Localization of vimentin, the nonspecific intermediate filament protein, in embryonal glia and in early differentiating neurons

Bignami, A.; Raju, T.R.; Dahl, D.

doi:10.1016/0012-1606(82)90035-5

Cited by 363 publications

(184 citation statements)

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“…The assertion that the anti-NILE antibody stains neuronal fiber tracts is based on the fact that it recognizes elements in tissue sections that are (7) identical to fiber tracts stained with antibody against neurofilament proteins but (2) distinct from the radial glial fibers stained by an antibody against the intermediate filament protein vimentin. The contrast between the distribution and appearance of neuronal and glial fibers detected by immunofluorescent staining with anti-NILE and anti-vimentin antibodies, respectively, was also seen in an earlier study which compared anti-neurofilament and anti-vimentin antibodies (Bignami et al, 1982). Although the level of resolution obtained with tissue sections at the light microscopic level does not allow us to distinguish between nerve fibers and closely associated glial elements, the results from tissue culture studies have demonstrated that both central and peripheral neurons express the NILE glycoprotein, whereas astrocytes and oligodendrocytes do not (Stallcup et al, 1983).…”

Section: Discussionsupporting

confidence: 51%

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Antibody against nerve growth factor-inducible large external (NILE) glycoprotein labels nerve fiber tracts in the developing rat nervous system

Stallcup¹,

Beasley²,

Levine³

1985

J. Neurosci.

125

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The NILE (nerve growth factor-inducible large external) glycoprotein is a 230,000-dalton molecule found on the surface of PC12 cells. immunologically cross-reactive glycoproteins in the molecular weight range of 215,000 to 230,000 have been found on many types of neurons in culture. Using immunohistochemical methods, we have shown that NILErelated glycoproteins are present in neuronal fiber tracts of the developing rat brain. Antibody against the NILE glycoprotein specifically labels processes that appear identical to those recognized by antibodies against the neurofilament triplet of proteins. These processes are clearly distinct from the radial glial fibers recognized by antibody against the intermediate filament protein vimentin. NILE glycoprotein is not distributed uniformly over the entire neuronal surface but is concentrated on neurites and is much less abundant on cell bodies. NILE-positive fiber tracts are first seen in the spinal cord and rhombencephalon on embryonic day 11 and over the next 2 days appear in the mesencephalon and diencephalon.Staining in the telencephalon is not seen until embryonic day 15. The appearance of NILE immunoreactivity in these various regions closely parallels the appearance of neurofilament polypeptides, suggesting that NILE-related glycoproteins are present during the early phases of fiber tract formation. This idea is supported by the finding that the NILE glycoprotein can be found postnatally in parts of the nervous system such as the cerebellar cortex and olfactory bulb which undergo major histogenesis during the postnatal period. In the cerebellum the appearance of NILE immunoreactivity in the two major fiber zones, the molecular layer and the white matter, parallels the development of the fiber structure of these layers. These findings support tissue culture studies which suggest a role for the NILE glycoprotein in mediating nerve fiber fasciculation.

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Section: Discussionsupporting

confidence: 51%

“…In addition to staining of serial sections we also did mature radial astrocytes (Schnitzer et al, 1981;Bignami et al, 1982) immunofluorescent double-staining of the same section using results in two distinctly differing staining patterns (Fig. 8, B and C).…”

Section: Resultsmentioning

confidence: 99%

Antibody against nerve growth factor-inducible large external (NILE) glycoprotein labels nerve fiber tracts in the developing rat nervous system

Stallcup¹,

Beasley²,

Levine³

1985

J. Neurosci.

125

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“…Interestingly, these cell populations continue to express vimentin during adulthood (Shaw et al, 1981;Pixley and De Vellis, 1984;Bonfanti et al, 1993;Peretto et al, 1997). Vimentin is a cytoskeletal, intermediate filament protein very abundant during development, which can be found in immature glial cells, including radial glia (Bignami et al, 1982;Dahl et al, 1981), and in highly undifferentiated neuronal precursors (Cochard and Paulin, 1984). In adult animals, although mainly replaced by other intermediate filament proteins such as GFAP in glial cells and neurofilament triplet protein in neurons (see Steinert and Roop, 1988;Gorham et al, 1991), vimentin persists in many cell populations which are enriched in carnosine-related dipeptides, namely cerebellar Bergmann glia, ependymal cells, tanycytes, a sub-population of astrocytes in large myelinated bundles (Shaw et al, 1981;Pixley and De Vellis, 1984), radial glia-like cells in the supraoptic nucleus (Bonfanti et al, 1993), astrocytes of the glial tubes , and olfactory receptor neurons Gorham et al, 1991).…”

