A Monoclonal Antibody That Recognizes an Adhesion Molecule Expressed by Certain Cells of Neuroectodermal and Mesenchymal Origin

Mittal, Bina; David, Samuel

doi:10.1006/mcne.1994.1006

Cited by 10 publications

(6 citation statements)

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“…2, A and B). This monoclonal antibody is species-specific and only recognizes native rat ceruloplasmin (9,18). In contrast, cells transfected with the cDNA for secreted ceruloplasmin did not show cell surface labeling with the monoclonal antibody to ceruloplasmin (Fig.…”

Section: Resultsmentioning

confidence: 82%

“…By using a monoclonal antibody (mAb 1A1), ceruloplasmin was shown to be expressed on the surface of astrocytes in the mammalian brain (9) as well as by leptomeningeal cells and fibroblasts in a number of tissues including the liver (18). However, hepatocytes, which produce the ceruloplasmin present in serum, do not express the GPI-anchored form.…”

Section: Discussionmentioning

confidence: 98%

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Alternative RNA Splicing Generates a Glycosylphosphatidylinositol-anchored Form of Ceruloplasmin in Mammalian Brain

Patel¹,

Dunn

David

2000

Journal of Biological Chemistry

183

142

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Ceruloplasmin is a copper-containing ferroxidase that is essential for normal iron homeostasis. Whereas ceruloplasmin in plasma is produced and secreted by hepatocytes, in the brain a glycosylphosphatidylinositol (GPI)-anchored form of ceruloplasmin is expressed on the surface of astrocytes. By using a cDNA cloning approach, we have now determined that the GPI-anchored form of ceruloplasmin is generated by alternative RNA splicing. The splicing occurs downstream of exon 18 and replaces the C-terminal 5 amino acids of the secreted form with an alternative 30 amino acids that signal GPI anchor addition. RNase protection analysis demonstrates that the GPI-anchored form is the major form in the brain, whereas the secreted form predominates in the liver. Individuals with aceruloplasminemia, a hereditary deficiency of ceruloplasmin, have severe iron deposition in a number of organs, including the brain where it results in neurodegeneration. Therefore, this novel GPI-anchored form of ceruloplasmin is likely to play an important role in iron metabolism in the central nervous system.

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Section: Resultsmentioning

confidence: 82%

Section: Discussionmentioning

confidence: 98%

Alternative RNA Splicing Generates a Glycosylphosphatidylinositol-anchored Form of Ceruloplasmin in Mammalian Brain

Patel¹,

Dunn

David

2000

Journal of Biological Chemistry

183

142

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“…These investigators generated a monoclonal antibody (1A1) to a cell-surface protein on astrocytes and leptomeningeal cells (Mittal and David, 1994); subsequent microsequencing of the immunopurified antigen showed it to be ceruloplasmin (Patel and David, 1997). They also demonstrated that after PIPLC treatment the 1A1 antigen expressed the cross-reactive determinant (CRD).…”

Section: Ran-2 a Glial Lineage Marker Corresponds To A Gpi-anchoredmentioning

confidence: 97%

Ran-2, a glial lineage marker, is a GPI-anchored form of ceruloplasmin

et al. 1998

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Cell interactions in the nervous system are frequently mediated by surface proteins that are attached to the membrane by a glycosyl phosphatidylinositol (GPI) anchor. In this study, we have characterized the expression of such proteins on glial cells. We have detected a major GPI-anchored protein on astrocytes and Schwann cells, with a molecular weight of 140 kD. When Schwann cells were treated with forskolin to promote a myelinating phenotype, expression of this 140-kD protein dramatically decreased, whereas another GPI-anchored protein of 80 kD was strongly induced; expression of other integral membrane proteins were likewise dramatically altered. The size and pattern of expression of the 140-kD protein suggested that it might correspond to the Ran-2 antigen, a glial lineage marker. This notion was confirmed by immunoprecipitating this 140-kD protein with the Ran-2 monoclonal antibody. The Ran-2 antigen is expressed over the entire Schwann cell surface in a punctate fashion; it is removed by phosphatidylinositol phospholipase C treatment, thereby confirming that it is GPI-anchored. When Schwann cells are cocultured with neurons, the Ran-2 antigen initially concentrates at sites of Schwann cell contact with neurons, suggesting that it may play a role in early Schwann cell-neuron interactions; it is then downregulated. Protein sequencing of the Ran-2 antigen immunopurified from rat brain membranes showed complete identity over two extended segments with the copper binding protein ceruloplasmin. These findings indicate that astrocytes and Schwann cells express a novel GPI-anchored form of ceruloplasmin and suggest that this GPI form plays a role in axonal-glial interactions.

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“…Culture of Bergmann glia (Mittal and David, 1994) and granule cells (Levi et al, 1989;Xia et al, 1995) have been described previously. Briefly, cerebella were removed aseptically from 8-to 10-day-old Wistar rats and chopped in two orthogonal directions with a mechanical tissue chopper (McIlwain, Brinkmann Instruments, Westbury, NY).…”

Section: Tissue Culturementioning

confidence: 99%

Coordinate regulation of NAD(P)H:Quinone oxidoreductase and glutathione-S-transferases in primary cultures of rat neurons and glia: Role of the antioxidant/electrophile responsive element

Ahlgren-Beckendorf

Reising

Schander

et al. 1999

Glia

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NAD(P)H:quinone oxidoreductase (QR) and glutathione‐S‐transferases (GSTs) are among the enzymes believed to protect an organism against oxidative stress. To test if redox‐cycling compounds regulate the expression of these enzymes in cells of neural origin, primary cultures of rat cerebellar neurons and glia were treated with tert‐butylhydroquinone (tBHQ) and hydroquinone (HQ). Basal levels of endogenous QR and GST activity were significantly greater in glia than neurons; and QR, GSTP1, and A3 were increased in glial but not neuronal cultures by treatment with tBHQ and HQ. A possible role for protein kinase C (PKC) in the tBHQ‐mediated increase in QR and GST was evaluated by activating PKC with phorbol 12‐myristate 13‐acetate or inhibiting PKC with bisindolylmaleimide I. PKC was not involved in maintaining basal expression or mediating the increased expression of GST or QR by tBHQ. Transcriptional activation of QR and rGSTP1 by tBHQ could be mediated through a common responsive element present in the 5′‐flanking region of both genes, the antioxidant/electrophile responsive element (ARE/EpRE). Transient transfection of the glial cultures with rGSTP1‐ or rQR1‐ARE/EpRE‐luciferase reporter constructs demonstrated that tBHQ transcriptionally activates the ARE/EpRE. Thus, the increased expression of genes regulated by the ARE/EpRE in cells of the central nervous system may provide protection against oxidative stress. GLIA 25:131–142, 1999. © 1999 Wiley‐Liss, Inc.

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A Monoclonal Antibody That Recognizes an Adhesion Molecule Expressed by Certain Cells of Neuroectodermal and Mesenchymal Origin

Cited by 10 publications

References 0 publications

Alternative RNA Splicing Generates a Glycosylphosphatidylinositol-anchored Form of Ceruloplasmin in Mammalian Brain

Alternative RNA Splicing Generates a Glycosylphosphatidylinositol-anchored Form of Ceruloplasmin in Mammalian Brain

Ran-2, a glial lineage marker, is a GPI-anchored form of ceruloplasmin

Coordinate regulation of NAD(P)H:Quinone oxidoreductase and glutathione-S-transferases in primary cultures of rat neurons and glia: Role of the antioxidant/electrophile responsive element

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