myelin-basic-protein and Neuritis

myelin-basic-protein has been researched along with Neuritis* in 28 studies

Reviews

2 review(s) available for myelin-basic-protein and Neuritis

ArticleYear
Guillain-Barre syndrome and allergic neuritis: is the P2 protein a common denominator.
    Progress in clinical and biological research, 1980, Volume: 39

    Topics: Amino Acid Sequence; Amino Acids; Animals; Antigens; Chemical Phenomena; Chemistry; Demyelinating Diseases; Humans; Myelin Basic Protein; Neuritis; Peripheral Nervous System Diseases; Polyradiculoneuropathy; Sciatic Nerve

1980
[Myelin proteins and demyelinating disease (author's transl)].
    Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme, 1974, Oct-01, Volume: 19, Issue:11

    Topics: Amino Acid Sequence; Binding Sites; Electrophoresis, Disc; Encephalomyelitis, Autoimmune, Experimental; Myelin Basic Protein; Myelin Sheath; Nerve Endings; Neuritis; Protein Conformation

1974

Trials

1 trial(s) available for myelin-basic-protein and Neuritis

ArticleYear
Antibodies against the myelin oligodendrocyte glycoprotein and the myelin basic protein in multiple sclerosis and other neurological diseases: a comparative study.
    Brain : a journal of neurology, 1999, Volume: 122 ( Pt 11)

    In experimental animal models of multiple sclerosis demyelinating antibody responses are directed against the myelin oligodendrocyte glycoprotein (MOG). We have investigated whether a similar antibody response is also present in multiple sclerosis patients. Using the recombinant human extracellular immunoglobulin domain of MOG (MOG-Ig) we have screened the sera and CSFs of 130 multiple sclerosis patients, 32 patients with other inflammatory neurological diseases (OIND), 30 patients with other non-inflammatory neurological diseases (ONND) and 10 patients with rheumatoid arthritis. We report that 38% of multiple sclerosis patients are seropositive for IgG antibodies to MOG-Ig compared with 28% seropositive for anti-myelin basic protein (MBP). In contrast, OIND are characterized by similar frequencies of serum IgG antibody responses to MOG-Ig (53%) and MBP (47%), whereas serum IgG responses to MOG-Ig are rare in ONND (3%) and rheumatoid arthritis (10%). Anti-MBP IgG antibodies, however, are a frequent finding in ONND (23%) and rheumatoid arthritis (60%). Our results provide clear evidence that anti-MOG-Ig antibodies are common in CNS inflammation. However, in OIND these antibody responses are transient, whereas they persist in multiple sclerosis. We demonstrate that the serum anti-MOG-Ig response is already established in early multiple sclerosis (multiple sclerosis-R0; 36%). In later multiple sclerosis stages frequencies and titres are comparable with early multiple sclerosis. In contrast, the frequency of anti-MBP antibodies is low in multiple sclerosis-R0 (12%) and increases during disease progression in relapsing-remitting (32%) and chronic progressive multiple sclerosis (40%), thus suggesting that anti-MBP responses accumulate over time. Finally we provide evidence for intrathecal synthesis of IgG antibodies to MOG-Ig in multiple sclerosis.

    Topics: Adult; Arthritis, Rheumatoid; Autoantibodies; Blotting, Western; Enzyme-Linked Immunosorbent Assay; Female; Humans; Immunoglobulins; Male; Middle Aged; Multiple Sclerosis; Myelin Basic Protein; Myelin Proteins; Myelin-Associated Glycoprotein; Myelin-Oligodendrocyte Glycoprotein; Nervous System Diseases; Neuritis; Recombinant Proteins; Retrospective Studies

1999

Other Studies

25 other study(ies) available for myelin-basic-protein and Neuritis

ArticleYear
White matter injury in young and aged rats after intracerebral hemorrhage.
    Experimental neurology, 2008, Volume: 214, Issue:2

    Experimental studies of intracerebral hemorrhage (ICH) have focused on neuron death, with little or no information on axonal and myelin damage outside the hematoma. Because development of effective therapies will require an understanding of white matter injury, we examined white matter injury and its spatial and temporal relationship with microglial/macrophage activation in a collagenase model of rat striatal ICH. The hematoma and parenchyma surrounding the hematoma were assessed in young and aged animals at 6 h, 1, 3 and 28 days after ICH onset. Demyelination occurred inside and at the edge of the hematoma; regions where we have shown substantial neuron death. In contrast, there was axonal damage without demyelination at the edge of the hematoma, and by 3 days this damage had spread to the surrounding parenchyma, a region where we have shown there is no neuron death. Because the axonal damage preceded infiltration of activated microglia into the white matter tracts (seen at 3 days), our results support the hypothesis that these cells respond to, rather than perpetrate the damage. Importantly, axonal damage was worse in aged animals, which provides a plausible explanation for the poorer functional recovery of older animals after ICH, despite a similar loss of grey matter. Our findings support strategies that target white matter injury to reduce neurological impairment after ICH.

