Occurrence of two different intermediate filament proteins in the same filament in situ within a human glioma cell line

Sharp, Gaynor; Osborn, Mary; Weber, Klaus

doi:10.1016/0014-4827(82)90227-0

Cited by 110 publications

(27 citation statements)

References 39 publications

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“…In our study, all GFAP-positive cells were stained with vimentin. This result agrees with previous reports [17]. Some cells containing vimentin but not GFAP are presumed to be nonglial, mesenchymal cells such as vascular cells.…”

Section: Discussionsupporting

confidence: 83%

Epiretinal Membrane of Proliferative Diabetic Retinopathy: An Immunohistochemical Study

Hosoda

Okada²,

Matsumura³

et al. 1993

Ophthalmic Res

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Nineteen cases of epiretinal membrane (ERM) in proliferative diabetic retinopathy were studied using immunohistochemical methods. Antibodies against type I-IV collagen, fibronectin (FN), glial fibrillary acidic protein (GFAP), vimentin and the monoclonal antibody (MAB) against human Müller cells were used to examine the membranes. Type II collagen was found on one side of the ERMs in 95% of the cases. The other types of collagen, FN and vimentin were also identified in most cases. Müller cells (GFAP- and MAB-positive) were found in 2/19 cases (11 %), and astrocytes (GFAP-positive but MAB-negative) were found in 10/19 cases (53%). These results suggest that type II collagen (vitreal collagen) may act as a scaffolding in the formation of ERMs and that glial elements of the ERMs consist mainly of astrocytes.

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Section: Discussionsupporting

confidence: 83%

Epiretinal Membrane of Proliferative Diabetic Retinopathy: An Immunohistochemical Study

Hosoda

Okada²,

Matsumura³

et al. 1993

Ophthalmic Res

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“…This molecular organization would be consistent with the antiparallel arrangement of IF dimers proposed on the basis of structural analysis of a-keratin (40) and could provide both homopolymers and heteropolymers not only the capacity for increased structural variability but also the potential for enhanced functional plasticity. That vimentin and GFAP are coexpressed in immature glial cells (36), some glioma cell lines (38,39), and reactive astrocytes (37), but not in mature, growth-arrested astrocytes, is compatible with this possibility and suggests that in each of these cell types the cytoskeleton might have quite distinct biological functions.…”

Section: Discussionsupporting

confidence: 54%

“…Rarely, GFAP and vimentin are present in the same cell (36,37). If copolymers between these two IF proteins can be formed, as suggested by in vitro studies (38,39), the very disparate sizes of the terminal regions of GFAP and vimentin suggest it is more likely that the individual IF protein molecules would be arranged head-to-head and tail-to-tail rather than in a headto-tail manner. This molecular organization would be consistent with the antiparallel arrangement of IF dimers proposed on the basis of structural analysis of a-keratin (40) and could provide both homopolymers and heteropolymers not only the capacity for increased structural variability but also the potential for enhanced functional plasticity.…”

Section: Discussionmentioning

confidence: 99%

Molecular cloning and primary structure of human glial fibrillary acidic protein.

Reeves

Helman

Allison

et al. 1989

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

191

118

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Glial fibrillary acidic protein (GFAP) is an intermediate-filament (IF) protein that is highly specific for cells of astroglial lineage, although its tissue-specific role is speculative. Determination of the primary structure of this protein should be of importance for understanding the functional role it plays in astroglia. Therefore, we isolated a cDNA clone encoding this protein and determined its nucleotide sequence. The predicted amino acid sequence indicates that GFAP shares structural similarities-particularl in the central rod domain and to a lesser degree in the carboxyl-terminal domain-with other IF proteins found in nonepithelial cell types. Considerable sequence divergence in the amino-terminal region of GFAP suggests that the tissue-specific functions ofthis IF protein might be mediated through this region of the molecule. In contrast, conservation of structural characteristics and a moderate degree of sequence conservation in the carboxyl-terminal region suggest functional similarities. Blot hybridization analysis using the GFAP cDNA as a probe failed to detect GFAP mRNA in both normal and neoplastic human tissues in which IF proteins other than GFAP are known to be expressed.

