The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Immunocytochemical observations on the distribution of myelin‐associated glycoprotein and myelin basic protein in multiple sclerosis lesions
Abstract
To study the distribution of myelin‐associated glycoprotein (MAG) in human nervous tissue and in multiple sclerosis (MS) lesions, we used paraffin sections and our modification of the peroxidase‐antiperoxidase technique. Sections of MS lesions also were treated with antiserum to basic protein (BP) and with histological stains for axons and myelin sheaths. In tissue from normal developing central nervous system, oligodendroglia, their processes, and newly formed myelin sheaths were intensely stained by MAG antiserum. In adults, MAG was found in periaxonal regions of myelinated fibers of the central and peripheral nervous system. The most striking finding in MS lesions was the extension of decreased MAG immunostaining into white matter that appeared normal when treated with BP antiserum or luxol fast blue. In acute early MS lesions the decrease in MAG immunostaining extended far beyond the margin of acute demyelination, where the BP staining of degenerating sheaths often was increased. In chronic inactive plaques, this decrease in periaxonal MAG immunostaining was limited to relatively few fibers in a thin rim around each lesion. These observations suggest that in MS, immunoreactivity of periaxonal MAG is altered before myelin breakdown begins. Early in degeneration, myelin sheaths and their fragments often were more intensely stained by BP antiserum than normal sheaths; later the staining intensity decreased. In shadow plaques, BP antiserum stained some oligodendroglia. Their appearance and location among thinly myelinated axons suggested that these oligondendroglia were forming new sheaths around previously demyelinated axons.
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Sternberger, N. H., Itoyama, Y., Kies, M. W., & Webster, H. D. (1978) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.75.5.2521 · Cited by 270
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Cited by
Oligodendrocytes: biology and pathology
Bradl, M., & Lassmann, H. (2010) · Acta Neuropathologica · doi:10.1007/s00401-009-0601-5 · Cited by 933
Subpial Demyelination in the Cerebral Cortex of Multiple Sclerosis Patients
Bø, L., Vedeler, C. A., Nyland, H. I., Trapp, B. D., & Mørk, S. J. (2003) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/62.7.723 · Cited by 757
Distinct Patterns of Multiple Sclerosis Pathology Indicates Heterogeneity in Pathogenesis
Lucchinetti, C. F., Brück, W., Rodriguez, M., & Lassmann, H. (1996) · Brain Pathology · doi:10.1111/j.1750-3639.1996.tb00854.x · Cited by 733
Loss of aquaporin 4 in lesions of neuromyelitis optica: distinction from multiple sclerosis
Misu, T., Fujihara, K., Kakita, A., Konno, H., Nakamura, M., Watanabe, S., Takahashi, T., Nakashima, I., Takahashi, H., & Itoyama, Y. (2007) · Brain · doi:10.1093/brain/awm047 · Cited by 614
Self-citationThe J1 glycoprotein—a novel nervous system cell adhesion molecule of the L2/HNK-1 family
Kruse, J., Keilhauer, G., Faissner, A., Timpl, R., & Schachner, M. (1985) · Nature · doi:10.1038/316146a0 · Cited by 584
Metadata
- Authors
- Itoyama, Y., Sterhberger, N. H., Webster, H. D., Quarles, R. H., Cohen, S. R., & Richardson, E. P.
- Venue
- Annals of Neurology
- Publisher
- Wiley
- Published
- 1980-02
- Volume
- 7
- Issue
- 2
- Pages
- 167-177
- ISSN
- 0364-5134 (ISSN-L)
- 1531-8249
- OpenAlex
- W2110662341
- Cited by
- 241
- References
- 1
- FWCI
- 15.04
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Immunocytochemical observations on the distribution of myelin‐associated glycoprotein and myelin basic protein in multiple sclerosis lesions. https://app.cochat.ai/papers/10.1002/ana.410070212
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- Itoyama, Y., Sterhberger, N. H., Webster, H. D., Quarles, R. H., Cohen, S. R., & Richardson, E. P. (1980). Immunocytochemical observations on the distribution of myelin‐associated glycoprotein and myelin basic protein in multiple sclerosis lesions. Annals of Neurology. https://doi.org/10.1002/ana.410070212
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