    Topics: Age Factors; Aging; Amyloid beta-Protein Precursor; Animals; Brain Injuries; Cerebral Hemorrhage; Demyelinating Diseases; Disease Models, Animal; Male; Microglia; Myelin Basic Protein; Nerve Fibers, Myelinated; Neuritis; Rats; Rats, Sprague-Dawley; Stroke

2008
An immunohistochemical, clinical and electroneuromyographic correlative study of the neural markers in the neuritic form of leprosy.
    Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologicas, 2006, Volume: 39, Issue:8

    The nerve biopsies of 11 patients with pure neuritic leprosy were submitted to routine diagnostic procedures and immunoperoxidase staining with antibodies against axonal (neurofilament, nerve growth factor receptor (NGFr), and protein gene product (PGP) 9.5) and Schwann cell (myelin basic protein, S-100 protein, and NGFr) markers. Two pairs of non-adjacent histological cross-sections of the peripheral nerve were removed for quantification. All the fascicles of the nerve were examined with a 10X-ocular and 40X-objective lens. The immunohistochemistry results were compared to the results of semithin section analysis and clinical and electroneuromyographic data. Neurofilament staining was reduced in 100% of the neuritic biopsies. NGFr positivity was also reduced in 81.8%, PGP staining in 100% of the affected nerves, S100 positivity in 90.9%, and myelin basic protein immunoreactivity in 90.9%. Hypoesthesia was associated with decreased NGFr (81.8%) and PGP staining (90.9%). Reduced potential amplitudes (electroneuromyographic data) were found to be associated with reduced PGP 9.5 (63.6%) and nerve fiber neurofilament staining (45.4%) by immunohistochemistry and with loss of myelinated fibers (100%) by semithin section analysis. On the other hand, the small fibers (immunoreactive dots) seen amid inflammatory cells continued to be present even after 40% of the larger myelinated fibers had disappeared. The present study shows an in-depth view of the destructive effects of leprosy upon the expression of neural markers and the integrity of nerve fiber. The association of these structural changes with the clinical and electroneuromyographic manifestations of leprosy peripheral neuropathy was also discussed.

    Topics: Adult; Antigens, Bacterial; Biomarkers; Biopsy; DNA, Bacterial; Electromyography; Female; Glycolipids; Humans; Immunoenzyme Techniques; Immunohistochemistry; Leprosy; Male; Mycobacterium leprae; Myelin Basic Protein; Nerve Fibers, Myelinated; Nerve Tissue Proteins; Neuritis; Neurofilament Proteins; Polymerase Chain Reaction; Receptors, Nerve Growth Factor; S100 Proteins

2006
Differential recognition of MBP epitopes in BALB/c mice determines the site of inflammatory disease induction.
    Journal of neuroimmunology, 1998, Aug-14, Volume: 89, Issue:1-2

    Although myelin basic protein (MBP)-recognizing T cells are not readily obtained after immunization of BALB/c mice with MBP (reflecting the BALB/c resistance to actively induced experimental autoimmune encephalomyelitis (EAE)), they can be expanded and cloned after several rounds of in vitro culture. The majority of BALB/c-derived clones recognize an epitope defined by MBP peptide 59-76. When transferred to naive BALB/c recipients, these clones cause classical EAE, with characteristic inflammation and demyelination of the central nervous system (CNS). We previously showed that two related clones recognizing a minor epitope, defined by MBP peptide 151-168, cause inflammation and demyelination preferentially of the peripheral nervous system (PNS). Because MBP has alternatively spliced isoforms, residues 151-168 are not present contiguously in all MBP isoforms. In order to determine whether induction of PNS disease is idiosyncratic to these sister clones, or related to their properties of epitope recognition, an independent T-cell line with similar recognition properties was studied. Clone 116F, derived from a BALB/c shiverer mouse, expresses a different T-cell receptor (TCR), with distinct TCR contact residues, but like the previously described T cells, this clone requires residues from both exons 6 and 7 for optimal stimulation. When adoptively transferred to BALB/c recipients, this clone preferentially induces disease of the PNS. A control BALB/c shiverer-derived MBP 59-76-recognizing clone, in contrast, induces CNS disease. These data strongly suggest that the site of disease initiation may correlate with epitope recognition, particularly when alternative isoforms are involved.

