Species Restriction of a Monoclonal Antibody Reacting with Residues 130 to 137 in Encephalitogenic Myelin Basic Protein

Sires, L. R.; Hruby, Sarka; Alvord, Ellsworth C.; Hellström, Ingegerd; Hellström, Karl Erik; Kies, Marian W.; Martenson, Russell E.; Deibler, Gladys E.; Beckman, Eric; Casnellie, John E.

doi:10.1126/science.6169147

Cited by 52 publications

(24 citation statements)

References 16 publications

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“…To compare the staining of IN-1 to that of certain myelin specific markers, adjacent sections were stained with IN-1 and mAbs against MBP, MOG and MAG (Sires et al, 1981;Linington et al, 1984;Poltorak et al, 1987). mAbs against MBP, MOG and MAG (Fig.…”

Section: Resultsmentioning

confidence: 99%

A monoclonal antibody (IN-1) which neutralizes neurite growth inhibitory proteins in the rat CNS recognizes antigens localized in CNS myelin

Rubin

Dusart

1994

J Neurocytol

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In previous studies two neurite growth inhibiting protein fractions of 35 and 250 kDa were identified in myelin preparations of the rat CNS. These activities were not found in the myelin of PNS. A monoclonal antibody (mAb IN-1) was raised against the 250 kDa protein fraction and selected for its ability to neutralize the inhibitory effect of CNS myelin and of both isolated protein fractions. IN-1 has been shown both in vitro and in vivo to neutralize the inhibitory effect of differentiated oligodendrocytes and CNS white matter. In the present study, the antigens of IN-1 were localized by immunohistochemistry on cryostat sections of the adult rat nervous system. The staining pattern of IN-1 was compared to that of mAbs specific for proteins found in CNS and PNS myelin. These proteins include myelin basic protein, myelin oligodendrocyte glycoprotein, and myelin associated glycoprotein. IN-1 stained white matter and myelinated fibre tracts in the CNS on sections of fresh frozen tissue fixed with 95% ethanol: 5% acetic acid (Clark's solution). Sciatic nerve myelin and spinal roots remained unstained. The staining pattern of IN-1 corresponded most closely to that of a mAb against myelin oligodendrocyte glycoprotein, a protein which occurs exclusively in CNS myelin and on differentiated oligodendrocytes.

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Section: Resultsmentioning

confidence: 99%

A monoclonal antibody (IN-1) which neutralizes neurite growth inhibitory proteins in the rat CNS recognizes antigens localized in CNS myelin

Rubin

Dusart

1994

J Neurocytol

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“…Further support for a central role of MBP is provided by the observation that immunization with MBP leads directly to the clinical and pathological condition of EAE, an in vivo model of MS [212,213]. MBP is not, however, the only potential myelin antigen, as similar arguments have been designed for the proteolipid protein [214] and lipid components (e.g.,gangliosides) [215] of myelin.…”

Section: D) Periaxinmentioning

confidence: 97%

Structure and Function of the Myelin Proteins: Current Status and Perspectives in Relation to Multiple Sclerosis

Tzakos¹,

Kursula²,

Troganis³

et al. 2005

CMC

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Multiple sclerosis (MS) is a chronic inflammatory disease of the central nervous system (CNS) characterized by demyelination and loss of neurological function, local macrophage infiltrate and neuroantigenspecific CD4 + T cells. MS arises from complex interactions between genetic, immunological, infective and biochemical mechanisms. Although the circumstances of MS etiology remain hypothetical, one persistent theme involves immune system recognition of myelin-specific antigens derived from myelin basic protein, the most abundant extrinsic myelin membrane protein, and/or another equally suitable myelin protein or lipid. Knowledge of the biochemical and physico-chemical properties of myelin proteins and lipids, particularly their composition, organization, structure and accessibility with respect to the compacted myelin multilayers, becomes central to understanding how and why myelin-specific antigens become selected during the development of MS. This review focuses on the current understanding of the molecular basis of MS with emphasis: (i) on the physical-chemical properties, organization, morphology, and accessibility of the proteins and lipids within the myelin multilayers; (ii) on the structure-function relationships and characterization of the myelin proteins relevant to the manifestation and evolution of MS; (iii) on conformational relationships between myelin epitopes which might become selected during the development of MS; (iv) on the structure of MHC/HLA in complex with MBP peptides as well as with TCR, which is crucial to the understanding of the pathogenesis of MS with the ultimate goal of designed antigen-specific treatments.

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“…The MBPs of oligodendrocytes were detected by the enhanced luminol reaction using Renaissance (Dupont NEN, Boston, MA). From the immunological aspect, the MBP monoclonal antibody (Sires et al [1981] Science 214:87–89) was revealed to recognize MBPs with molecular masses of 21.5 kDa and 18.5 kDa. Furthermore, we found that Ile‐166 in the rat 18.5‐kDa MBP isomers was replaced by methionine.…”

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confidence: 99%

Study of expression of myelin basic proteins (MBPs) in developing rat brain using a novel antibody reacting with four major isoforms of MBP

Akiyama

Ichinose

Omori

et al. 2002

J of Neuroscience Research

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Myelin basic proteins (MBPs) are the major protein components of myelin. MBP isoforms are known to have different expression patterns. In order to distinguish the different expression patterns on myelination, we have developed a novel antibody reacting with the four major isoforms of MBPs with molecular masses of 21.5 kDa, 18.5 kDa, 17.0 kDa, and 14.0 kDa. These MBPs were initially separated by acid urea gel and sodium dodecyl sulfate polyacrylamide gel electrophoreses and detected with the luminol reaction. Then the antibody developed was used to determine the relative amounts of MBP isoforms. The MBPs of oligodendrocytes were detected by the enhanced luminol reaction using Renaissance (Dupont NEN, Boston, MA). From the immunological aspect, the MBP monoclonal antibody (Sires et al. [1981] Science 214:87-89) was revealed to recognize MBPs with molecular masses of 21.5 kDa and 18.5 kDa. Furthermore, we found that Ile-166 in the rat 18.5-kDa MBP isomers was replaced by methionine. The 14.0-kDa and 18.5-kDa isoforms of MBP are the most abundant MBP species and comprise more than 70% of the total MBPs in 3.5-and 24-month-old rats. MBPs are expressed during development and the compositions of MBPs in mature (3.5 months old) and aged (24 months old) rats were almost the same. The expression of the 14.0-kDa and 18.5-kDa MBPs occurred earlier in the cerebellum and the spinal cord than in the cerebrum by approximately 1 week. MBPs are also expressed upon oligodendrocyte maturation by interacting with astrocytes. The above results suggest that the regulation of MBP isoforms during development and oligodendrocyte differentiation may indicate the point of occurrence of both the unique patterns of isoform expression and the shift in intracellular localization of MBPs with the maturation of oligodendrocytes.

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Species Restriction of a Monoclonal Antibody Reacting with Residues 130 to 137 in Encephalitogenic Myelin Basic Protein

Cited by 52 publications

References 16 publications

A monoclonal antibody (IN-1) which neutralizes neurite growth inhibitory proteins in the rat CNS recognizes antigens localized in CNS myelin

A monoclonal antibody (IN-1) which neutralizes neurite growth inhibitory proteins in the rat CNS recognizes antigens localized in CNS myelin

Structure and Function of the Myelin Proteins: Current Status and Perspectives in Relation to Multiple Sclerosis

Study of expression of myelin basic proteins (MBPs) in developing rat brain using a novel antibody reacting with four major isoforms of MBP

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