selective and complementary application of diverse approaches, of which solution and solid-state NMR spectroscopy are the most powerful to elucidate site-specific features. We review here several recent solution and solid-state NMR spectroscopic studies of 18.5 kDa MBP, and the induced partial disorder-to-order transitions that it has been demonstrated to undergo when complexed with calmodulin, actin, and phospholipid membranes.

scholarly journals Vaccination with DNA Encoding an Immunodominant Myelin Basic Protein Peptide Targeted to Fc of Immunoglobulin G Suppresses Experimental Autoimmune Encephalomyelitis

1998 ◽  
Vol 187 (9) ◽  
pp. 1543-1548 ◽  
Author(s):  
Anna Lobell ◽  
Robert Weissert ◽  
Maria K. Storch ◽  
Cecilia Svanholm ◽  
Katrien L. de Graaf ◽  
...  
Keyword(s):  
Autoimmune Disease ◽  
Experimental Autoimmune Encephalomyelitis ◽  
Myelin Basic Protein ◽  
Basic Protein ◽  
Cell Epitope ◽  
Interferon Γ ◽  
Dna Encoding ◽  
Autoimmune Encephalomyelitis ◽  
The Central Nervous System ◽  
Experimental Autoimmune

We explore here if vaccination with DNA encoding an autoantigenic peptide can suppress autoimmune disease. For this purpose we used experimental autoimmune encephalomyelitis (EAE), which is an autoaggressive disease in the central nervous system and an animal model for multiple sclerosis. Lewis rats were vaccinated with DNA encoding an encephalitogenic T cell epitope, guinea pig myelin basic protein peptide 68–85 (MBP68–85), before induction of EAE with MBP68–85 in complete Freund's adjuvant. Compared to vaccination with a control DNA construct, the vaccination suppressed clinical and histopathological signs of EAE, and reduced the interferon γ production after challenge with MBP68–85. Targeting of the gene product to Fc of IgG was essential for this effect. There were no signs of a Th2 cytokine bias. Our data suggest that DNA vaccines encoding autoantigenic peptides may be useful tools in controlling autoimmune disease.

Oligoclonal IgGs against DNA, Histones, and Myelin Basic Protein in the Cerebrospinal Fluid of Patients with Multiple Sclerosis

2021 ◽  
Vol 7 (1) ◽  
Author(s):  
Kostrikina IA ◽  
◽  
Granieri E ◽  
Nevinsky GA ◽  
◽  
...  
Keyword(s):  
Multiple Sclerosis ◽  
Cerebrospinal Fluid ◽  
Myelin Basic Protein ◽  
Basic Protein ◽  
Main Role ◽  
Barr Virus ◽  
The Central Nervous System ◽  
Epstein Barr ◽  
Ms Pathogenesis ◽  
Myelin Proteolipid

Multiple Sclerosis (MS) is known as a chronic demyelinating pathology of the central nervous system. The most accepted MS pathogenesis theory assigns the main role to demyelination of myelin-proteolipid shells due to inflammationrelated with autoimmune reactions. One of the features of MS patients is the enhanced synthesis of oligoclonal IgGs in the bone marrow Cerebrospinal Fluid (CSF). By antigen-specific immunoblotting after isoelectrofocusing of IgGs, oligoclonal IgGs in CSF of MS patients were revealed only against the components of Epstein-Barr virus and Chlamydia. However, there was still unknown to which human auto-antigens in MS patients oligoclonal IgGs may be produced. Here it was first shown that in the CSF of a narrow percentage of MS patients, oligoclonal IgGs are produced against their own antigens: DNA (24% patients), histones (20%), and myelin basic protein (12%). At the same time, the CSF of MS patients contains a very large amount of auto-IgGs-abzymes that hydrolyze DNA, histones, and myelin basic protein, which during isofocusing, are distributed throughout the gel from pH 3 to 10. It is concluded that these multiple IgGs-abzymes, which are dangerous to humans since stimulate development of MS, in the main are non-oligoclonal antibodies.

scholarly journals Translation of myelin basic protein mRNA in oligodendrocytes is regulated by integrin activation and hnRNP-K

