Identification of tubulin associated with rat brain myelin

Gozes, Illana; Richter‐Landsberg, Christiane

doi:10.1016/0014-5793(78)80076-3

Cited by 39 publications

(18 citation statements)

References 23 publications

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“…In addition to the well-defined changes in myelin and astroglial proteins in MS and SSPE, the levels of tubulin and the neurofilament proteins also appeared to be decreased. In neurons tubulin is present in the microtubule system, in the axonal plasma membrane (Estridge, 1977), in synaptosomal membranes (Kelly and Cotman, 1978), and has also been reported to be a constituent of highly purified myelin (Gozes and Richter-Landsberg, 1978). In the present study strong tubulin banding was seen in myelin samples with both staining methods.…”

Section: S 5 a B C D E F G H A B C D E F G Hsupporting

confidence: 66%

The Immunological Identification of Brain Proteins on Cellulose Nitrate in Human Demyelinating Disease

Newcombe¹,

Glynn²,

Cuzner³

1982

Journal of Neurochemistry

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An immunological technique has been employed to identify proteins, separated in polyacrylamide gels, which show changes in brain samples from cases of multiple sclerosis and subacute sclerosing panencephalitis. Sodium dodecylsulphate‐treated proteins in particulate and soluble fractions were separated in polyacrylamide slab gels, transferred electrophoretically onto cellulose nitrate sheets, incubated with specific antisera and visualized by an immunoperoxidase method. Protein bands showing changes were identified using antisera raised against the myelin basic and Wolfgram proteins, the neurofilament triplet proteins, tubulin and glial fibrillary acidic protein. In addition to the loss of myelin proteins, decreases in the neurofilament proteins and in tubulin were seen in both multiple sclerosis and subacute sclerosing panencephalitis samples. The distribution of glial fibrillary acidic protein polypeptides in the particulate and soluble fractions of plaque samples appeared to vary according to the degree of fibrosis. Changes in the levels of the myelin‐associated glycoprotein, the lower molecular weight component of the Wolfgram protein, albumin and immunoglobulin G, none of which were visualized by protein staining, were also seen. This immunological technique has allowed a closer examination of changes occurring in brain protein spectra in multiple sclerosis and subacute sclerosing panencephalitis.

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Section: S 5 a B C D E F G H A B C D E F G Hsupporting

confidence: 66%

The Immunological Identification of Brain Proteins on Cellulose Nitrate in Human Demyelinating Disease

Newcombe¹,

Glynn²,

Cuzner³

1982

Journal of Neurochemistry

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“…Involvement of actin and tubulin during myelin formation has been suggested in that both proteins have been shown to copurify with myelin from rat brain (45), and purified MBP forms complexes with these proteins (45)(46)(47). A colocalization between MBP and the microtubule protein tubulin has also been reported (48).…”

Section: Discussionmentioning

confidence: 95%

Functional implications for the microtubule-associated protein tau: localization in oligodendrocytes.

LoPresti¹,

Szuchet

Papasozomenos³

et al. 1995

Proc. Natl. Acad. Sci. U.S.A.

347

260

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We present evidence that the microtubuleassociated protein tau is present in oligodendrocytes (OLGs), the central nervous system cells that make myelin. By showing that tau is distributed in a pattern similar to that of myelin basic protein, our results suggest a possible involvement of tau in some aspect of myelination. Tau protein has been identified in OLGs in situ and in vitro. In interfascicular OLGs, tau localization, revealed by monoclonal antibody Tau-5, was confined to the cell somata. However, in cultured ovine OLGs with an exuberant network of processes, tau was detected in cell somata, cellular processes, and membrane expansions at the tips of these processes. Moreover, in such cultures, tau appeared localized adjacent to or coincident with myelin basic protein in membrane expansions along and at the ends of the cellular processes. The presence of tau mRNA was documented using fluorescence in situ hybridization. The distribution of the tau mRNA was similar to that of the tau protein.Western blot analysis of cultured OLGs showed the presence of many tau isoforms. Together, these results demonstrate that tau is a genuine oligodendrocyte protein and pave the way for determining its functional role in these cells.

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“…A recent publication suggested that microtubules regulate calcium signalling between mitochondria and endoplasmic reticulum in neurons (Mironov et al 2005) and NAP was shown to be associated with calcium mobilization (Visochek et al 2005). Although the bulk cellular tubulin is cytoplasmic, tubulin association with membranes was also observed (Gozes and Richter-Landsberg 1978;Gozes and Littauer 1979;Zisapel et al 1980). Morphological studies revealed co-localization of microtubules with mitochondria and endoplasmic reticulum that was decreased after microtubule disruption.…”

Section: Discussionmentioning

confidence: 99%

“…2005). Although the bulk cellular tubulin is cytoplasmic, tubulin association with membranes was also observed (Gozes and Richter‐Landsberg 1978; Gozes and Littauer 1979; Zisapel et al . 1980).…”

Section: Discussionmentioning

confidence: 99%

Peptide neuroprotection through specific interaction with brain tubulin

Divinski

Holtser-Cochav

Vulih-Schultzman

et al. 2006

Journal of Neurochemistry

Self Cite

103

110

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This study aimed to identify the neuronal target for the potent neuroprotective peptide NAP. When added to pheochromocytoma cells (neuronal model), NAP was found in the intracellular milieu and was co-localized with microtubules. NAP induced neurite outgrowth and protected primary neurons against microtubule-associated ZnCl 2 toxicity. Rapid microtubule reorganization into distinct microtubules ensued after NAP addition to both pheochromocytoma cells and primary cerebral cortical neurons, but not to fibrobalsts. While binding neuronal tubulin and protecting pheochromocytoma cells against oxidative stress, NAP did not bind tubulin extracted from fibroblasts, nor did it protect those cells against oxidative stress. Affinity chromatography identified the brain-specific bIII-tubulin as a major NAP binding protein. Paclitaxel (a microtubule aggregating agent that interacts with b-tubulin) reduced NAP tubulin binding. Thus, the underlying mechanism for the neuroprotection offered by NAP is targeting neuronal microtubules that are essential for neuronal survival and function.

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Identification of tubulin associated with rat brain myelin

Cited by 39 publications

References 23 publications

The Immunological Identification of Brain Proteins on Cellulose Nitrate in Human Demyelinating Disease

The Immunological Identification of Brain Proteins on Cellulose Nitrate in Human Demyelinating Disease

Functional implications for the microtubule-associated protein tau: localization in oligodendrocytes.

Peptide neuroprotection through specific interaction with brain tubulin

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