Immuno-Electron Microscopic Localization of the Encephalitogenic Basic Protein in Myelin

Herndon, Robert M.; Rauch, Helene C.; Einstein, Elizabeth Roboz

doi:10.3109/08820137309022789

Cited by 74 publications

(23 citation statements)

References 22 publications

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“…In some reports, MBP has been shown to be inaccessible to anti-MBP antibody unless the membrane is disrupted by mechanical or chemical means (Kornguth and Anderson, 1965; Hern- , 1973;Guarnieri et al, 1974;Sternberger et al, 1978). Labelling of isolated, intact spinal cord from the cat suggested that MBP was inaccessible to the chemical labelling reagents used (Poduslo and Braun, 1975;Golds and Braun, 1976).…”

Section: Discussionmentioning

confidence: 99%

“…Mendell and Whitaker (1978) localized P, (MBP of the PNS) to the IPL in sciatic nerve myelin by immunoelectron microscopy but were unable to localize MBP in the CNS myelin. Other researchers have localized MBP to the major dense line in vitro and in vivo (Herndon et al, 1973;Poduslo and Braun, 1975;Roussel and Nussbaum, 1981), while Omlin and colleagues (Omlin et al, 1982) localized MBP in the CNS and PNS to the MDL. Although some staining at the IPL was observed also, Omlin et al, 1982 regarded this minor staining pattern as non-specific labelling.…”

Section: Introductionmentioning

confidence: 99%

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Localization of basic proteins in human myelin

McLaurin

Ackerley

Moscarello

1993

J of Neuroscience Research

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The myelin basic protein (MBPs) represent a family of proteins (charge isomers) which account for 35% of the total myelin protein. Localization studies have been inconclusive because MBP is not a single protein. Antibodies obtained by injection of MBP into animals recognized all members of the MBP family. In the studies reported here, we have fractionated the MBPs into specific components or charge isomers. One of these which contains citrulline accounts for about 20% of the total MBP. We report the localization of this single MBP to the intraperiod line of myelin by immunoelectron microscopy. For these studies several specific antibodies were used including antibodies raised against total MBP, specific MBP peptides, and against a tetracitrulline peptide. This latter antibody was specific for component 8 (C-8) of MBP. Since C-8 is the only MBP which contains citrulline it was used to localize this particular form of MBP principally to the intraperiod line by immunogold electron microscopy, while antibody against total MBP (consisting of all charge isomers C-1-->C-8) labelled both the major dense line and the intraperiod line. When the anti-citrulline antibody was used with a 3 nm gold conjugated Fab fragments prepared from the secondary antibody, 66.5% of the gold particles were localized to the intraperiod line, while 11.2% of gold particles were localized to the major dense line. On the other hand, with the monoclonal anti-MBP antibodies reactive with residues 69-74, 59.4% of the gold particles were localized to the major dense line and 23.6% of gold particles at the intraperiod line. Other supporting evidence includes increased labelling of myelin by 125I labelled anti-citrulline IgG when isolated myelin was swollen, a process known to take place at the intraperiod line. Gold particles were demonstrated at the intraperiod line in swollen and recompacted myelin. C-8 was shown to associate preferentially with lipids asymmetrically localized to the intraperiod line.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Localization of basic proteins in human myelin

McLaurin

Ackerley

Moscarello

1993

J of Neuroscience Research

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“…MBP represents 5-15 % of PNS myelin protein [118] and is a highly basic extrinsic membrane protein present at the cytoplasmic surfaces of compact myelin membranes [119][120][121][122][123]. The human MBP contains 170 amino acids including 12 lysine, 19 arginine, 2 glutamic acid and 9 aspartic acid residues.…”

Section: D) Myelin Basic Protein (Mbp)mentioning

confidence: 99%

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 use of immunochemical techniques in an attempt to localize the CNS myelin basic protein have provided similar findings, namely, that the basic protein is essentially inaccessible to anti-basic protein antibody in intact myelin and only becomes accessible when the membrane is disrupted (Kornguth and Anderson, 1965;Tomasi and Kornguth, 1968;Herndon et al, 1973;Guarnieri et al, 1974).…”

Section: B Myelin Proteins and Lipid-protein Interactionsmentioning

confidence: 90%

Myelin

1977

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Immuno-Electron Microscopic Localization of the Encephalitogenic Basic Protein in Myelin

Cited by 74 publications

References 22 publications

Localization of basic proteins in human myelin

Localization of basic proteins in human myelin

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

Myelin

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