Antibody ligation of CD9 modifies production of myeloid cells in long- term cultures

Oritani, Kenji; Wu, Xiying; Medina, Kay L.; Hudson, Jane; Miyake, Kensuke; Gimble, Jeffrey M.; Burstein, Samuel A.; Kincade, Paul W.

doi:10.1182/blood.v87.6.2252.bloodjournal8762252

Cited by 58 publications

(11 citation statements)

References 31 publications

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“…4 were shown previously to inhibit cell functions in vitro. For example, KM114 (reference 48), R1-2 (reference 19), MFR5 (reference 23), and Ha2/5 (reference 46) inhibited cell adhesion, whereas KMC8 and 2F7 inhibited myeloid and T cell development, respectively (references 10, 53).…”

Section: Resultsmentioning

confidence: 99%

Role of Transmembrane 4 Superfamily (Tm4sf) Proteins Cd9 and Cd81 in Muscle Cell Fusion and Myotube Maintenance

Tachibana

Hemler

1999

The Journal of Cell Biology

222

166

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The role of transmembrane 4 superfamily (TM4SF) proteins during muscle cell fusion has not been investigated previously. Here we show that the appearance of TM4SF protein, CD9, and the formation of CD9–β1 integrin complexes were both regulated in coordination with murine C2C12 myoblast cell differentiation. Also, anti-CD9 and anti-CD81 monoclonal antibodies substantially inhibited and delayed conversion of C2C12 cells to elongated myotubes, without affecting muscle-specific protein expression. Studies of the human myoblast-derived RD sarcoma cell line further demonstrated that TM4SF proteins have a role during muscle cell fusion. Ectopic expression of CD9 caused a four- to eightfold increase in RD cell syncytia formation, whereas anti-CD9 and anti-CD81 antibodies markedly delayed RD syncytia formation. Finally, anti-CD9 and anti-CD81 monoclonal antibodies triggered apoptotic degeneration of C2C12 cell myotubes after they were formed. In summary, TM4SF proteins such as CD9 and CD81 appear to promote muscle cell fusion and support myotube maintenance.

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Section: Resultsmentioning

confidence: 99%

Role of Transmembrane 4 Superfamily (Tm4sf) Proteins Cd9 and Cd81 in Muscle Cell Fusion and Myotube Maintenance

Tachibana

Hemler

1999

The Journal of Cell Biology

222

166

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“…A number of the surface markers have been implicated in hematopoietic support. For example, antibodies directed against CD9 (Oritani et al, 1996; Aoyama et al, 1999), CD29 (Jacobsen et al, 1992; Wu et al, 1994), CD44 (Miyake et al, 1990), CD49 d (Miyake et al, 1991a), and CD106 (Miyake et al, 1991b; Funk et al, 1995) interfere with the proliferation and differentiation of hematopoietic stem cells. Preliminary studies indicate that adipose tissue‐derived stromal cells are capable of supporting hematopoiesis in vitro (R.W.S., H.A.L., D.M.F., J.M.G., unpublished observations) in addition to their adipogenic and osteogenic capabilities.…”

Section: Discussionmentioning

confidence: 99%

Surface protein characterization of human adipose tissue‐derived stromal cells

Gronthos¹,

Franklin²,

Leddy³

et al. 2001

Journal Cellular Physiology

958

647

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Human bone marrow stromal cells are a multipotent population of cells capable of differentiating into a number of mesodermal lineages as well as supporting hematopoeisis. Their distinct protein and gene expression phenotype is well characterized in the literature. Human adipose tissue presents an alternative source of multipotent stromal cells. In this study, we have defined the phenotype of the human adipose tissue-derived stromal cells in both the differentiated and undifferentiated states. Flow cytometry and immunohistochemistry show that human adipose tissue-derived stromal cells have a protein expression phenotype that is similar to that of human bone marrow stromal cells. Expressed proteins include CD9, CD10, CD13, CD29, CD34, CD44, CD 49(d), CD 49(e), CD54, CD55, CD59, CD105, CD106, CD146, and CD166. Expression of some of these proteins was further confirmed by PCR and immunoblot detection. Unlike human bone marrow-derived stromal cells, we did not detect the STRO-1 antigen on human adipose tissue-derived stromal cells. Cells cultured under adipogenic conditions uniquely expressed C/EBPalpha and PPARdelta, two transcriptional regulators of adipogenesis. Cells cultured under osteogenic conditions were more likely to be in the proliferative phases of the cell cycle based on flow cytometric analysis of PCNA and Ki67. The similarities between the phenotypes of human adipose tissue-derived and human bone marrow-derived stromal cells could have broad implications for human tissue engineering.

