Reply by Dr. Shelanski

Shelanski, H. A.

doi:10.1016/0002-9378(51)90039-7

Cited by 13 publications

(12 citation statements)

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“…On the contrary, a2P-labeled proteins are constantly present at the bottom and the top of the ultracentrifugation profile. It seems therefore that both thyroid and brain 6 S tubulins are, in vitro as well as in vivo [13], a very poor substrate, if not at all, for protein kinases.…”

Section: 6mentioning

confidence: 99%

Non phosphorylationin vitro of the 6 S tubulin from brain and thyroid tissue

1972

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Section: 6mentioning

confidence: 99%

Non phosphorylationin vitro of the 6 S tubulin from brain and thyroid tissue

1972

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“…Although earlier studies suggested a similarity in composition between microtubules and l0-nm filaments, recent structural and chemical studies have demonstrated that they are distinct. Microtubules and 10-nm filaments have been consistently found together in BHK21 cells (18,19,25,54) and in nerve axons (35,43,57) . It was therefore of interest to extend the earlier studies from this laboratory which demonstrated an association of microtubules with nuclear movements and aligment in SV5-infected BHK21-F syncytia, to an examination of the role in such movement of all three cytoplasmic fibers, i .e, microtubules, microfilaments, and 10-nm filaments.…”

mentioning

confidence: 96%

“…Recently, 10-nm filaments have been characterized as a class of cytoplasmic fibers with unique antigenic and biochemical properties (20,34,43,48,49,54,57) . They have been observed in the same orientation in the cytoplasm as microtubules (19,25,54), and are thought to depend on micro-334 THE JOURNAL OF CELL BIOLOGY " VOLUME 83,1979 tubules for their distribution in the cell (19) .…”

Section: Wang Cross and Choppinmentioning

confidence: 99%

Involvement of microtubules and 10-nm filaments in the movement and positioning of nuclei in syncytia.

Wang¹,

Cross²,

Choppin³

1979

The Journal of Cell Biology

102

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Previous studies (Holmes, K. V., and P. W. Choppin. J. showed that infection of baby hamster kidney (BHK21-F) cells with the parainfluenza virus SV5 causes extensive cell fusion, that nuclei migrate in the syncytial cytoplasm and align in tightly-packed rows, and that microtubules are involved in nuclear movement and alignment. The role of microtubules, 10-nm filaments, and actin-containing microfilaments in this process has been investigated by immunofluorescence microscopy using specific antisera, time-lapse cinematography, and electron microscopy . During cell fusion, microtubules and 10-nm filaments from many cells form large bundles which are localized between rows of nuclei . No organized bundles of actin fibers were detected in these areas, although actin fibers were observed in regions away from the aligned nuclei . Although colchicine disrupts microtubules and inhibits nuclear movement, cytochalasin B (CB; 20-50 NLg/ml) does not inhibit cell fusion or nuclear movement. However, CB alters the shape of the syncytium, resulting in long filamentous processes extending from a central region. When these processes from neighboring cells make contact, fusion occurs, and nuclei migrate through the channels which are formed. Electron and immunofluorescence microscopy reveal bundles of microtubules and 10-nm filaments in parallel arrays within these processes, but no bundles of microfilaments were detected. The effect of CB on the structural integrity of microfilaments at this high concentration (20 leg/ml) was demonstrated by the disappearance of filaments interacting with heavy meromyosin. Cycloheximide (20 p,g/ml) inhibits protein synthesis but does not affect cell fusion, the formation of microtubules and 10-nm filament bundles, or nuclear migration and alignment; thus, continued protein synthesis is not required . The association of microtubules and 10-nm filaments with nuclear migration and alignment suggests that microtubules and 10-nm filaments are two components in a system which serves both cytoskeletal and force-generating functions in intracellular movement and position of nuclei.KEY WORDS cell fusion immunofluorescence microscopy microfilaments -simian virus 5 cytochalasin B Previous studies from this laboratory showed that infection of monolayers of baby hamster kidney (BHK21-F) cells with the parainfluenza virus, sim-J. CELL BIOLOGY

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“…Within the neuron population not all types are equally susceptible; for ex.ample, the dorsal root ganglion cell is highly resistant to aluminum toxicity. Susceptible neuronsand human cerebral fetal neurons are among the susceptible group -appear to respond in one of two ways: A small proportion are stimulated to produce lOOA 0 filaments, chemically and immunologically identical to neurofilaments (17), and some neurons undergo a marked inhibition of protein synthesis and die without neurofibrillary degeneration. In some brain regions with neurofibrillary degeneration in Alzheimer's disease, aluminum concentrations approaching those lethal to both cats and human cerebral neurons in tissue culture have been found.…”

Section: Aluminum As a Cytotoxic Factormentioning

confidence: 99%

Brain Aging and Alzheimer's Disease^*

DeBoni

1978

Canadian Psychiatric Association Journal

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The most common cause of senile dementia appears to be a pathological process indistinguishable from that found in presenile dementia of the Alzheimer type. Consideration of the neuropathological changes suggest that this disease may involve the interaction of at least three processes: a viral-like infection, a disorder in the immune system and the neurotoxic effect of an environmental agent. The evidence in support of this hypothesis is reviewed.

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Reply by Dr. Shelanski

Cited by 13 publications

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Non phosphorylationin vitro of the 6 S tubulin from brain and thyroid tissue

Non phosphorylationin vitro of the 6 S tubulin from brain and thyroid tissue

Involvement of microtubules and 10-nm filaments in the movement and positioning of nuclei in syncytia.

Brain Aging and Alzheimer's Disease^*

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Reply by Dr. Shelanski

Cited by 13 publications

References 0 publications

Non phosphorylationin vitro of the 6 S tubulin from brain and thyroid tissue

Non phosphorylationin vitro of the 6 S tubulin from brain and thyroid tissue

Involvement of microtubules and 10-nm filaments in the movement and positioning of nuclei in syncytia.

Brain Aging and Alzheimer's Disease*

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Brain Aging and Alzheimer's Disease^*