    Topics: Alternative Splicing; Amino Acid Substitution; Animals; Antibody Specificity; Clone Cells; Cloning, Molecular; Demyelinating Diseases; Epitopes; Exons; Female; Mice; Mice, Inbred BALB C; Mice, Neurologic Mutants; Molecular Sequence Data; Myelin Basic Protein; Neuritis; Peptide Fragments; Peripheral Nervous System; Receptors, Antigen, T-Cell; T-Lymphocytes

1998
In vitro synthesis of antibodies to myelin antigens by Epstein-Barr virus-transformed B lymphocytes from patients with neurologic disorders.
    Journal of the neurological sciences, 1991, Volume: 104, Issue:1

    Anti-myelin antibodies can be found in sera from patients with neurologic disorders of suspected immune-mediated pathogenesis such as multiple sclerosis and inflammatory polyneuropathies. However, the specificity of these findings is controversial. In the present study, in vitro synthesis of antibodies to myelin components was compared to their presence in sera in diverse neurological disorders. Epstein-Barr virus was used to activate B lymphocytes for in vitro antibody production. Anti-myelin basic protein and anti-galactocerebroside antibodies were secreted in vitro by B lymphocytes derived from patients with neurological disorders of various etiologies and pathogenetic mechanisms. Anti-myelin basic protein antibodies were detected in many more cell culture supernatants than in sera from the same patients. In vitro secretion of antibodies to myelin antigens, as well as the presence of these antibodies in body fluids, are apparently non-specific for disease type and may be secondary to neural tissue damage.

    Topics: Aged; Aged, 80 and over; Antibody Formation; Antigens, Viral; B-Lymphocytes; Branchial Region; Facial Paralysis; Female; Galactosylceramides; Herpesvirus 4, Human; Humans; Lymphocyte Activation; Male; Myasthenia Gravis; Myelin Basic Protein; Myelin Sheath; Nervous System Diseases; Neuritis; Radioimmunoassay

1991
Peripheral nerve demyelination in rabbits after inoculation with Freund's complete adjuvant alone or in combination with lipid haptens.
    Journal of neuroimmunology, 1987, Volume: 16, Issue:3

    The pathology of demyelination in rabbits with experimental allergic neuritis (EAN) or galactocerebroside-induced neuritis was compared to that in rabbits inoculated with either an emulsion of lipid haptens (gangliosides, lecithin and cholesterol) and Freund's complete adjuvant or Freund's complete adjuvant (FCA) alone. In rabbits inoculated with bovine peripheral myelin in FCA, perivenular demyelination associated with infiltrates of lymphocytes and macrophages occurred after 30 days, while those animals inoculated with galactocerebroside (GC) in Freund's adjuvant did not develop lesions until 60-90 days. GC rabbits had demyelination and severe nerve edema without cellular infiltrates. In rabbits inoculated with FCA alone, demyelination was restricted to ganglia and proximal nerve roots. Myelin basic protein (MBP) and GC antibodies from EAN, GC and lipid hapten-inoculated rabbits were detected by ELISA in sera at all post-inoculation time points. Appreciable P0 and P2 antibody titers were detected only in EAN animals. The results indicate that Freund's complete adjuvant alone or in combination with lipid haptens is capable of producing neuropathic effects in the rabbit independent of those produced by EAN or galactocerebroside neuritis.

    Topics: Animals; Antibodies; Demyelinating Diseases; Female; Freund's Adjuvant; Galactosylceramides; Haptens; Lipids; Myelin Basic Protein; Myelin Sheath; Neuritis; Peripheral Nerves; Rabbits

1987
Use of an ELISA in the differential diagnosis of cauda equina neuritis and other equine neuropathies.
    Equine veterinary journal, 1987, Volume: 19, Issue:1

    In 27 potential neuropathies an enzyme-linked immunosorbent assay, using P2 preparations from either bovine or equine myelin, detected all cases of cauda equina neuritis in which there was caudal involvement. The test was of limited value in differentiating neuropathies involving only cranial or other peripheral nerves.