Section: Discussionmentioning

confidence: 99%

Carnosine-related dipeptides in the mammalian brain

Bonfanti

Peretto

Marchis

et al. 1999

Progress in Neurobiology

186

107

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-Carnosine and structurally related dipeptides are a group of histidine-containing molecules widely distributed in vertebrate organisms and particularly abundant in muscle and nervous tissue. Although many theories have been proposed, the biological function(s) of these compounds in the nervous system remains enigmatic. The purpose of this article is to review the distribution of carnosine-related dipeptides in the mammalian brain, with particular reference to some cell populations wherein these molecules have been demonstrated to occur very recently. The high expression of carnosine in the mammalian olfactory receptor neurons led to infer that this dipeptide could play a role as a neurotransmitter/modulator in olfaction. This prediction, which has not yet been fully demonstrated, does not explain the localization of carnosine-related dipeptides in other cell types, such as glial and ependymal cells. A recent demonstration of high carnosine-like immunoreactivity in the subependymal layer of rodents, an area of the forebrain which shares with the olfactory neuroepithelium the occurrence of continuous neurogenesis during adulthood, supports the hypothesis that carnosine-related dipeptides could be implicated in some forms of structural plasticity. However, the particular distribution of these molecules in the subependymal layer, along with their expression in glial/ependymal cell populations, suggests that they are not directly linked to cell migration or cell renewal. In the absence of a unified theory about the role of carnosine-related dipeptides in the nervous system, some common features shared by different cell populations of the mammalian brain which contain these molecules are discussed.

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“…Second, antibodies to vimentin are known to stain radial glia in embryonic nervous tissue from several species, including birds (see, e.g., Tapscott et al, 1981;Bignami et al, 1982;Pixley and devellis, 1984;Alvarez-Buylla et al, 1987). Third, R5, H5, and antivimentin stained cultured tectal cells similarly (Fig.…”

Section: Identification Of Glial Antigensmentioning

confidence: 90%

Developmentally regulated and spatially restricted antigens of radial glial cells

Herman

Victor

Sanes

1993

Developmental Dynamics

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Radial glial cells, present in many parts of the embryonic vertebrate central nervous system (CNS), have been implicated in the guidance of neuroblasts from the ventricular zone to their laminar destinations. Moreover, radial glial cells may be progenitors of some CNS neurons and glia. To gain new insight into the structure and development of these cells, we have generated and characterized a panel of monoclonal antibodies that recognize radial glial cells of the chick optic tectum. Mice were immunized with homogenates of embryonic day (E) 10 tectum, and antibodies were analyzed by immunofluorescence and immunoblotting. We describe here three pairs of antibodies. 1) H5 and a previously generated antibody, R5 (Drager et al., J. Neurosci. 42025, 1984), stain the whole extent of the radial glial cell from E7 to E20. In cultures prepared from El0 tecta, both stain a filamentous meshwork in glial cells but not in neurons. On immunoblots, both recognize a protein of -52 kD that is closely related (or identical) to vimentin. 2) H28 and H29 stain radial glia between E7 and E14, but not later. Moreover, H28 and H29 staining is markedly more intense in the ventricular and intermediate zones than in the laminae of the tectal plate. Both of these antibodies recognize an intracellular epitope in cultured glial cells and a protein of -35 kD on immunoblots. 3) H2 and H27 recognize antigens concentrated in the most superficial processes and endfeet of radial glia in late (E16-E20) embryos. They stain distinct structures in cultured glia, suggesting that they recognize distinct antigens. H27 recognizes a protein of -29 kD on immunoblots. Thus antibodies H5 and R5 are good markers of radial glial cells at all stages, whereas the others define antigens that are developmentally regulated and localized to discrete domains. Together, these antibodies can be used to study temporal and spatial specializations of radial glia. o 1993 %ley-Liss, Inc.

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Localization of vimentin, the nonspecific intermediate filament protein, in embryonal glia and in early differentiating neurons

Cited by 363 publications

References 26 publications

Antibody against nerve growth factor-inducible large external (NILE) glycoprotein labels nerve fiber tracts in the developing rat nervous system

Antibody against nerve growth factor-inducible large external (NILE) glycoprotein labels nerve fiber tracts in the developing rat nervous system

Carnosine-related dipeptides in the mammalian brain

Developmentally regulated and spatially restricted antigens of radial glial cells

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