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“…We presume that chicken and mouse vimentins copolymerize when they are coexpressed in undifferentiated cells; although our antibodies react with both chicken and mouse vimentin and hence are not capable of discriminating between the two molecules by immunofluorescence microscopy, copolymerization of vimentin and desmin, vimentin and glial fibrillary acidic protein, and vimentin and neurofilament protein has been described (35,75,76,82,83). As chicken vimentin-expressing MEL cells differentiate, the composition of intermediate filaments probably changes gradually frotn a mouse-chicken vimentin heteropolymer to a chicken vimentin homopolymer.…”

Section: Transfection Of Mel Cells With the Chicken Vimentin Genementioning

confidence: 84%

Expression of transfected vimentin genes in differentiating murine erythroleukemia cells reveals divergent cis-acting regulation of avian and mammalian vimentin sequences.

Ngai¹,

Bond²,

Wold³

et al. 1987

Mol. Cell. Biol.

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We studied the expression of transfected chicken and hamster vimentin genes in murine erythroleukemia (MEL) cells. MEL cells normally repress the levels of endogenous mouse vimentin mRNA during inducermediated differentiation, resulting in a subsequent loss of vimentin filaments. (8,29,36,77).The generality and diversity of vimentin expression suggest that its regulation is necessarily complex. This complexity is particularly evident from a comparison of avian and mammalian erythropoiesis. The mature avian erythrocyte is a nucleated biconvex ellipsoidally shaped cell. Ultrastructural analyses of avian erythrocytes have revealed a network of intermediate filaments that spans the cytoplasm and appears to anchor the centrally located nucleus (34,89,92). The major subunit protein of these filaments is vimentin (36). * Corresponding author.In contrast, the anucleate, biconcave disk-shaped mammalian erythrocyte contains no intermediate filaments. Studies of human hematopoiesis in vivo have demonstrated that vimentin is expressed early in erythroid differentiation but is lost in the erythroblastic stages (22).In chicken erythroid cells, vimentin filaments are assembled rapidly and stably from a soluble pool of newly synthesized vimentin (5, 62). The efficiency and rapidity of vimentin assembly in vivo suggest that the extent of vimentin filament formation is determined primarily by the amount of vimentin synthesized. We have shown that the expression of vimentin protein during erythropoiesis is determined primarily by mRNA abundance (10, 69). In chicken embryonic erythropoiesis, vimentin mRNA is found at low levels in immature, mitotic primitive cells and accumulates to increasingly higher levels during terminal differentiation of the definitive erythroid lineage, apparently underlying similar changes at the protein level (10). During differentiation of murine erythroleukemia (MEL) cells in vitro, vimentin mRNA levels rapidly and extensively decline (-25-fold reduction), rendering a concomitant decrease in vimentin synthesis and a subsequent loss of vimentin filaments (69). The striking difference in the changes of vimentin mRNA abundances (and, ultimately, vimentin filaments) during mammalian and avian erythropoiesis presents an opportunity to study not only the factors responsible for the dynamic positive and negative regulation of the vimentin gene but also the basis for the evolutionary divergence of the two erythropoietic programs with regard to vimentin expression.In the present study, we addressed these issues by examining the behavior of transfected chicken and hamster vimentin genes in differentiating MEL cells. The utility of studying both resident and transfected genes during in vitro differentiation of MEL cells is well established (reviewed in references 13 and 55). We demonstrate that, in MEL cell lines harboring and expressing chicken vimentin genes,

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Occurrence of two different intermediate filament proteins in the same filament in situ within a human glioma cell line

Cited by 110 publications

References 39 publications

Epiretinal Membrane of Proliferative Diabetic Retinopathy: An Immunohistochemical Study

Epiretinal Membrane of Proliferative Diabetic Retinopathy: An Immunohistochemical Study

Molecular cloning and primary structure of human glial fibrillary acidic protein.

Expression of transfected vimentin genes in differentiating murine erythroleukemia cells reveals divergent cis-acting regulation of avian and mammalian vimentin sequences.

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