    Topics: Animals; Cauda Equina; Chromatography, High Pressure Liquid; Diagnosis, Differential; Electrophoresis, Polyacrylamide Gel; Enzyme-Linked Immunosorbent Assay; Female; Horse Diseases; Horses; Male; Myelin Basic Protein; Myelin P2 Protein; Neuritis; Peripheral Nervous System Diseases

1987
Cause and prevention of postinfectious and postvaccinal neuropathies in light of a new theory of autoimmunity.
    Lancet (London, England), 1986, Aug-02, Volume: 2, Issue:8501

    Topics: Adjuvants, Immunologic; Animals; Antigens; Autoimmune Diseases; Disease Models, Animal; Humans; Infections; Myelin Basic Protein; Myelin P2 Protein; Neuritis; Vaccines

1986
Sequence homology between certain viral proteins and proteins related to encephalomyelitis and neuritis.
    Science (New York, N.Y.), 1985, Jul-19, Volume: 229, Issue:4710

    Post-infectious or post-vaccinal demyelinating encephalomyelitis and neuritis may be due to immunological cross-reactions evoked by specific viral antigenic determinants (epitopes) that are homologous to regions in the target myelins of the central and peripheral nervous systems. Such homologies have been found by computer searches in which decapeptides in two human myelin proteins were compared with proteins of viruses known to infect humans. These viruses include measles, Epstein-Barr, influenza A and B, and others that cause upper respiratory infections. Several regions identified in myelin basic protein and P2 protein can be related to experimental allergic encephalomyelitis or neuritis in laboratory animals.

    Topics: Animals; Base Sequence; Chickens; Encephalomyelitis; Epitopes; Guinea Pigs; Haplorhini; Humans; Measles; Myelin Basic Protein; Myelin P2 Protein; Neuritis; Rabbits; Rats; Rats, Inbred Lew; Viral Proteins; Viral Vaccines

1985
Spontaneous and experimental neuritis and the distribution of the myelin protein P2 in the nervous system.
    Journal of neurochemistry, 1984, Volume: 42, Issue:1

    The P2 contents of nervous tissues from the human, rabbit, guinea pig, and Lewis rat were measured by radioimmunoassay. The ventral spinal roots contained more P2 than any other tissue. Human dorsal roots and peripheral nerves contained 41-65% of the amount in human ventral roots. Human olfactory and optic nerves and brain contained 1.1-2.7%, spinal cord, 2.8%, cranial nerve VIII, 11%, and cerebral grey matter, 0%. The relative amounts in the rabbit nervous system were similar except that the spinal cord contained 20% of the amount in the ventral roots. Qualitative estimates in the guinea pig showed that the spinal roots and peripheral nerves contained more P2 than the spinal cord, and that none was present in the brain. In the Lewis rat, P2 could be detected in the spinal roots and peripheral nerves but not in the CNS. The distribution of P2 in the human nervous system parallels the incidence and severity of lesions in acute polyradiculoneuritis. It also explains the absence of any lesions in the CNS when experimental allergic neuritis is induced in the Lewis rat.

    Topics: Animals; Guinea Pigs; Humans; Liver; Myelin Basic Protein; Myelin P2 Protein; Nervous System; Neuritis; Neuritis, Autoimmune, Experimental; Rabbits; Radioimmunoassay; Rats; Species Specificity; Tissue Distribution

1984
Susceptibility and resistance to experimental autoimmune encephalomyelitis and neuritis in the guinea pig correlate with the induction of procoagulant and anticoagulant activities.
    Journal of immunology (Baltimore, Md. : 1950), 1984, Volume: 133, Issue:6