2011 ◽  
Vol 192 (5) ◽  
pp. 797-811 ◽  
Author(s):  
Lisbeth S. Laursen ◽  
Colin W. Chan ◽  
Charles ffrench-Constant
Keyword(s):  
Protein Synthesis ◽  
Myelin Basic Protein ◽  
Myelin Sheath ◽  
Basic Protein ◽  
Inhibitory Effect ◽  
Integrin Activation ◽  
Hnrnp K ◽  
Sheath Formation ◽  
The Central Nervous System ◽  
Mrna Binding

Myelination in the central nervous system provides a unique example of how cells establish asymmetry. The myelinating cell, the oligodendrocyte, extends processes to and wraps multiple axons of different diameter, keeping the number of wraps proportional to the axon diameter. Local regulation of protein synthesis represents one mechanism used to control the different requirements for myelin sheath at each axo–glia interaction. Prior work has established that β1-integrins are involved in the axoglial interactions that initiate myelination. Here, we show that integrin activation regulates translation of a key sheath protein, myelin basic protein (MBP), by reversing the inhibitory effect of the mRNA 3′UTR. During oligodendrocyte differentiation and myelination α6β1-integrin interacts with hnRNP-K, an mRNA-binding protein, which binds to MBP mRNA and translocates from the nucleus to the myelin sheath. Furthermore, knockdown of hnRNP-K inhibits MBP protein synthesis during myelination. Together, these results identify a novel pathway by which axoglial adhesion molecules coordinate MBP synthesis with myelin sheath formation.

scholarly journals Hericium erinaceus mycelium and its small bioactive compounds promote oligodendrocyte maturation with an increase in myelin basic protein

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Hui-Ting Huang ◽  
Chia-Hsin Ho ◽  
Hsin-Yu Sung ◽  
Li-Ya Lee ◽  
Wan-Ping Chen ◽  
...  
Keyword(s):  
Myelin Basic Protein ◽  
Bioactive Compounds ◽  
Basic Protein ◽  
Ex Vivo ◽  
Neurological Diseases ◽  
Neonatal Rat ◽  
Tissue Slices ◽  
Rat Pups ◽  
The Central Nervous System ◽  
Cerebellar Tissue

AbstractOligodendrocytes (OLs), myelin-producing glia in the central nervous system (CNS), produce a myelin extension that enwraps axons to facilitate action potential propagation. An effective approach to induce oligodendrogenesis and myelination is important to foster CNS development and promote myelin repair in neurological diseases. Hericium (H.) erinaceus, an edible and culinary-medicinal mushroom, has been characterized as having neuroprotective activities. However, its effect on OL differentiation has not yet been uncovered. In this study using oligodendrocyte precursor cell (OPC) cultures and an ex vivo cerebellar slice system, we found that the extract from H. erinaceus mycelium (HEM) not only promoted the differentiation of OPCs to OLs in the differentiation medium, but also increased the level of myelin basic protein (MBP) on neuronal fibers. Moreover, daily oral administration of HEM into neonatal rat pups for 7 days enhanced MBP expression and OLs in the corpus callosum of the postnatal rat brain. The effect of HEM-derived bioactive compounds, the diterpenoid xylosides erinacine A (HeA) and HeC and a sesterterpene with 5 isoprene units called HeS, were further evaluated. The results showed that HeA and HeS more potently stimulated MBP expression in OLs and increased the number of OLs. Moreover, overlap between MBP immunoreactivity and neuronal fibers in cultured cerebellar tissue slices was significantly increased in the presence of HeA and HeS. In summary, our findings indicate that HEM extract and its ingredients HeA and HeS display promising functional effects and promote OL maturation, providing insights into their potential for myelination in neurodevelopmental disorders.

scholarly journals Evidence For The Involvement of B Cells and Antibody in The Pathogenesis of Multiple Sclerosis in Immunized Mouse With Recombinant Myelin Basic Protein Peptide

