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  • 1
    Electronic Resource
    Electronic Resource
    HISTOCHEMISTRY OF MYELIN–XV. CHANGES IN THE MYELIN PROTEINS OF THE PERIPHERAL NERVE UNDERGOING WALLERIAN DEGENERATION–ELECTROPHORETIC AND MICRODENSITOMETRIC OBSERVATIONS (1972)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 19 (1972), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The chronological order of changes in rat peripheral nerve proteins during Wallerian degeneration has been investigated by microdensitometric and electrophoretic techniques. Both methods revealed an early loss of myelin proteins. The histochemical microdensitometric study showed a very substantial early loss of stainable protein basic groups and a somewhat slower progressive loss of the major protein component of peripheral nerve myelin (the J band). The electrophoretic study showed an early loss of both the J band protein and the slower-moving basic protein band. The histochemical study also suggested that some cerebroside may be lost in the early stage of Wallerian degeneration. It is concluded that degradation of myelin proteins is an initial event in the process of myelin breakdown.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1972.tb05114.x
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  • 2
    Electronic Resource
    Electronic Resource
    HISTOCHEMISTRY OF MYELIN XIV PERIPHERAL NERVE MYELIN PROTEINS: ELECTROPHORETIC AND HISTOCHEMICAL CORRELATIONS (1972)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 19 (1972), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— Myelin from the peripheral nervous system has been shown to contain two basic protein components and an electrophoretically slower-moving major protein, the ‘J’ band. The ‘J’ band protein cannot be selectively removed by aqueous or organic solvents and does not correspond to proteolipid or acidic protein. Histochemical stains applied to peripheral nervous systems myelin proteins separated by polyacrylamide electrophoresis indicate that ‘J’ band protein is analogous with the neurokeratin of the nerve sheath. Trypanophilia observed histochemically in unfixed myelin is principally due to basic proteins. With prolonged tryptic digestion ‘J’ band protein is degraded. Thus, previous classifications of myelin proteins based on trypsin sensitivity have been modified. All peripheral nervous system myelin proteins should be regarded as trypsin-sensitive, the basic protein being relatively more and the ‘J’ band protein relatively less susceptible.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1972.tb01481.x
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  • 3
    Electronic Resource
    Electronic Resource
    PROTEOLYTIC ACTIVITY AND BASIC PROTEIN LOSS IN AND AROUND MULTIPLE SCLEROSIS PLAQUES: COMBINED BIOCHEMICAL AND EIISTOCHEMICAL OBSERVATIONS (1972)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 19 (1972), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— This combined histochemical and biochemical study has shown that acid proteinase activity (PH 3.5) is increased around histologically-defined active plaques of multiple sclerosis (MS). Biochemical estimation showed that the enzyme is more active in most samples of ‘normal’ white matter in MS than in controls. A gradient of enzyme activity was observed: control white matter-white matter distant from plaqueclose white matter-edgsplaque. Both electrophoretic and histochemical techniques revealed a reduction or absence of basic (encephalitogenic) protein in the plaques. Electrophoresis showed a diminution of encephalitogenic protein outside some plaques. Phospholipids that remain on the base-line of thin-layer chromatoplates were shown to be predominantly phosphoinositides combined with encephalitogenic protein
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1972.tb01382.x
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  • 4
    Electronic Resource
    Electronic Resource
    HISTOCHEMISTRY OF MYELIN. XIII DIGESTION OF BASIC PROTEIN OUTSIDE ACUTE PLAQUES OF MULTIPLE SCLEROSIS (1971)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 18 (1971), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— Plaques of multiple sclerosis from a patient with a short clinical history were investigated by qualitative and quantitative histochemical methods. One of three plaques examined showed perivenous lymphocytic infiltration; this plaque was regarded as a particularly early acute lesion. In this plaque a relatively wide zone of diminished staining for basic protein extended outwards around the edge of the lesion. A narrower and irregular zone of diminished cerebroside staining was also seen around the plaque. Staining for phosphoglycerides and cholesterol was relatively normal up to the edge of the lesion; no zone of reduced staining for these lipids was seen outside the plaque. Proteolytic activity was increased throughout the lesion (pH 3.5 〉 7.4). The two less acute plaques showed no obvious loss of basic protein and cerebroside outside the plaque. Addendum: Two further acute plaques of multiple sclerosis obtained recently, showed a similar loss of basic protein outside of lesion.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1971.tb00010.x
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  • 5
    Electronic Resource
    Electronic Resource
    HISTOCHEMISTRY OF MYELIN—XII ANIONIC STAINING OF MYELIN BASIC PROTEINS FOR HISTOLOGY, ELECTROPHORESIS AND ELECTRON MICROSCOPY (1971)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 18 (1971), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— Phosphotungstic acid haematoxylin, trypan blue and amidoblack techniques have been developed as anionic dye methods for staining myelin basic proteins. All methods displayed central and peripheral nervous system myelin in histochemical prepa rations and stained brain basic proteins in electrophoretic polyacrylamide gels: phosphotungstic acid haematoxylin appeared to be the most selective of these techniques. Electron photomicrographs of peripheral nerve stained by phosphotungstic acid haematoxylin showed that the major part of myelin basic protein is located in the period dense line. The basic proteins stained by phosphotungstic acid haematoxylin showed an early loss in rat sciatic nerve undergoing Wallerian degeneration and had completely disappeared from the centre of 20 plaques of multiple sclerosis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1971.tb11966.x
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  • 6
    Electronic Resource
    Electronic Resource
    Proteolysis and myelin breakdown: a review of recent histochemical and biochemical studies (1969)
    Springer