    Activation of macrophage procoagulant activity (MPCA) is involved in the manifestation of EAE and EAN in susceptible guinea pigs and provides a mechanism for the deposition of fibrin, which is a feature of histologic lesions of EAE. Peritoneal exudate cells (PEC) from susceptible (strain 13) guinea pigs immunized with either central or peripheral nervous tissue antigens produce procoagulant activity when incubated with the immunogen in vitro. The production of the procoagulant is quantitative and antigen-specific and is maximal at the time of clinical signs of the disease. After recovery, the production of procoagulant activity decreased. The MPCA test was able to discriminate the biochemical differences existing between chicken and mammalian peripheral nerve proteins, thus providing a quantitative and sensitive indicator of cell-mediated immunity in EAE and EAN. The autoimmune response to brain and nerve antigens in nonsusceptible (strain 2) guinea pigs was coincident with the antigen-specific production of a cell-bound anticoagulant activity by stimulated mononuclear cells. The production of anticoagulant activity followed the same sequence of time changes after immunization as that of the MPCA in susceptible guinea pigs, and high immunizing doses of nerve antigens induced high levels of anticoagulant activity. The same cells produced high levels of procoagulant when incubated with tuberculin or lipopolysaccharide. The recalcification time of normal plasma was prolonged by the anticoagulant, and the decreased clotting time of plasma induced by the procoagulant activity obtained by incubating sensitized strain 13 PEC with myelin basic protein was suppressed by the anticoagulant produced by culturing sensitized strain 2 PEC with myelin basic protein. Preliminary evidence indicates that the anticoagulant has properties similar to antithrombin III. The anticoagulant could play a role in the control of effector cell function, and therefore in recovery from clinical features of EAE and EAN in susceptible guinea pigs.

    Topics: Animals; Ascitic Fluid; Autoimmune Diseases; Blood Coagulation; Disease Susceptibility; Encephalomyelitis, Autoimmune, Experimental; Female; Guinea Pigs; Immunity, Innate; Male; Myelin Basic Protein; Nerve Tissue Proteins; Neuritis; Neutralization Tests; Protein Precursors; Thioglycolates

1984
[Mutual relationships of inflammatory disorders of the central and peripheral nervous systems. Clinico-immunological observations].
    Casopis lekaru ceskych, 1982, Nov-12, Volume: 121, Issue:45

    Topics: Adult; Child; Encephalitis; Humans; Lymphocyte Activation; Meningitis; Multiple Sclerosis; Myelin Basic Protein; Neuritis; Peripheral Nerves; Tissue Extracts

1982
Allergic neuritis: a neuritogenic peptide from the P2 protein that induces disease in rats.
    Journal of immunology (Baltimore, Md. : 1950), 1981, Volume: 126, Issue:3

    Peptide CN1, a large 93 residue peptide, derived from residues 21-113 of the bovine and rabbit P2 protein of sciatic nerve myelin, induces severe allergic neuritis in Lewis rats. When complexed with phosphatidylserine and tested at 50 microgram dosage in Freund's complete adjuvant, it induces severe clinical and histologic signs (cellular infiltration and demyelination of the sciatic nerve) in most animals. It is as potent in disease induction as the P2 protein on a weight basis. In contrast, when not complexed with phosphatidylserine, Peptide CN1 induced only mild clinical signs and histologic lesions in 3 of 10 rats. CNBr peptides CN2 and CN3, derived from the carboxyl and amino terminal ends, respectively, were not active. Spleen and lymph node cells from rats sensitized to Peptide CN1 responded to both P2 and Peptide CN1 in culture in the mitogenic assay. These data show that the major neuritogenic domain for the rat resides in the CN1 region.

    Topics: Animals; Cattle; Hypersensitivity; Lymph Nodes; Mitogens; Myelin Basic Protein; Myelin P2 Protein; Myelin Proteins; Neuritis; Peptide Fragments; Rabbits; Rats; Rats, Inbred Lew; Spleen

1981
Structure of bovine P2 basic protein: sequence of a carboxyterminal segment that is a neuritogen in rabbits.
    Journal of neurochemistry, 1981, Volume: 36, Issue:3

    The sequence of the carboxyterminal 18 amino acids released by cyanogen bromide digestion of the bovine P2 protein was determined. It has several interesting structural and immunological properties. It contains the only two half-cystines in the molecule that have the capacity to form an intrachain disulfide bond. Using the rabbit as a test animal, this carboxyterminal peptide was capable of producing experimental allergic neuritis. The sequence of this peptide is Val-Val-Glu-Cys-Lys-Met-Lys-Asp-Val-Val-Cys-Thr-Arg-Ile-Tyr-Glu-Lys-Val.

