Antigenic regions for the humoral response to myelin basic protein

Whitaker, John N.; Chou, C H; Chou, Fch; Kibler, Robert F.

doi:10.1016/0161-5890(79)90076-2

Cited by 24 publications

(3 citation statements)

References 27 publications

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“…Tigyi et al (1984) reported the production of a monoclonal antibody to bovine MBP that was suggested to cross-react between residues 119 and 160 of human MBP. Our success in obtaining antibodies to more N-terminal regions of the molecule may be due to the fact that new determinants become accessible after cleavage of the whole MBP molecule (Whitaker et al, 1979;Fritz and Chou, 1983).…”

Section: Discussionmentioning

confidence: 99%

“…The major encephalitogenic sites of MBP responsible for the cellular response in experimental allergic encephalomyelitis have been defined (Eylar, 1973). There is less information available regarding the antigenic determinants of the MBP molecule (Driscoll et al, 1974;Whitaker et al, 1979). The use of monoclonal antibodies has enabled the localization of some of the epitopes (Sires et al, 1981;Carnegie et al, 1983;Fritz and Chou, 1983;Tigyi et al, 1984).…”

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confidence: 99%

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Rat and Mouse Monoclonal Antibodies to Human Myelin Basic Protein

Elfman

Kynoch

Siddle

et al. 1986

Journal of Neurochemistry

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BALB/c mice and Lewis rats were immunized with human myelin basic protein and its N- and C-terminal fragments. Mouse X mouse fusions produced seven monoclonal antibodies, all of the IgG class and directed against the N-terminal fragment. Five of the antibodies seemed to be against the same epitope, between amino acid residues 92 and 118. One antibody bound between residues 45 and 91, and the remaining antibody reacted with both peptides 1-44 and 45-91. Three monoclonal antibodies, all of the IgM class, were obtained by rat X rat hybridization. Two monoclonal antibodies, raised against whole myelin basic protein and the C-terminal fragment, respectively, each bound to peptide 118-178. The remaining antibody, raised against the N-terminal fragment, bound to peptide 45-91. These monoclonal antibodies are of interest for use in clinical radioimmunoassays and for immunohistochemical investigation of the structural relationships of the myelin sheath.

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Rat and Mouse Monoclonal Antibodies to Human Myelin Basic Protein

Elfman

Kynoch

Siddle

et al. 1986

Journal of Neurochemistry

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“…One aspect drawing special attention in various experimental models of autoimmunity was the identification of the autoimmunogenic molecule and the epitopes responsible for the induction of antibodies and/or autoreactive cells (1)(2)(3)(4).…”

Section: Introductionmentioning

confidence: 99%

Humoral Autoimmune Response to Rat Male Accessory Glands. Comparative Specificity Studies of Auto and Heteroantibodies

Pistoresi-Palencia

Pesoa

Galmarini

et al. 1986

JJMSB

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P₂, P₁, and P₀ myelin protein expression in developing rat sixth nerve: A quantitative immunocytochemical study

Hahn

Whitaker

Kachar

et al. 1987

J of Comparative Neurology

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Myelination and the expression of myelin proteins P2, P1, and P0 were studied quantitatively in the rat sixth cranial nerve during development. The postnatal development and growth of all myelin sheaths in this nerve have been studied morphometrically in a companion paper. Epon-embedded blocks with closely matched topography in the transverse plane were selected from rats perfused at ages 1-4, 8, 15, and 20 days. From each block, serial semithin sections were cut, etched, and immunostained according to the peroxidase-antiperoxidase method with well-characterized polyclonal antisera that reacted specifically with P0 glycoprotein and the basic proteins P1 and P2. The immunoreactivities of individual myelin sheaths were measured by densitometry. Numbers of compact myelin lamellae, myelin spiral lengths, and axon diameters were determined on electronmicrographs of adjacent thin sections. At birth anti-P0 immunoreactivity was found on sheaths with two and more compact lamellae; neither P1 nor P2 immunoreactivity was observed. On day 2, myelin sheaths with five and eight lamellae were stained respectively by anti-P1 and anti-P2. On day 3 the percentages of myelin sheaths stained were substantially higher: P0 95%, P1 78%, P2 15%. By day 4, anti-P0 and anti-P1 immunoreactivity was present in 95% of myelin sheaths; 35% were stained by anti-P2. For P2, staining intensity and percentage of myelin sheaths stained continued to increase and by day 20, 85% were anti-P2-positive. The density of immunoreactivity was not uniform in all myelin sheaths. At young ages staining varied with all three proteins. The variability decreased as myelin sheaths thickened; it persisted longest for anti-P2. We conclude that the density and distribution of immunoreactivities of P0, P1, and P2 reflect their relative concentrations during myelin sheath development and growth. We attribute lack of detectable anti-P2 immunoreactivity in some small sheaths at 20 days to their early stage of myelination and also to limitations of the method. We infer from our observations that all myelin-forming Schwann cells express P2 basic protein.

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Antigenic regions for the humoral response to myelin basic protein

Cited by 24 publications

References 27 publications

Rat and Mouse Monoclonal Antibodies to Human Myelin Basic Protein

Rat and Mouse Monoclonal Antibodies to Human Myelin Basic Protein

Humoral Autoimmune Response to Rat Male Accessory Glands. Comparative Specificity Studies of Auto and Heteroantibodies

P₂, P₁, and P₀ myelin protein expression in developing rat sixth nerve: A quantitative immunocytochemical study

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Antigenic regions for the humoral response to myelin basic protein

Cited by 24 publications

References 27 publications

Rat and Mouse Monoclonal Antibodies to Human Myelin Basic Protein

Rat and Mouse Monoclonal Antibodies to Human Myelin Basic Protein

Humoral Autoimmune Response to Rat Male Accessory Glands. Comparative Specificity Studies of Auto and Heteroantibodies

P2, P1, and P0 myelin protein expression in developing rat sixth nerve: A quantitative immunocytochemical study

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P₂, P₁, and P₀ myelin protein expression in developing rat sixth nerve: A quantitative immunocytochemical study