Identification of a Role for the Sialomucin CD164 in Myogenic Differentiation by Signal Sequence Trapping in Yeast

Lee, Youl-Nam; Kang, Jong‐Sun; Krauss, Robert M.

doi:10.1128/mcb.21.22.7696-7706.2001

Cited by 17 publications

(22 citation statements)

References 51 publications

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“…Therefore, altered localization of the Itm2A protein could also occur upon induction of differentiation. When expressed on the plasma membrane, Itm2A could be implicated in cellcell interactions, leading to enhanced differentiation potential, analogous to the sialomucin CD164 protein, for example (Lee et al, 2001). When E4 thymoma cells were induced with ionomycin or PMA, a portion of Itm2A moved from intracellular organelles to the plasma membrane (Kirchner and Bevan, 1999), supporting this hypothesis.…”

Section: Discussionmentioning

confidence: 79%

Constitutive overexpression of the integral membrane protein Itm2A enhances myogenic differentiation of C2C12 cells

plas

Merregaert

2004

Cell Biology International

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Integral membrane protein 2A (Itm2A) is a transmembrane protein belonging to a family composed of at least two other members, Itm2B and Itm2C, all of them having a different expression pattern. The protein serves as a marker for early stages in chondrogenesis and T-cell development. Itm2A is also highly expressed in skeletal muscle. In order to understand the role of Itm2A in muscle development, we constitutively overexpressed exogenous Itm2A in C2C12 myoblast cells. Several clones expressing high levels of Itm2a were isolated and characterized. Overexpression was associated with enhanced tube formation and the appearance of multinuclear cells. Gene expression analysis demonstrated that muscle creatin kinase was upregulated in the presence of exogenous Itm2A. Interestingly, proliferation rates were not altered in the undifferentiated myoblast C2C12 cells. These results demonstrate that overexpression of Itm2a in C2C12 enhances myogenic differentiation in vitro.

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Section: Discussionmentioning

confidence: 79%

Constitutive overexpression of the integral membrane protein Itm2A enhances myogenic differentiation of C2C12 cells

plas

Merregaert

2004

Cell Biology International

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“…Recent work has established that culture medium conditioned with a bacterial sialidase inhibits expression of MyoD and the myogenic program in C2C12 cells [13]. In order to determine whether high lysosomal sialidase activity is similarly capable of reducing cell surface sialylation, FACS analysis was performed on differentiating C2C12 cells transduced with Ad-Sial nor .…”

Section: Overexpression Of Lysosomal Sialidase Inhibits Myogenic Diffmentioning

confidence: 99%

“…For example, the cell-surface sialomucin CD164/ endolyn is involved in the differentiation of C2C12 and F3 myoblasts, an activity that disappeared following treatment of cells with a bacterial sialidase [13]. Myoblast cell lines such as C2C12 serve as an excellent model system in 0014 which to study the processes of cellular differentiation and fusion.…”

Section: Introductionmentioning

confidence: 99%

Overexpression of MyoD-inducible lysosomal sialidase (neu1) inhibits myogenesis in C2C12 cells

Champigny¹,

Perry²,

Rudnicki³

et al. 2005

Experimental Cell Research

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“…3C). Full-length N-cadherin was coexpressed with CDO-Fc, BOC-Fc, or (as a control) CD164-Fc, a fusion protein harboring the ectodomain of the promyogenic cell-surface sialomucin, CD164 (22). Cell lysates then were precipitated with protein A-Sepharose to bring down the Fc fusion proteins and immunoblotted with antibodies to cadherin.…”

Section: Colocalization Of Cdo and Boc With Cadherins In C2c12 Myoblamentioning

confidence: 99%

Promyogenic members of the Ig and cadherin families associate to positively regulate differentiation

Kang

Feinleib

Knox

et al. 2003

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

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Determination and differentiation of cells in the skeletal muscle lineage is positively regulated by cell-cell contact. Cell-surface proteins proposed to mediate this effect include both classical cadherins and Ig superfamily members; potential interactions between the promyogenic activities of these classes of protein, however, are unknown. We show here that CDO and BOC, two promyogenic Ig superfamily members that bind to each other in a cis fashion, form complexes with N-and M-cadherin. These complexes contain ␤-catenin and are enriched at sites of cell-cell contact between myoblasts. In transient expression assays, the ectodomains and intracellular regions of CDO, BOC, and N-cadherin each interact independently, suggesting that the interactions occur in a cis fashion; consistent with this conclusion, cadherin-mediated cell adhesion is not required for them to occur. Stable expression in myoblasts of a CDO deletion mutant deficient in its ability to associate with N-cadherin interferes with differentiation as assessed by biochemical, morphological, and reporter gene assays, suggesting that this interaction is functionally important in myogenesis. Thus, some of the cell-cell contact-mediated activities that are required for myogenesis seem to be based on interdependent activities of promyogenic classical cadherins and Ig superfamily members. Many types of cell-cell communication require the formation of intimate intercellular contacts (1). Cadherins play a key role in mediating such phenomena, because they are centrally involved in establishing cell-cell adhesive structures. Furthermore, cadherin-based adhesion can activate signaling pathways via two nonmutually exclusive mechanisms: (i) control of the ability of juxtacrine signaling ligands and receptors to make intercellular connections and (ii) direct regulation of signaling processes (1, 2). Among the numerous cellular activities that are regulated by cadherins is cell differentiation (1).Skeletal myogenesis is viewed as a paradigm for understanding the molecular events that link cell-lineage determination, cell differentiation, and tissue-specific gene expression (3, 4). Interestingly, determination and differentiation of cells in the skeletal muscle lineage is positively regulated by cell-cell contact (5-7). Several cadherins have been implicated in this process including N-, M-, and R-cadherin. N-cadherin has been studied most extensively; several lines of evidence indicate that it plays a positive role in skeletal myogenesis. Expression of a dominantnegative form of N-cadherin in early Xenopus laevis embryos suppresses expression of the myogenic transcription factor, MyoD, in muscle progenitor cells (8). Furthermore, several different function-perturbing antibodies to N-cadherin inhibit myogenic differentiation in vitro of chick primitive streak epiblast cells (9), primary chicken embryo myoblasts (10), and C2C12 murine myoblasts (11). Conversely, incubation of C2C12 and other myoblast cell lines with beads coated with recombinant N-cadherin extracellul...

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Identification of a Role for the Sialomucin CD164 in Myogenic Differentiation by Signal Sequence Trapping in Yeast

Cited by 17 publications

References 51 publications

Constitutive overexpression of the integral membrane protein Itm2A enhances myogenic differentiation of C2C12 cells

Constitutive overexpression of the integral membrane protein Itm2A enhances myogenic differentiation of C2C12 cells

Overexpression of MyoD-inducible lysosomal sialidase (neu1) inhibits myogenesis in C2C12 cells

Promyogenic members of the Ig and cadherin families associate to positively regulate differentiation

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