    Topics: Amino Acid Sequence; Animals; Cattle; Chemical Phenomena; Chemistry; Myelin Basic Protein; Myelin P2 Protein; Neuritis; Peptide Fragments; Rabbits

1981
Genetic control of susceptibility to experimental allergic neuritis and the immune response to P2 protein.
    Neurology, 1981, Volume: 31, Issue:8

    Topics: Animals; Body Weight; Disease Susceptibility; Female; Hypersensitivity; Immunity, Cellular; Immunization; Lymphocyte Activation; Male; Myelin Basic Protein; Myelin P2 Protein; Neuritis; Rats

1981
Circulating antibodies to the neuritogenic myelin protein, P2, in neuritis of the cauda equina of the horse.
    Nature, 1981, Sep-24, Volume: 293, Issue:5830

    Topics: Animals; Autoantibodies; Autoimmune Diseases; Cattle; Cauda Equina; Female; Horse Diseases; Horses; Male; Myelin Basic Protein; Neuritis

1981
Allergic neuritis: phospholipid requirement for the disease-inducing conformation of the P2 protein.
    Biochimica et biophysica acta, 1981, Jun-29, Volume: 669, Issue:1

    The P2 protein, a small, highly ordered basic protein of peripheral nerve myelin, is a potent inducer of allergic neuritis in rats when complexed with phospholipids such as phosphatidylserine. Isolated P2 protein administered without lipid is a poor neuritogen, and if first oxidized with performic acid, aminoethylated in 8 M urea or heat denatured, it loses nearly all activity. When the aminoethylated or oxidized forms are combined with phosphatidylserine, however, they recover essentially full neuritogenic activity. Complexing with lipid also greatly enhances the activity of the heart denatured form. Spleen cells sensitized to the aminoethylated and heated forms of P2 protein show a pronounced mitogenic response to either of these forms as well as to the P2 protein itself, but only when sensitization is initiated with the lipid complex. These data indicate that the lipid complex reverses the distortion acquired by chemical treatment or denaturation and converts the P2 molecule into a conformation approximating that of the native P2 protein in myelin. These studies imply that the neuritogenic domain, while highly sensitive to denaturing conditions, requires interaction with phospholipids in order to attain the most favourable conformation for inducing a cell-mediated response that leads to disease.

    Topics: Animals; Antigens; Autoimmune Diseases; Immunochemistry; In Vitro Techniques; Lymphocyte Activation; Myelin Basic Protein; Myelin P2 Protein; Neuritis; Phosphatidylserines; Phospholipids; Protein Conformation; Rabbits; Rats

1981
Experimental allergic neuritis in the Lewis rat: characterization of the activity of peripheral myelin and its major basic protein,P2.
    Brain research, 1980, Feb-24, Volume: 184, Issue:2

    Experimental allergic neuritis has been produced in the inbred Lewis rat in the absence of experimental allergic encephalomyelitis (EAE) using bovine intradural root myelin. The lack of EAE is probably because P1 is only weakly encephalitogenic in the rat. One of the basic proteins of bovine peripheral myelin, P2, was isolated and demonstrated to be pure by amino acid analysis and SDS PAGE. It was found to have a molecular weight of 15,400 and contained 4 mol 1/2-cystine/mol. This P2 was found to be highly neuritogenic and is probably the sole neuritogenic antigen in this system. The successful demonstration of its neuritogenicity must be due in large part to the use of the inbred Lewis rat and bovine P2, but an explanation could also involve the omission of denaturing organic solvents, the prevention of oxidative denaturation and presumably the fact that any changes which may occur are not sufficient to prevent recognition of the active site by the immune system of the inbred Lewis rat. P2 was neuritogenic down to 5 micrograms/animal. Its activity was enhanced by but not dependent on the presence of Mycobacterium in the adjuvant. This suggested that release of P2 could possibly break tolerance and produce an auto-immune disease such as the Guillain--Barre syndrome.

    Topics: Amino Acids; Animals; Autoimmune Diseases; Cattle; Electrophoresis, Polyacrylamide Gel; Male; Molecular Weight; Myelin Basic Protein; Myelin Sheath; Neuritis; Rats; Rats, Inbred Lew

1980
The neuritogenicity and encephalitogenicity of P2 in the rat, guinea-pig and rabbit.
    Journal of the neurological sciences, 1980, Volume: 48, Issue:2

    In inbred Lewis rats, P2 basic protein from bovine peripheral nervous system (PNS) myelin produced experimental allergic neuritis (EAN) without involvement of the brain or spinal cord. In guinea-pigs, bovine P2 did not produce EAN but large doses produced mild experimental allergic encephalomyelitis (EAE). In rabbits, bovine P2 produced both mild EAE and EAN. Human P2 produced severe EAN in the Lewis rat, but only mild EAN with quite marked EAE in the guinea-pig. Material cross-reacting with bovine P on immunodiffusion was identified in the extracts from the nerves of all three species but only in the spinal cord of the guinea-pig and rabbit, not in the rat spinal cord. The species differences in response to immunisation with P2 cannot be simply explained by the presence or absence of P2 in their PNS or CNS, but may reflect differences in the immune response.

