A cell surface glycoprotein involved in the compaction of embryonal carcinoma cells and cleavage stage embryos

Hyafil, François; Morello, Dominique; Babinet, Charles; Jacob, François

doi:10.1016/0092-8674(80)90456-0

Cited by 401 publications

(186 citation statements)

References 16 publications

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“…It is known that E-cadherin plays a major role in cell-cell contact of epithelial cells (Hyafil et al, 1980). Indeed, an anti-E-cadherin antibody could completely inhibit the formation of compact cell aggregates in Csk K þ cells (Figure 5a), suggesting that SFK activity under the control of Csk is involved in the regulation of E-cadherin-mediated cell-cell contacts.…”

Section: Modulation Of Sfk By Csk Does Not Affect the E-cadherin/b-camentioning

confidence: 92%

Csk defines the ability of integrin-mediated cell adhesion and migration in human colon cancer cells: implication for a potential role in cancer metastasis

et al. 2004

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Progression of human colon cancer is often associated with elevated expression and activity of the Src family tyrosine kinase (SFK). SFK is ordinarily in equilibrium between inactive and primed states by a balance of negative regulatory kinase Csk and its counteracting tyrosine phosphatase(s), both of which act on the regulatory C-terminal tyrosine of SFK. To evaluate the contribution of the regulatory system of SFK in cancer progression, we here modulated the equilibrium status of SFK by introducing wild-type or dominant-negative Csk in human epithelial colon cancer cells, HCT15 and HT29. Overexpression of wild-type Csk induced decreased SFK activation, increased cell-cell contacts mediated by E-cadherin, decreased the number of focal contacts and decreased cell adhesion/migration and in vitro invasiveness. Conversely, expression of a dominant-negative Csk resulted in elevated SFK activation, enhanced phosphorylation of FAK and paxilllin, enhanced cell scattering, an increased number of focal contacts, dramatic rearrangement of actin cytoskeleton and increased cell adhesion/ migration and in vitro invasiveness. In these scattered cells, however, localization, expression and phosphorylation of either E-cadherin or b-catenin were not significantly affected, suggesting that the E-cadherin-mediated cell-cell contact is indirectly regulated by SFK. Furthermore, all these events occurred absolutely dependent on integrin-mediated cell adhesion. These findings demonstrate that Csk defines the ability of integrin-SFKmediated cell adhesion signaling that influences the metastatic potential of cancer cells.

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Section: Modulation Of Sfk By Csk Does Not Affect the E-cadherin/b-camentioning

confidence: 92%

Csk defines the ability of integrin-mediated cell adhesion and migration in human colon cancer cells: implication for a potential role in cancer metastasis

et al. 2004

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“…For example, differential localization of N-, E-(L-CAM), and, very recently R-, B-, and T-cadherins has been described in the chick embryo Duband et al, 1987Duband et al, , 1988Thiery et al, 1984;Inuzuka et al, 1991a,b;Napolitano et al, 1991;Ranscht and Bronner-Fraser, 1991). Likewise, during mouse development N-, E-, P-, or M-cadherins are expressed in a selective manner (Hatta and Takeichi, 1986;Hyafil et al, 1980;Nose and Takeichi, 1986;Donalies et al, 1991).…”

Section: Introductionmentioning

confidence: 99%

N‐cadherin transcripts in Xenopus laevis from early tailbud to tadpole

Simonneau

Broders

Thiery

1992

Developmental Dynamics

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Cadherins are Ca+ +-dependent cell adhesion molecules which play a key role in morphogenesis and histogenesis. T w o mRNAs clones (8 and 9) corresponding to two N-cadherin pseudo-allelic genes are present in Xenopus Zaeuis. We report here that these transcripts share a highly homologous coding region but diverge in the non-coding region. We have determined the pattern of N-cadherin expression at the mRNA level by in situ hybridization with a riboprobe complementary to the EC5 domain of Xenopus Ncadherin clone 8. This part of the sequence is the least conserved in the cadherin gene family, minimizing the risk of cross-hybridization to other cadherins. N-cadherin transcripts are not detectable in the first stages of development. Expression first appears in the neural plate and reaches its maximum level in the CNS at tailbud stage. From early tadpole, it diminishes, so that a very weak signal is detected in the premetamorphic frog brain. N-cadherin expression is not uniform within the CNS, with some areas such as the roof of the rhombencephalon and the olfactory bulbs expressing higher levels of the transcripts. N-cadherin is present in several mesodermal derivatives such as the notochord, the pronephros, and the heart. It is, however, virtually absent from the myotomes and appears in skeletal muscles at later stages of differentiation. All placodes express high levels of N-cadherin. The non-neural ectoderm and the endoderm are always negative. In the brain and the heart, high levels of hybridization are observed with probes corresponding to both copies of the N-cadherin pseudo-allelic genes in their 5' non-coding region, indicating that both alleles are transcribed. o 1992 Wiley-Liss, Inc.

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“…The cell adhesion molecule uvomorulin is involved in the compaction process of mouse preimplantation embryos and the aggregation of embryonal carcinoma cells (2,3). In postimplantation embryos and in adult tissues, uvomorulin is exclusively expressed in epithelial cells (4); in particular, it is concentrated in the intermediate junctions of the intestine epithelial cell layer (5).…”

mentioning

confidence: 99%

Chromosomal mapping of the structural gene coding for the mouse cell adhesion molecule uvomorulin.

Eistetter

Adolph

Ringwald

et al. 1988

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

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The gene coding for the mouse cell adhesion molecule uvomorulin has been mapped to chromosome 8. Uvomorulin cDNA clone F5113 identified restriction fragment length polymorphisms in Southern blots of genomic DNA from mouse species Mus musculus domesticus and Mus spretus. By analyzing the segregation pattern of the gene in 75 offspring from an interspecific backcross a single genetic locus, Um, was dermed on chromosome 8. Recombination frequency between UM and the co-segregating loci serum esterase 1 (Es-i) and tyrosine aminotransferase (Tat) places Um about 14 centimorgan (cM) distal to Es-i, and 5 cM proximal to Tat. In situ hybridization of uvomorulin [3H]cDNA to mouse metaphase chromosomes located the Um locus close to the distal end of chromosome 8 (bands C3-E1). Since uvomorulin is evolutionarily highly conserved, its chromosomal assignment adds an important marker to the mouse genetic map.

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A cell surface glycoprotein involved in the compaction of embryonal carcinoma cells and cleavage stage embryos

Cited by 401 publications

References 16 publications

Csk defines the ability of integrin-mediated cell adhesion and migration in human colon cancer cells: implication for a potential role in cancer metastasis

Csk defines the ability of integrin-mediated cell adhesion and migration in human colon cancer cells: implication for a potential role in cancer metastasis

N‐cadherin transcripts in Xenopus laevis from early tailbud to tadpole

Chromosomal mapping of the structural gene coding for the mouse cell adhesion molecule uvomorulin.

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