Rosenthal fibers share epitopes with αB-crystallin, glial fibrillary acidic protein, and ubiquitin, but not with vimentin

Immunoelectron microscopy with colloidal gold

N. Tomokane, Toru Iwaki, J. Tateishi, A. Iwaki, J. E. Goldman

Research output: Contribution to journalArticle

105 Citations (Scopus)

Abstract

Ultrastructural immunoreactivities of αB-crystallin, glial fibrillary acidic protein (GFAP), ubiquitin, and vimentin in Rosenthal fibers (RFs) isolated from an Alexander's disease brain were investigated using nonosmium and low-temperature embedding technique. The morphology of RFs embedded in Lowicryl K4M resin was well preserved after treatment with 0.5% Triton X-100. αB-crystallin immunoreactivity was present in RFs of various sizes and was the strongest in loosely scattered deposits, which were considered to be the initial stage of RFs. Glial fibrillary acidic protein immunoreactivity in RFs was heavy, homogeneous throughout RFs, and equivalent to that in networks of glial filaments. Immunoreactivities of both αB-crystallin and GFAP were mainly restricted to the high electron-dense areas within RFs and were proved to exist close to each other by double immunolabeling. Rosenthal fibers were negative for vimentin. Ubiquitin immunoreactivity was relatively homogeneous in RFs with small diameters, but in RFs with large diameters, the immunoreactivity diminished in the center. Based on these observations, combined with the tendency of self-aggregation of αB-crystallin, it is conceivable that RFs are huge aggregation products of αB-crystallin involving GFAP, and that ubiquitination may be a consequent phenomenon, as it may be in other intracytoplasmic inclusions, such as neurofibrillary tangles and Lewy bodies.

Original languageEnglish
Pages (from-to)875-885
Number of pages11
JournalAmerican Journal of Pathology
Volume138
Issue number4
Publication statusPublished - Jan 1 1991

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Gold Colloid
Crystallins
Immunoelectron Microscopy
Glial Fibrillary Acidic Protein
Vimentin
Ubiquitin
Epitopes
Alexander Disease
Lewy Bodies
Neurofibrillary Tangles
Ubiquitination
Octoxynol
Neuroglia
Electrons
Temperature
Brain

All Science Journal Classification (ASJC) codes

  • Pathology and Forensic Medicine

Cite this

Rosenthal fibers share epitopes with αB-crystallin, glial fibrillary acidic protein, and ubiquitin, but not with vimentin : Immunoelectron microscopy with colloidal gold. / Tomokane, N.; Iwaki, Toru; Tateishi, J.; Iwaki, A.; Goldman, J. E.

In: American Journal of Pathology, Vol. 138, No. 4, 01.01.1991, p. 875-885.

Research output: Contribution to journalArticle

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abstract = "Ultrastructural immunoreactivities of αB-crystallin, glial fibrillary acidic protein (GFAP), ubiquitin, and vimentin in Rosenthal fibers (RFs) isolated from an Alexander's disease brain were investigated using nonosmium and low-temperature embedding technique. The morphology of RFs embedded in Lowicryl K4M resin was well preserved after treatment with 0.5{\%} Triton X-100. αB-crystallin immunoreactivity was present in RFs of various sizes and was the strongest in loosely scattered deposits, which were considered to be the initial stage of RFs. Glial fibrillary acidic protein immunoreactivity in RFs was heavy, homogeneous throughout RFs, and equivalent to that in networks of glial filaments. Immunoreactivities of both αB-crystallin and GFAP were mainly restricted to the high electron-dense areas within RFs and were proved to exist close to each other by double immunolabeling. Rosenthal fibers were negative for vimentin. Ubiquitin immunoreactivity was relatively homogeneous in RFs with small diameters, but in RFs with large diameters, the immunoreactivity diminished in the center. Based on these observations, combined with the tendency of self-aggregation of αB-crystallin, it is conceivable that RFs are huge aggregation products of αB-crystallin involving GFAP, and that ubiquitination may be a consequent phenomenon, as it may be in other intracytoplasmic inclusions, such as neurofibrillary tangles and Lewy bodies.",
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T1 - Rosenthal fibers share epitopes with αB-crystallin, glial fibrillary acidic protein, and ubiquitin, but not with vimentin

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