    Topics: Animals; Antigens; Autoimmune Diseases; Cattle; Demyelinating Diseases; Encephalomyelitis, Autoimmune, Experimental; Guinea Pigs; Humans; Male; Myelin Basic Protein; Neuritis; Rabbits; Rats; Rats, Inbred Lew; Species Specificity; Spinal Nerve Roots

1980
Neuropathological comparative studies on experimental allergic neuritis (EAN) induced in rabbits by P2 protein-ganglioside complexes.
    The Japanese journal of experimental medicine, 1980, Volume: 50, Issue:6

    The light microscopical examinations were performed on the peripheral nerve (PN) lesions in rabbits induced by bovine peripheral nerve (BPN) myelin and by its components. Morphology of the PN lesions induced by P2 protein-ganglioside complex were equivalent to those induced by PN myelin (original EAN); and some of them were more remarkable in severity than the original EAN. The lesions were composed of myelin destruction, numerous macrophages containing myelin debris, completely demyelinated axons and remyelinating fibers. P2-I, acid treated P2-I and P2-II proteins induced PN lesions. Histologically they were moderate to minimal in severity in that order. However, when each protein was injected as the complex with ganglioside, PN lesions obviously became severer, respectively. These findings indicate the possibility that the P2-ganglioside complex may be involved in the chemical principle of EAN, and also the findings strongly support the theory proposed by Nagai et al. that gangliosides may play an essential role in rabbit EAN to give P2 protein a special conformation necessary for antigenic activity.

    Topics: Animals; Autoimmune Diseases; Demyelinating Diseases; Gangliosides; Immunization; Male; Myelin Basic Protein; Myelin P2 Protein; Myelin Proteins; Neuritis; Peripheral Nerves; Rabbits

1980
Suppression of experimental allergic neuritis with P2 protein of PNS myelin.
    Zeitschrift fur Naturforschung. Section C, Biosciences, 1979, Volume: 34, Issue:7-8

    Experimental allergic neuritis was induced in the guinea pig with bovine PNS myelin. Treatment with P2 protein at the onset of the disease markedly reduced the severity of the clinical signs compared with untreated controls and animals treated with CNS myelin basic protein. The mortality was reduced from 94% in the combined control group to 50% in the treated group. Saline was a better vehicle for administration of the suppressive inoculation than incomplete Freund's adjuvant.

    Topics: Animals; Autoimmune Diseases; Cattle; Guinea Pigs; Myelin Basic Protein; Myelin Proteins; Myelin Sheath; Neuritis; Peripheral Nerves

1979
Experimental allergic neuritis induced by a basic neuritogenic protein (P1L) of human peripheral nerve origin.
    European journal of immunology, 1977, Volume: 7, Issue:4

    Experimental allergic neuritis (EAN) in the peripheral nervous system, without involvement of the central nervous system, was produced in laboratory animals by the injection of a basic neuritogenic protein, P1L, purified from human peripheral nerves. The animals manifested a positive skin test with P1L, and their lymphocytes were found to be transformed in vitro in the presence of this protein several days before the appearance of the clinical signs. Passive transfer of the disease was performed with lymph node cells from donor guinea pigs immunized with P1L protein. EAN, the experimental model for the human disease Guillaain-Barré syndrome, was shown to be a transient disease and could be suppressed by the administration of hydrocortisone.