    Journal of molecular histology 1 (1969), S. 559-578 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Synopsis Proteins are important constituents of the myelin sheath and serve to maintain its structural integrity. One of the protein components is susceptible to tryptic digestion and may be regarded as a particularly vulnerable part of the myelin sheath. The initial events in myelin breakdown may involve disruption of lipid-protein attachments followed later by chemical degradation of released lipids. In Wallerian degeneration the activity of proteolytic enzymes increases by 12 hr after nerve section. Proteolytic enzyme activity increases in the prodromal phase of diphtheritic neuropathy. Extracts of degenerating nerve cause proteolysis of normal myelin with loss of trypanophilic basic protein and lipid; selective loss of basic protein occurs very early in Wallerian degeneration and has also been found in and around plaques of multiple sclerosis. Proteolytic activity is increased at the edges of ‘active’ multiple sclerosis lesions. It has been shown that the basic encephalitogenic protein is susceptible to digestion by neural proteases, yielding an active encephalitogenic fragment. It is inferred from these collective observations that proteases play an important role in early myelin breakdown and may also be implicated in the pathogenesis of multiple sclerosis plaques by digesting basic protein, by releasing lipid from its attachment to such protein, and by liberating an active encephalitogenic peptide. The factors responsible for the activation and release of proteases remain unknown.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01012862
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  • 7
    Electronic Resource
    Electronic Resource
    Degraded proteolipid in multiple sclerosis plaques-histochemical electrophoretic observations (1975)
    Springer
    Journal of molecular histology 7 (1975), S. 599-604 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Synopsis Electrophoretic analysis of multiple sclerosis plaques has disclosed the presence of a protein band with a mobility approximately the same as myelin proteolipid. The presence of this band was unexpected in view of the virtual absence of myelin from plaques. By application of histochemical staining procedures to electrophoretic ‘micro’ gels it has been shown that this plaque protein does not stain with Sudan Black (for lipid) and dimethylaminobenzaldehyde (for tryptophan) and cannot, therefore, be identified as normal proteolipid. The abnormal band is not associated with glial components or residual myelin within the plaque. We consider that this material might be a degradation product of myelin proteolipid formed during the demyelinating process.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01003797
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  • 8
    Electronic Resource
    Electronic Resource
    Histochemistry of myelin. IX. Neutral and acid proteinases in early Wallerian degeneration (1970)
    Springer
    Journal of molecular histology 2 (1970), S. 209-218 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Synopsis Acid and neutral proteinases, ‘leucine aminopeptidase’ (l-leucyl-β-naphthylamidase) and acid phosphatase were studied in rat sciatic nerves undergoing Wallerian degeneration. Biochemical evidence indicated that increased activity of both proteases and acid phosphatase occurred by 12 hr after nerve section. Histochemical changes in these three enzymes were apparent after three days. Biochemical estimation of neutral ‘leucine aminopeptidase’ (an enzyme predominantly located in myelin in the normal peripheral nerve) showed increased activity near the of the first week of degeneration. During the second week after nerve section all the enzymes studied became markedly more active. The parallel increase in activity of acid proteinase and acid phosphatase and the similarities in their histochemical distribution suggest that the acid proteinase is of lysosomal origin. Such changes in early Wallerian degeneration appear to precede macrophage invasion of the nerve and to arise mainly from the degenerating axon, the Schwann cell, or both. In spite of the delayed increase in ‘leucine aminopeptidase’ it seems possible that some proteinase activity also arises from myelin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01003470
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  • 9
    Electronic Resource
    Electronic Resource
    Histochemistry of myelin. VIII. Proteolytic activity around multiple sclerosis plaques (1970)
    Springer
    Journal of molecular histology 2 (1970), S. 199-208 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Synopsis Twenty-two plaques from six cases of multiple sclerosis were examined histochemically, with particular reference to demonstrating proteolytic activity by the gelatin-silver autogram method. Proteolytic activity was increased around plaques that were characterized as active (i.e. with increased cell population and NADH dehydrogenase activity at their edges). Inactive plaques showed little or no proteolytic activity. Proteolytic activity around active lesions could not be attributed to lipid-laden microglia: oligodendroglia or the myelin sheath are considered as alternative sources. Acid phosphatase and ‘non-specific’ cholinesterase were mainly localized in lipid-laden microglia and the activity of these two enzymes was not otherwise prominent around active plaques. The oligodendroglia from unaffected white matter were found not to contain either of these enzymes. In view of previous observations that proteolytic enzymes causein vitro myelin breakdown and are also implicated in Wallerian degeneration, it is suggested that local proteolysis may be an initiating factor in the demyelinating process of multiple sclerosis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01003469
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  • 10
    Electronic Resource
    Electronic Resource
    The PASDORO method for simultaneously demonstrating DNA and lipids in the brain (1970)
    Springer
    Journal of molecular histology 2 (1970), S. 87-89 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Conclusions and summary The PASDORO method has the advantage of allowing DNA and globular lipid to be demonstrated in frozen sections of formalin-fixed tissue. Its disadvantage is that, in most tissues, basement membrane staining interferes with the selective demonstration of DNA. However, in the central nervous system it is advantageous to be, able to trace capillary basement membrane. In this way cells related to the capillary endothelium can be easily identified. The addition of staining with Oil Red O to the basic PASD technique permits lipid-laden microglia to be readily identified around necrotic and demyelinating lesions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01003457
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