Isolation from peripheral nerve of a protein similar to the glial fibrillary acidic protein

Dahl, D.; Bignami, A.

doi:10.1016/0014-5793(76)80522-4

Cited by 33 publications

(6 citation statements)

References 16 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Although not present in homogenates of freshly excised nerve (17,20,24), a small and variable amount of this protein was identified in nerve extracted with 6 M guanidine hydrochloride or 50% formic acid before solubilization in SDS (6). A similar protein was also isolated from peripheral nerves subjected to prolonged and complex extraction procedures developed for CNS proteins (4). It is also possible that the presumptive neurofilament proteins of 50,000-54,000 mol wt occur at other locations in different electrophoretic systems (12).…”

Section: Discussionmentioning

confidence: 99%

Neurofilament proteins of rat peripheral nerve and spinal cord.

Schlaepfer¹,

Freeman²

1978

The Journal of Cell Biology

215

View full text Add to dashboard Cite

Intact neurofilaments were isolated in parallel from rat peripheral nerve and spinal cord by osmotic shock into hypotonic media containing divalent cation chelators. Isolated neurofilaments were washed and separated by multiple centrifugations in 0.1 M NaCI. Abundant intact neurofilaments were identified in the washed pellets by negative staining techniques. Their origin from neurofilaments was confirmed by immune electron microscopy. Washed neurofilaments were extracted from lipid and membranous components with 8 M urea.Analyses of neurofilament isolates on sodium dodecyl sulfate gels showed that proteins of 200,000, 150,000, and 69,000 mol wt were the major components of intact neurofilaments derived from rat peripheral and central nervous systems. These same proteins were identified in whole tissue homogenates of both sources and became enriched during the isolation of intact neurofilaments. A minor component of 64,000 mol wt arose during isolation. Other proteins were identified as contaminants. Small amounts of proteins with electrophoretic migration of tubulin and actin remain in neurofilament isolates.KEY WORDS intermediate filaments mammalian neurofilaments 9 protein subunits gel electrophoresis -immune electron microscopy Although neurofilaments are abundant within large axons (13,14,39,40) and dendrites (38,40,41), they have remained a poorly understood organelle. Attempts to identify the neurofilament subunit protein from different sources have resuited in conflicting data. The 50,000-54,000 mol wt neurofilament protein isolated from mammalian brain (8,9, 18,(34)(35)(36)42) is not seen in the electrophoretic profiles of other neurofilamentrich tissues such as mammalian peripheral nerve (17, 20, 24) or invertebrate axoplasm from squid (20, 23) and Myxicola (15,17, 20). Conversely, the larger neurofilament proteins of peripheral nerve (17, 20, 24), squid axoplasm (20, 23), and Myxicola axoplasm (15,17, 20) have not been identified as major components in neurofllaments isolated from brain (8,9, 18,(34)(35)(36)42).Differences in protein composition among neurofilament isolates may arise from an inherent lability of neurofilament proteins. Mammalian neurofilament proteins are rapidly altered during WaUerian degeneration (33), concomitant with a postulated calcium influx into the axoplasm (25, 26, 29, 31). A similar breakdown of neurofilament proteins occurs when invertebrate neurofilaments are exposed to calcium (15). Some alterations of neurofilament proteins could occur during the prolonged preparative procedures used to isolate neurofilaments from mammalian brain tissues. A relationship between the 50,000-54,000 mol wt neurofilament proteins and higher molecular weight proteins in brain neurofilament iso-J. CELL BIOLOGY 9 The Rockefeller University Press 9

show abstract

Section: Discussionmentioning

confidence: 99%

Neurofilament proteins of rat peripheral nerve and spinal cord.

Schlaepfer¹,

Freeman²

1978

The Journal of Cell Biology

215

View full text Add to dashboard Cite

show abstract

“…They both occur amid a background of abundant skeins of microfilaments, and both appear to be continuous with them [39]. Recently, Dahl and Bignami [40] described the isolation of a protein from peripheral nerve filaments that is similar to the glial fibrillary acid protein. This is of interest, since it demonstrates that peripheral nerve filaments and glial filaments ma17 share at least one common fibrillary protein, and it suggests that Rosenthal fibers may indeed be related to the morphologically similar granular electron-dense masses seen in our patient's peripheral nerve.…”

Section: However Bradley and Williamsmentioning

confidence: 99%

Giant axonal neuropathy: A childhood disorder of microfilaments

Koch

Schultz

Williams

et al. 1977

Annals of Neurology

View full text Add to dashboard Cite

A sural nerve biopsy was performed on an 8-year-old boy with a chronic, slowly progressive polyneuropathy. Light and electron microscopy as well as teased nerve-fiber preparations demonstrated numerous giant axons filled with closely packed neurofilaments. Both myelinated and unmyelinated fibers were involved. Segmental demyelination, remyelination, and onion-bulb formation by multiple Schwann cell processes were observed, suggesting recurrent Schwann cell dysfunction. Abundant aggregates of cytoplasmic microfilaments occurred in Schwann cells, endothelial cells, perineurial cells, endoneurial fibroblasts, and endomysial fibroblasts. These findings support the proposal that giant axonal neuropathy is a generalized disorder of cytoplasmic microfilaments and that segmental demyelination occurs concomitantly with axonal and Schwann cell disease. The pathogenesis of this rare disorder is discussed with reference to experimental toxic neuropathies.

show abstract

“…Since GFA protein has been found to be structurally related to neurofilament protein according to biochemical and immunological criteria (6,17,19), it was also of interest to investigate whether the GFA protein is limited to glial cells by a method which permits a higher resolution of fine structural detail, In addition, it seemed pertinent to study the subcellular distribution of GFA protein at the ultrastructural level and, as part of a study on the localization of various nervous system antigens, to obtain improved tissue preservation.…”

mentioning

confidence: 99%

Ultrastructural localization of glial fibrillary acidic protein in mouse cerebellum by immunoperoxidase labeling.

Schachner¹,

Hedley‐Whyte²,

Hsu³

et al. 1977

The Journal of Cell Biology

318

View full text Add to dashboard Cite

Glial fibrillary acidic protein was localized at the electron microscope level in the cerebellum of adult mice by indirect immunoperoxidase histology. In confirmation of previous studies at the light microscope level, the antigen was detectable in astrocytes and their processes, but not in neurons or their processes, or in oligodendroglia. Astrocytic processes were stained in white matter, in the granular layer surrounding synaptic glomerular complexes, and in the molecular layer in the form of radially oriented fibers and of sheaths surrounding Purkinje cell dendrites. Astrocytic endfeet impinging on meninges and perivascular membranes were also antigen positive. In astrocytic perikarya and processes, the immunohistochemical reaction product appears both as a diffuse cytoplasmic label and as elongated strands, which by their distribution and frequency could be considered glial filaments.

show abstract

Isolation from peripheral nerve of a protein similar to the glial fibrillary acidic protein

Cited by 33 publications

References 16 publications

Neurofilament proteins of rat peripheral nerve and spinal cord.

Neurofilament proteins of rat peripheral nerve and spinal cord.

Giant axonal neuropathy: A childhood disorder of microfilaments

Ultrastructural localization of glial fibrillary acidic protein in mouse cerebellum by immunoperoxidase labeling.

Contact Info

Product

Resources

About