    Topics: Animals; Autoimmune Diseases; Disease Models, Animal; Guinea Pigs; Humans; Hydrocortisone; Immunity, Cellular; Immunization, Passive; Immunosuppression Therapy; Lymphocyte Activation; Myelin Basic Protein; Myelin Proteins; Nerve Tissue Proteins; Neuritis; Polyradiculopathy; Rats; Skin Tests

1977
Neuritogenic and encephalitogenic properties of the peripheral nerve basic proteins.
    Journal of neuropathology and experimental neurology, 1975, Volume: 34, Issue:1

    Two basic proteins, P1 of molecular weight 14,200 and P2 of molecular weight 12,300, purified from bovine peripheral nerve, were assayed for biological activity. The P1 protein is an exclusively neuritogenic agent, capable of producing clinical signs of experimental allergic neuritis (EAN) and histological abnormalities in the peripheral nervous system (PNS) of guinea pigs and rabbits, without any changes in their central nervous system (CNS). P2 protein, like the CNS basic encephalitogenic protein (BE), has combined neuritogenic and encephalitogenic activities, therefore it induces in these animals neurological signs and pathological evidence of EAN, as well as histological characteristics of experimental allergic encephalomyelitis (EAE).

    Topics: Animals; Brain; Cattle; Disease Models, Animal; Encephalomyelitis, Autoimmune, Experimental; Guinea Pigs; Myelin Basic Protein; Nerve Tissue Proteins; Neuritis; Peripheral Nerves; Rabbits; Schwann Cells; Sciatic Nerve; Species Specificity

1975
Anti-synaptic antibody in allergic encephalomyelitis. I. Neurophysiological studies, in guinea pigs, on the exposed cerebral cortex and peripheral nerves, following immunological challenges with myelin and synaptosomes.
    Brain research, 1975, Aug-08, Volume: 93, Issue:2

    The potential evoked at the surface of the cerebral cortex of a guinea pig, by stimulation of the contralateral forepaw, usually consists of an initial double positive wave whose waveform remains unchanged during rapid stimulation. In a guinea pig with experimental allergic encephalomyelitis (EAE) the response is attenuated at low frequencies of stimulation. Observations were also made on animals with experimental allergic neuritis (AEN). These animals showed a peripheral specificity for decreased conduction velocity, but have normal cortical evoked responses. Histological studies were undertaken in parallel with the electrophysiological studies and the concordance and discordance between the two is discussed. We conclude that there is no evident correlation between the severity of the electrophysiological effects and the histological lesions. An attempt was also made to induce an immunological challenge in guinea pigs, in the same way that EAE and EAN is produced, by the injection of synaptosomes. No clinical signs or alterations in the histology or electrophysiology of the animals were seen. A discussion is included on the elucidation of the site of action of EAE by discriminating between the direct effects on myelin and synapses and by the indirect effects of myelin damage on synapses. No firm conclusion is reached and the matter is left for further analysis in the subsequent paper. Finally, the neurophysiological alterations, demonstrated in the EAE and EAN situations, are discussed in terms of a humoral factor possibly acting on the myelin sheath and indirectly affecting synaptic function. This matter is further discussed in the subsequent paper.

    Topics: Animals; Central Nervous System; Cerebral Cortex; Disease Models, Animal; Electric Stimulation; Encephalomyelitis, Autoimmune, Experimental; Evoked Potentials; Fecal Incontinence; Forelimb; Guinea Pigs; Humans; Myelin Basic Protein; Myelin Sheath; Neural Conduction; Neuritis; Paralysis; Rats; Sciatic Nerve; Synaptosomes; Urinary Incontinence

1975
Experimental allergic neuritis: cells binding horseradish peroxidase conjugates of myelin basic proteins.
    Journal of immunology (Baltimore, Md. : 1950), 1974, Volume: 113, Issue:1

    Topics: Animals; Autoimmune Diseases; Cattle; Ganglia, Spinal; Lymph Nodes; Lymphocytes; Lysosomes; Macrophages; Myelin Basic Protein; Myelin Sheath; Neuritis; Peroxidases; Plasma Cells; Rabbits; Sciatic Nerve

1974
Comparative studies on the myelin proteins of bovine peripheral nerve and spinal cord.
    Journal of neurochemistry, 1972, Volume: 19, Issue:11

    Topics: Amino Acids; Animals; Antigens; Cattle; Cerebrosides; Cholesterol; Deoxycholic Acid; Electrophoresis, Disc; Hypersensitivity; In Vitro Techniques; Microscopy, Electron; Myelin Basic Protein; Myelin Sheath; Nerve Tissue Proteins; Neuritis; Nucleotides; Peripheral Nerves; Phospholipids; Phosphoric Diester Hydrolases; Spinal Cord; Spinal Nerve Roots; Surface-Active Agents

1972