Schwann Cell CD9 Expression Is Regulated by Axons

Banerjee, Shilpi A.; Patterson, Paul H.

doi:10.1006/mcne.1995.1034

Cited by 27 publications

(15 citation statements)

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“…This correlation is particularly striking in the ventral horn of the spinal cord, where CD9 expression parallels the transient expression of other surface proteins involved in neurite outgrowth such as TAG-1 (Dodd et al, 1988) and DM-GRASP/SC1 (Burns et al, 1991;Tanaka et al, 1991;Tole and Patterson, 1993). CD9 expression in myelinating Schwann cells during development and after injury in vivo also suggests that immature Schwann cells do not express CD9, whereas differentiating Schwann cells do so (Banerjee and Patterson, 1995;Kaprielian et al, 1995).…”

Section: Discussionmentioning

confidence: 96%

“…CD9, a member of the tetraspan family of cell surface molecules, has been implicated as a signaling molecule in various cellular processes such as adhesion, growth, motility, and differentiation in the hematopoietic and nervous systems (Wright and Tomlinson, 1994;Anton et al, 1995;Banerjee and Patterson, 1995;Hadjiargyrou and Patterson, 1995). The ability of activating anti-CD9 mAbs to cause cellular changes was utilized to elucidate many of these functions.…”

Section: Discussionmentioning

confidence: 99%

“…CD9 is expressed in Schwann cells during development (Kaprielian et al, 1995) and after injury (Banerjee and Patterson, 1995) in a pattern that mimics the myelin genes, suggesting the possibility that CD9 may play a signaling role in vivo. Moreover, experiments using mAbs against CD9 have implicated this protein in Schwann cell adhesion, proliferation, and migration (Anton et al, 1995;Hadjiargyrou and Patterson, 1995).…”

Section: Abstract: Cd9; Tetraspan Proteins; Antibody Perturbation; Nmentioning

confidence: 99%

“…Cells were viewed and photographed using an inverted Nikon fluorescence microscope (Diaphot 300). S100 immunohistochemistry was performed as described previously (Banerjee and Patterson, 1995), except that the secondary Ab was an anti-rabbit Ab conjugated with FITC (Vector Laboratories, Burlingame, CA) and the stained material was mounted in glycerol containing n-propyl gallate, as described above.…”

Section: Abstract: Cd9; Tetraspan Proteins; Antibody Perturbation; Nmentioning

confidence: 99%

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An Antibody to the Tetraspan Membrane Protein CD9 Promotes Neurite Formation in a Partially α3β1 Integrin-Dependent Manner

1997

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The tetraspan cell surface glycoprotein, CD9, has been implicated in cellular signaling during growth and differentiation in the hematopoietic and nervous systems. Because CD9 expression is induced early in development in sensory and sympathetic neuroblasts, we investigated the role of CD9 in neurite outgrowth. We plated dissociated cells from neonatal sympathetic ganglia on immobilized anti-CD9 antibodies or antibodies against other cell surface molecules. We show here that B2C11, an anti-CD9 antibody that has been shown previously to activate Schwann cells in vitro, promotes robust neurite outgrowth from sympathetic neurons that is greater than that on other antibody surfaces and is comparable to neurite outgrowth on a collagen substratum. In addition, B2C11 causes dramatic morphological changes in neurons and glia from dissociated ganglia, including a flattening of these cells.Because CD9 interacts with integrins in many cell types including Schwann cells, and specifically with the ␣3␤1 integrin in some cells, we tested whether the effect of B2C11 on neurite outgrowth is mediated by this integrin. An anti-␣3␤1 antibody, Ralph 3-1, attenuates the extent of neurite outgrowth on B2C11 and collagen, but not on laminin. Because the ␣3␤1 integrin has been shown to mediate neurite outgrowth on different substrates, these results provide a functional significance for the CD9-␣3␤1 interaction; downstream signaling may be activated by this cis interaction on the cell surface in response to external cues that promote neurite outgrowth.

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Section: Discussionmentioning

confidence: 96%

Section: Discussionmentioning

confidence: 99%

Section: Abstract: Cd9; Tetraspan Proteins; Antibody Perturbation; Nmentioning

confidence: 99%

Section: Abstract: Cd9; Tetraspan Proteins; Antibody Perturbation; Nmentioning

confidence: 99%

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An Antibody to the Tetraspan Membrane Protein CD9 Promotes Neurite Formation in a Partially α3β1 Integrin-Dependent Manner

1997

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“…1). Most of these proteins are likely to represent transmembrane proteins such as the adhesion molecules NCAM and L1, which are downregulated with myelination, and the beta-4 integrin subunit and the tetraspan protein CD9, which are upregulated with axon contact and myelination (Einheber et al, 1993;Banerjee and Patterson, 1995). Marked changes in CAM expression reflect dramatic changes in the anatomic relationships between axons and Schwann cells associated with the transition from ensheathment to myelination (reviewed in Salzer, 1995).…”

Section: Differential Expression Of Cell-surface Proteins During Schwmentioning

confidence: 98%

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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