Localization of a Basic Protein in the Myelin of Various Species With the Aid of Fluorescence and Electron Microscopy

Kornguth, Steven; Anderson, John W.

doi:10.1083/jcb.26.1.157

Cited by 51 publications

(22 citation statements)

References 14 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: 96%

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: 96%

Localization of basic proteins in human myelin

McLaurin

Ackerley

Moscarello

1993

J of Neuroscience Research

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“…MBP was shown to be inaccessible to anti MBP antibodies unless the membrane was disrupted by mechanical or chemical means (Korngurth and Anderson 1965;Herndon et aI., 1973;Guarnieri et ai., 1974;Sternberg et al, 1978;Om lin et al, 1982). Labelling of intact cat spinal cord suggested that MBP was inaccessible to chemical labelling reagents (Poduslo and Braun 1975;Golds and Braun, 1978) from which the authors concluded that MBP was at the MOL, corresponding to the cytoplasmic surfaces of the oligodendrocyte.…”

Section: Localization Of Mbpmentioning

confidence: 98%

Myelin Basic Protein, the “Executive” Molecule of the Myelin Membrane

Moscarello

1997

Cell Biology and Pathology of Myelin

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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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Localization of a Basic Protein in the Myelin of Various Species With the Aid of Fluorescence and Electron Microscopy

Cited by 51 publications

References 14 publications

Localization of basic proteins in human myelin

Localization of basic proteins in human myelin

Myelin Basic Protein, the “Executive” Molecule of the Myelin Membrane

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

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