Distribution of CD9 in the developing and mature rat nervous system

Tole, Shubha; Patterson, Paul H.

doi:10.1002/aja.1001970203

Cited by 43 publications

(55 citation statements)

References 36 publications

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“…They are thus supposed to be "adapters for membrane proteins" or "molecular facilitators" that mediate the formation of large molecular complexes and allow them to function more efficiently. CD9 is one of the best characterized TM4SF members, and a number of studies have suggested that CD9 is involved in cell signaling (21,22), cell growth (6), cell motility (23,24), cell adhesion (25)(26)(27), tumor cell metastasis (28 -30), and development and maintenance of neural system (31)(32)(33)(34). However, despite such fundamental roles, evidence to demonstrate the role of CD9 in molecular complexes is limited.…”

Section: Hb-egf/tgf-␣ Chimericmentioning

confidence: 99%

Importance of the Major Extracellular Domain of CD9 and the Epidermal Growth Factor (EGF)-like Domain of Heparin-binding EGF-like Growth Factor for Up-regulation of Binding and Activity

Nakamura

Mitamura

Takahashi

et al. 2000

Journal of Biological Chemistry

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Heparin-binding epidermal growth factor (EGF)-like growth factor (HB-EGF) is a member of the EGF family of growth factors. The membrane-anchored form of HB-EGF (proHB-EGF) is mitogenically active to neighboring cells as well as being a precursor of the soluble form. In addition to its mitogenic activity, proHB-EGF has the property of binding to diphtheria toxin (DT), serving as the specific receptor for DT. Tetramembrane-spanning protein CD9, a member of the TM4 superfamily, is physically associated with proHB-EGF at the cell surface and up-regulates both mitogenic and DT binding activities of proHB-EGF. To understand this up-regulation mechanism, we studied essential regions of both CD9 and proHB-EGF for up-regulation. Immunoprecipitation experiments revealed that not only CD9 but also other TM4 proteins including CD63, CD81, and CD82 associate with proHB-EGF on the cell surface. However, these TM4 proteins did not up-regulate DT binding activity of proHB-EGF. Transfection of a series of chimeric constructs comprising CD9 and CD81 showed that the major extracellular domain of CD9 is essential for up-regulation. Assays of DT binding activity and juxtacrine mitogenic activity of the deletion mutants of proHB-EGF and chimeric molecules, derived from proHB-EGF and TGF-␣, showed that the essential domain of proHB-EGF for up-regulation is the EGF-like domain. These results indicate that the interaction of the extracellular domains of both molecules is important for up-regulation.

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Section: Hb-egf/tgf-␣ Chimericmentioning

confidence: 99%

Importance of the Major Extracellular Domain of CD9 and the Epidermal Growth Factor (EGF)-like Domain of Heparin-binding EGF-like Growth Factor for Up-regulation of Binding and Activity

Nakamura

Mitamura

Takahashi

et al. 2000

Journal of Biological Chemistry

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“…One of these proteins, CD9, has been recently described in the rat nervous system (Tole and Patterson, 1993;Kaprielian et al, 1995). CD9 interacts in cis (within the membrane of the same cell) with members of the integrin protein family in many cell types, and many of the functions ascribed to CD9 may depend on CD9 -integrin interactions (Higashihara et al, 1985;Slupsky et al, 1989;Letarte et al, 1992;Rubinstein et al, 1994;Nakamura et al, 1995;Shaw et al, 1995).…”

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

confidence: 99%

“…CD9 is also expressed by neurons (Tole and Patterson, 1993;Kaprielian et al, 1995). Although CD9 is not detectable on migrating neural crest cells, expression is upregulated very soon after these cells coalesce into various tissue derivatives (E11-E12 in the rat), and CD9 is found on the surface of neuroblasts in the SCG at E12 and in DRG at E15.…”

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

confidence: 99%

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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“…Increasing evidence suggests that this protein is involved in a variety of functions, such as cell signaling (Tai et al, 1996;Griffith et al, 1991), cell growth , cell motility (Shaw et al, 1995;Schmidt et al, 1996), cell adhesion Anton et al, 1995;Masellis-Smith and Shaw, 1994), tumor cell metastasis (Ikeyama et al, 1993;Miyake et al, 1991;Si and Hersey, 1993), muscle cell formation (Tachibana and Hemler, 1999), development and maintenance of the neural system (Kaprielian et al, 1995;Tole and Patterson, 1993;Nakamura et al, 1996;Kagawa et al, 1997), sperm-egg fusion (Miyado et al, 2000;Le Naour et al, 2000;Kaji et al, 2000) and viral infections (Loffler et al, 1997;Schmid et al, 2000). CD9 forms complexes with a number of membrane proteins which include integrin =3>1 (Nakamura et al, 1995), =6>1 (Berditchevski et al, 1996;Hadjiargyrou et al, 1996), the neural adhesion molecule L1 (Schmidt et al, 1996), CD46 (Lozahic et al, 2000), the membrane-anchored form of heparin-binding EGF-like growth factor (proHB-EGF) (Iwamoto et al, 1994) and other members of the tetraspanins .…”

mentioning

confidence: 99%

Domain Analysis of the Tetraspanins. Studies of CD9/CD63 Chimeric Molecules on Subcellular Localization and Upregulation Activity for Diphtheria Toxin Binding.

Ryu

Takahashi

Nakamura

et al. 2000

Cell Struct. Funct.

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ABSTRACT. CD9 and CD63 belong to a tetramembrane-spanning glycoprotein family called tetraspanin, and are involved in a wide variety of cellular processes, but the structure-function relationship of this family of proteins has yet to be clarified. CD9 associates with diphtheria toxin receptor (DTR), which is identical to the membraneanchored form of heparin-binding EGF-like growth factor (proHB-EGF). CD9 upregulates the diphtheria toxin (DT) binding activity of DTR/proHB-EGF, while CD63 does not upregulate the DT binding activity in spite of the fact that this protein also associates with DTR/proHB-EGF on the cell surface. CD9 molecules localize on the cell surface, while those of CD63 localize predominantly at lysosomes and intracellular compartments. We made CD9/ CD63 chimeric molecules and then studied their intracellular localization and upregulation activities. The C-terminal regions of CD63, which includes the lysosome sorting motif, showed a strong inhibitory effect on the expression of the chimeric proteins at the cell surface, while mutants lacking the lysosome sorting motif delivered more efficiently on the cell surface, indicating that the lysosome sorting motif contributes to the inhibitory effect of the C-terminal region. However, the N-terminal half of this family of proteins containing the 1st to 3rd transmembrane domains also seems to influence the cell surface expression. For the upregulation of DT binding activity the large extracellular loop (EC2) of CD9 was essential, while the remaining regions influenced the upregulation activity by changing the efficiency of cell surface expression. From these results we discussed the structure-function relationship of this family of proteins.

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Distribution of CD9 in the developing and mature rat nervous system

Cited by 43 publications

References 36 publications

Importance of the Major Extracellular Domain of CD9 and the Epidermal Growth Factor (EGF)-like Domain of Heparin-binding EGF-like Growth Factor for Up-regulation of Binding and Activity

Importance of the Major Extracellular Domain of CD9 and the Epidermal Growth Factor (EGF)-like Domain of Heparin-binding EGF-like Growth Factor for Up-regulation of Binding and Activity

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

Domain Analysis of the Tetraspanins. Studies of CD9/CD63 Chimeric Molecules on Subcellular Localization and Upregulation Activity for Diphtheria Toxin Binding.

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