2021 ◽  
Author(s):  
Maryam Sahlolbei ◽  
Maryam Hajizadeh ◽  
Marzie Naseri ◽  
Hossein Ghanbarian ◽  
Seyed Mahmoud Hashemi ◽  
...  
Keyword(s):  
Multiple Sclerosis ◽  
Nervous System ◽  
B Cells ◽  
Myelin Basic Protein ◽  
Plasma Cells ◽  
Basic Protein ◽  
Mice Model ◽  
Nerve Lesions ◽  
Autoreactive B Cells ◽  
The Central Nervous System

Abstract Over the years, regarding great progresses in knowledge of immunology and neuroscience, the treatment of multiple sclerosis (MS) has been changed. The earlier strategies were focused mainly on T lymphocytes as pioneer cells responsible to inflammatory damage in the central nervous system lesions, whereas B cells, plasma cells and antibodies are also found in the active nerve lesions in MS patients. Despite the accumulating evidence, the role of Myelin basic protein (MBP) antibodies in progression of lesions in nervous system is not completely clear yet. In this regard, here, we present data on B cells and antibody level after MBP immunization of MS mice model. Recombinant fusion protein harboring Myelin basic protein peptide (amino acids 83–99) and CFP was produced in E. coli and purified with chromatography. Then, the C57BL / 6 mice were immunized by rMBP-CFP. Antibody-based assay was used to quantify the level of reactivity to the MBP in mice serum. Subsequently, humoral immunity was analyzed by immunohistochemistry (IHC), ELISA, and Flow cytometry. Our data indicated an increase in autoreactive B cells and MBP specific antibodies after immunization. IHC analysis revealed an increasing penetration rate of immune cells and the nerve lesions development in the nervous system following increasing in MBP antibody titers.This study represented data to support this idea that reactive B cells and antibodies to MBP may contribute to MS pathogenesis. Hence, targeting of these autoreactive B cells and antibodies can be used as potential tools in treatment of MS patients.

scholarly journals Enzymic hydrolysis of myelin basic protein and other proteins in central nervous system and lymphoid tissues from normal and demyelinating rats

1976 ◽  
Vol 156 (3) ◽  
pp. 627-633 ◽  
Author(s):  
G F Buletza ◽  
M E Smith
Keyword(s):  
Spinal Cord ◽  
Central Nervous System ◽  
Nervous System ◽  
Myelin Basic Protein ◽  
Proteolytic Activity ◽  
Experimental Allergic Encephalomyelitis ◽  
Basic Protein ◽  
Allergic Encephalomyelitis ◽  
The Central Nervous System ◽  
Experimental Allergic

Proteolytic activity of central-nervous-system tissue of the normal rat was examined over the pH range 2-9 with casein, haemoglobin and myelin basic protein as substrates. With casein as a substrate, brain and spinal cord homogenates showed very similar activity profiles with increasing pH, with the main peaks of proteolytic activity at pH 3-4 and 5-6. When haemoglobin was used, one broad main peak of activity from pH 3 to 5 was demonstrated. There was no optimum pH, however, for proteolytic activity with myelin basic protein as a substrate, and considerable hydrolysis were observed from pH 3.5 up to pH8. Proteolytic activity at the various pH values was compared by using homogenates of spinal cords from rats with acute experimental allergic encephalomyelitis and those from rats injected with Freund's adjuvant alone. The profiles of activity were similar with peaks at pH 3.5 and 5.5 with casein as a substrate, but the specific activity was significantly higher at most pH values in the spinal-cord homogenates from rats with experimental allergic encephalomyelitis. Similarly the spinal-cord homogenates from these latter rats contained much more proteolytic activity toward myelin basic protein throughout the pH range than was present in the control spinal cords. Homogenates from lymph nodes of rats with experimental allergic encephalomyelitis and from those of the controls contained two to three times as much proteolytic activity as that of the central-nervous-system tissue and had a different proteolytic activity profile form that of the central-nervous system, with higher activity at the neutral than at acid pH. The results are discussed with regard to the probability that inflammatory cells such as lymphocytes may be the cause of the increased proteolytic activity in the central nervous system of animals with experimental allergic encephalomyelitis, and that enzymes from these cells possess the capability of digesting myelin basic protein.

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