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  • 11
    Electronic Resource
    Electronic Resource
    Comment on the note by Z. Lojda and M. Elleder (1971)
    Springer
    Histochemistry and cell biology 28 (1971), S. 229-230 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00305678
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  • 12
    Electronic Resource
    Electronic Resource
    Aldehyde blockade and periodate oxidation (1977)
    Springer
    Journal of molecular histology 9 (1977), S. 787-787 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01003073
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  • 13
    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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  • 14
    Electronic Resource
    Electronic Resource
    Histochemistry of myelin. X. Proteolysis of normal myelin and release of lipid by extracts of degenerating nerve (1970)
    Springer
    Journal of molecular histology 2 (1970), S. 315-321 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Synopsis (1) Anin vitro system is described for studying the effects of homogenized peripheral nerve supernatant on normal central and peripheral myelin. (2) Reduced trypanophilia of normal myelin is attributed to loss of basic trypsin-digestible protein caused by the high activity of proteolytic enzymes in degenerating nerve. (3) Physical changes in myelin lipids, characterized by greatly accelerated myelin-bud formation, occurred in sections treated with degenerating nerve supernatants. (4) These results suggest that the initial stage of myelin breakdown-i.e. before the lipids are chemically degraded-depends on the digestion of basic trypsin-digestible protein in the myelin. Hence, the lipids become dissociated from the protein skeleton of the sheath.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01004999
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  • 15
    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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  • 16
    Electronic Resource
    Electronic Resource
    Histochemistry of myelin. XI. Loss of basic protein in early myelin breakdown and multiple sclerosis plaques (1970)
    Springer
    Journal of molecular histology 2 (1970), S. 323-328 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Synopsis the early stages of Wallerian degeneration in peripheral nerves are accompanied by loss of a trypanophilic, trypsin-digestible basic protein from myelin. This loss of basic protein is ascribed to the activity of proteolytic enzymes. The reduced trypanophilia in degenerating nerves could not be attributed to loss of lipid. Likewise, the tryptophan-rich trypsin-resistant neurokeratin component of peripheral nerve myelin showed no change in the first week of degeneration. Loss of basic protein has been observed in and surrounding plaques of multiple sclerosis. We infer that digestion of basic protein would lead to the release of the encephalitogenic antigen contained therein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01005000
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  • 17
    Electronic Resource
    Electronic Resource
    Bromine-Sudan Black: a general stain for lipids including free cholesterol (1972)
    Springer
    Journal of molecular histology 4 (1972), S. 505-515 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Synopsis Preliminary bromination (with bromine water) increases the intensity of staining of tissue lipids with Sudan Black and certain other dyes. The mechanism appears to be due to the formation of sudanophilic bromo-derivatives of cholesterol and to the retention of certain other lipids, notably phosphatidyl choline and free fatty acids, during staining. The advantage of the bromine-Sudan Black method is that all tissue lipids are stained, except saturated fatty acids, saturated triglycerides and perhaps saturated cholesterol esters. In practice, such lipids rarely, if ever, occur alone, and normally are admixed with their stainable unsaturated counterparts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01011130
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  • 18
    Electronic Resource
    Electronic Resource
    Cholinesterases in peripheral nervous system. III. Validity of localisation around the node of Ranvier (1968)
    Springer
    Journal of molecular histology 1 (1968), S. 68-77 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Synopsis A series of experiments was designed to exclude the possibility that the acetylcholinesterase reaction of the rat's node of Ranvier is artefactual. Copper ions were not bound by perinodal acid mucopolysaccharides (or axons) at pH 6.0, which is the same value as that used in the histochemical cholinesterase techniques. No positive evidence was found for diffusion of acetylcholinesterase out of teased nerve fibres. Likewise, no evidence was obtained that acetylcholinesterase, acetylthiocholine or thiocholine are bound at pH 6.0 by perinodal acid mucopolysaccharides (or axons). It is concluded that local non-specific binding of copper, enzyme, substrate or reaction-product cannot account for the acetylcholinesterase reaction in either the node of Ranvier or the axon.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01054295
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  • 19
    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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  • 20
    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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