Novel function of the cell adhesion molecule uvomorulin as an inducer of cell surface polarity

McNeill, Helen; Ozawa, Masayuki; Kemler, Rolf; Nelson, W. James

doi:10.1016/0092-8674(90)90368-o

Cited by 411 publications

(230 citation statements)

References 42 publications

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“…Cell polarity is also important in regulating permeability, and for maintaining protein and lipid differences between apical and basolateral membranes (Molitoris & Nelson, 1990). Although the process by which differentiation of epithelium occurs is not fully understood, it is known that several factors, such as type I collagen (Zuk et al, 1989) and uvomorulin, an epithelial cell adhesion molecule which mediates cell-cell interactions (Gumbiner et al, 1988), influence cell polarity (Behrens et al, 1989;McNeill et al, 1990). The loss of tight junction formation in PI cells may be the result of virus-mediated loss of uvomorulin.…”

Section: Discussionmentioning

confidence: 99%

Infection of a polarized epithelial cell line with wild-type reovirus leads to virus persistence and altered cellular function

Montgomery

Yang

Verdin

et al. 1991

Journal of General Virology

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Section: Discussionmentioning

confidence: 99%

Infection of a polarized epithelial cell line with wild-type reovirus leads to virus persistence and altered cellular function

Montgomery

Yang

Verdin

et al. 1991

Journal of General Virology

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“…E-cadherin is a cell adhesion molecule known to play an essential role in epithelial cell di erentiation and, like C-CAM, its expression is often decreased in tumors of epithelial origin (McNeill et al, 1990;Takeichi, 1991). Restoration of expression is associated with diminished invasiveness and metastasis in a large variety of epithelial cancers (Foty and Steinberg, 1997;Mareel et al, 1992;Miyaki et al, 1995).…”

Section: Expression Of C-cam1 In Vivo and In Vitromentioning

confidence: 99%

C-CAM1 expression: Differential effects on morphology, differentiation state and suppression of human PC-3 prostate carcinoma cells

et al. 1999

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“…E-cadherin colocalizes with spectrin, and it coisolates with spectrin and ankyrin in extracts of epithelial cells (Nelson and Hammerton, 1989). Moreover, expression of E-cadherin induces a polarized distribution of spectfin and ankyrin to sites of cell-cell contact (McNeill et al, 1990). E-cadherin was localized at cell-cell junctions of cells expressing the ankyrin-binding domain of beta,rspectrin, even though these cells had lost other aspects of epithelial morphology (Fig.…”

Section: Localization Of Actin Ankyrin Adducin Na+k+-atpase and mentioning

confidence: 99%

Expression of functional domains of beta G-spectrin disrupts epithelial morphology in cultured cells.

Moorthy

Bennett

1995

The Journal of Cell Biology

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Abstract. Spectrin is a major structural protein associated with the cytoplasmic surface of plasma membranes of many types of cells. To study the functions of spectrin, we transfected Caco-2 intestinal epithelial cells with a plasmid conferring neomycin resistance and encoding either actin-binding or ankyrin-binding domains of beta~-spectrin fused with beta-galactosidase. These polypeptides, in principle, could interfere with the interaction of spectrin with actin or ankyrin, as well as block normal assembly of alpha-and betaspectrin subunits. Cells expressing the fusion proteins represented only a small fraction of neomycin-resistant cells, but they could be detected based on expression of beta-galactosidase. Cells expressing spectrin domains exhibited a progressive decrease in amounts of endogenous betac-spectrin, although alpha-spectrin was still present. Betac-spectrin-deficient cells lost epithelial cell morphology, became multinucleated, and eventually disappeared after 10-14 d in culture. Spectrin-associated membrane proteins, ankyrin and adducin, as well as the Na÷,K÷-ATPase, which binds to ankyrin, exhibited altered distributions in cells transfected with betac-spectrin domains. E-cadherin and F-actin, in contrast to ankyrin, adducin, and the Na÷,K÷-ATPase, were expressed, and they exhibited unaltered distribution in betao-spectrin-deficient cells. Cells transfected with the same plasmid encoding betagalactosidase alone survived in culture as the major population of neomycin-resistant cells, and they exhibited no change in morphology or in the distribution of spectrin-associated membrane proteins. These results establish that betac-spectrin is essential for the normal morphology of epithelial cells, as well as for their maintenance in monolayer culture. S PV.CTRIN is an elongated actin-binding protein that is the principal component of a system of structural proteins associated with the cytoplasmic surface of plasma membranes of most metazoan cells (reviewed by Bennett and Gilligan, 1993). Spectrin is comprised of two subunits, termed alpha and beta, that are aligned side-to-side to form heterodimers, and the dimers are linked head-to-head to form tetramers. Beta subunits contain most of the recognition sites of spectrin for other proteins including ankyrin, protein 4.1 actin, as well as the site for ankyrin-independent association of spectrin with membranes. Beta~-spectrin is the most common type of beta subunit, and it is expressed in most vertebrate tissues (Hu et al., 1992). The structure and function of spectrin has been best characterized in mammalian erythrocytes from both in vivo and in vitro studies (Palek and Lambert, 1990;Delaunay and Dhermy, 1993;Gallagher and Forget, 1993;Bennett and Gilligan, 1993). Erythrocyte spectrin forms a membrane-associated polygonal network by the associations of spectrin with actin illaments and with integral membrane proteins through linkages with ankyrin and protein 4.1. Defects and deficiencies in components of the spectrin-actin network result in abnormally fr...

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Novel function of the cell adhesion molecule uvomorulin as an inducer of cell surface polarity

Cited by 411 publications

References 42 publications

Infection of a polarized epithelial cell line with wild-type reovirus leads to virus persistence and altered cellular function

Infection of a polarized epithelial cell line with wild-type reovirus leads to virus persistence and altered cellular function

C-CAM1 expression: Differential effects on morphology, differentiation state and suppression of human PC-3 prostate carcinoma cells

Expression of functional domains of beta G-spectrin disrupts epithelial morphology in cultured cells.

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