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“…The TM4SF comprises a group of cell surface proteins such as CD81 (21)(22)(23), CD82 (22,24), and CD53 (25), which are characterized by the presence of four hydrophobic domains. The precise biochemical function of the TM4SF is unknown, although recent studies largely suggest a role for this superfamily in the regulation of cell development (26,27), proliferation/activation (26), adhesion (28) and motility (29). Our present results show that CD9, generally as a member of the TM4SF, joins a growing list of molecules responsible for cell activation and specifically in the T cell, delivers a costimulatory signal essential for cell activation (vide infra).…”

Section: Discussionmentioning

confidence: 99%

A role for CD9 molecules in T cell activation.

Tai

Yashiro

Ryo

et al. 1996

The Journal of Experimental Medicine

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SummaryCostimulation mediated by the CD28 molecule plays an important role in optimal activation of T cells. However, CD28-deficient mice can mount effective T cell-dependent immune responses, suggesting the existence of other costimulatory systems. In a search for other costimulatory molecules on T cells, we have developed a monoclonal antibody (mAb) that can costimulate T cells in the absence of antigen-presenting cells (APC). The molecule recognized by this mAb, 9D3, was found to be expressed on almost all mature T cells and to be a protein of ,'-~24 kD molecular mass. By expression cloning, this molecule was identified as CD9. 9D3 (anti-CD9) synergized with suboptimal doses of anti-CD3 mAb in inducing proliferation by virgin T cells. Costimulation was induced by independent ligation of CD3 and CD9, suggesting that colocalization of these two molecules is not required for T cell activation. The costimulation by anti-CD9 was as potent as that by anti-CD28. Moreover, anti-CD9 costimulated in a CD28-independent way because anti-CD9 equally costimulated T cells from the CD28-deficient as well as wild-type mice. Thus, these results indicate that CD9 serves as a molecule on T cells that can deliver a potent CD28-independent costimulatory signal. Full activation of the T cell has been shown to require two independent signals (1). The first signal is provided by antigen-specific T cell receptor (TCR) interacting with processed antigen peptides plus major histocompatibitity complex (MHC) molecules on APC. This signal leads to an effective T cell response only when accompanied by a second costimulatory signal(s) presented by the APC. The lack of costimulation not only prevents activation but also induces tolerance called anergy (1). Identifying molecules capable of delivering costimulatory signals has been the subject of a large number of recent investigations (2-5). CD28 expressed on T cells was found to be a receptor for the costimulatory molecules CD80 and CD86 on APC (6). CD28 engagement, by either anti-CD28 mAb or ligands (CD80/ CD86), has been shown to costimulate T cells in the absence of APC, resulting in T cell activation (7-9). Conversely, the blocking of CD28-1igand interactions induced substantial inhibition of T cell activation (2). These observations indicated that the CD28-CD80/CD86 interaction functions as a critical pathway of T cell costimulation. Nevertheless, recent studies have revealed that CD28-deficient mice can develop normal in vivo immune responses (10) and that T cells from these mice mount APC-dependent responses for T cell activa~:ion in vitro although the response is reduced compared to T cells from wild-type mice (10, 11). Thus, these results strongly suggest that there may exist other molecules capable of providing costimulatory activity.In this report, we have developed a rat IgG mAb (9D3) by immunization with cells of a murine thymic stromal clone (12). This mAb recognized a protein of"-,24 kD that is expressed on immunizing thymic stromal cells as well as murine T cells. By cDNA expr...

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Antibody ligation of CD9 modifies production of myeloid cells in long- term cultures

Cited by 58 publications

References 31 publications

Role of Transmembrane 4 Superfamily (Tm4sf) Proteins Cd9 and Cd81 in Muscle Cell Fusion and Myotube Maintenance

Role of Transmembrane 4 Superfamily (Tm4sf) Proteins Cd9 and Cd81 in Muscle Cell Fusion and Myotube Maintenance

Surface protein characterization of human adipose tissue‐derived stromal cells

A role for CD9 molecules in T cell activation.

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