Polarized Expression of HD1: Relationship with the Cytoskeleton in Cultured Human Colonic Carcinoma Cells

Fontao, Lionel; Dirrig, Sylvie; Owaribe, Katsushi; Kédinger, Michèle; Launay, Jean-François

doi:10.1006/excr.1996.3465

Cited by 34 publications

(33 citation statements)

References 42 publications

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“…Aside of the IFs extending along the lateral membrane, a faint but distinct basal network was originally shown by Franke and coworkers at the basal pole of enterocytes [22] (Fig. 1C, arrowhead), and may be related to the presence of hemidesmosomes [40]. Alternatively, it has been shown that focal adhesions may act polymerizing keratin IFs [41].…”

Section: Location Location Location: Apical Distribution Of Intermementioning

confidence: 76%

Intermediate filaments: A role in epithelial polarity

Oriolo

Wald

Palau

et al. 2007

Experimental Cell Research

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Intermediate filaments have long been considered mechanical components of the cell that provide resistance to deformation stress. Practical experimental problems, including insolubility, lack of good pharmacological antagonists, and the paucity of powerful genetic models, have handicapped the research of other functions. In single-layered epithelial cells, keratin intermediate filaments are cortical, either apically polarized or apico-lateral. This review analyzes phenotypes of genetic manipulations of simple epithelial cell keratins in mice and C. elegans that strongly suggest a role of keratins in apico-basal polarization and membrane traffic. Published evidence that intermediate filaments can act as scaffolds for proteins involved in membrane traffic and signaling is also discussed. Such a scaffolding function would generate a highly polarized compartment within the cytoplasm of simple epithelial cells. While in most cases mechanistic explanations for the keratinnull or overexpression phenotypes are still missing, it is hoped investigators will be encouraged to study these as yet poorly understood functions of intermediate filaments.

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Section: Location Location Location: Apical Distribution Of Intermementioning

confidence: 76%

Intermediate filaments: A role in epithelial polarity

Oriolo

Wald

Palau

et al. 2007

Experimental Cell Research

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“…Double staining for α6β4 and the actin cytoskeleton revealed co-localization of these 2 molecules mainly in spikes and filipodia (data not shown). Although in epithelial cells α6β4 was described not to associate with the actin cytoskeleton (Fontao et al, 1997;Grassi et al, 1999), such an association has been seen in, for example, transfected fibroblasts .…”

Section: Discussionmentioning

confidence: 99%

The association of the tetraspanin D6.1A with the α6β4 integrin supports cell motility and liver metastasis formation

Herlevsen

Schmidt

Miyazaki

et al. 2003

Journal of Cell Science

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The metastatic subline of a rat pancreatic adenocarcinoma differs from the non-metastasizing subline by overexpression of 5 membrane molecules: CD44 variant isoforms, EpCAM, the tetraspanin D6.1A, an uPAR-related molecule and, as described here, the α6β4 integrin.An antibody-defined molecule was identified by mass spectrometry and cloning as α6β4 integrin. Transfectioninduced expression of α6β4 in the non-metastasizing subline did not support migration on laminin 5 or tumor progression. However, when the non-metastasizing subline was doubly transfected to express α6β4 and the D6.1A tetraspanin, intraperitoneally injected tumor cells frequently formed liver metastasis. For the following reasons we assume that metastasis formation is supported by an interaction between α6β4 and D6.1A. (i) The 2 molecules can associate and co-localize. (ii) Co-localization is strengthened by PKC stimulation. (iii) PKC stimulation, which induces a migratory phenotype, leads to a redistribution of α6β4/D6.1A complexes. In resting cells, the molecules co-localize at the trail of the cell; during PKC stimulation they become transiently internalized and are (re-)expressed in the leading lamella. Thus, in the appropriate milieu, i.e. intraperitoneally, α6β4 changes from an adhesion-supporting towards a migrationsupporting molecule by its association with a tetraspanin. The findings provide a convincing experimental explanation for the repeatedly described involvement of α6β4 in tumor progression.Key words: α6β4 integrin, Tetraspanin, Metastasis, Adhesion, Motility SummaryThe association of the tetraspanin D6.1A with the α6β4 integrin supports cell motility and liver metastasis formation

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“…In contrast, laminin-332/α6β4 integrin complexes nucleate the assembly of hemidesmosomes in stratified squamous epithelial tissues and in some glands whereas in simple epithelial cells such as those that line the gut the same complex assembles into a variant of the hemidesmosome (a "type II hemidesmosome") ( Fig. 2) [30,31]. Hemidesmosomes are considered to mediate more stable anchorage of cells to their ECM than focal contacts [32,33].…”

Section: Subunits and Assembly Of Matrix Adhesive Complexesmentioning

confidence: 99%

Laminin-332-Integrin Interaction: A Target For Cancer Therapy?

Tsuruta

Kobayashi²,

Imanishi³

et al. 2008

CMC

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For many years, extracellular matrix (ECM) was considered to function as a tissue support and filler. However, we now know that ECM proteins control many cellular events through their interaction with cell-surface receptors and cytoplasmic signaling pathways. For example, they regulate cell proliferation, cell division, cell adhesion, cell migration, and apoptosis. We focus in this review on a laminin isoform, laminin-332 (formerly termed laminin-5), a major component of the basement membrane (BM) of skin and other epithelial tissues. It is composed of 3 subunits (α3, β3, and γ2) and interacts with at least two integrin receptors expressed by epithelial cells (α3β1 and α6β4 integrin). Mutations in either laminin-332 or integrin α6β4 result in junctional epidermolysis bullosa, a blistering skin disease, while targeting of laminin-332 by autoantibodies in cicatricial pemphigoid leads to dysadhesion of epithelial cells from their underlying connective tissue. Abnormal expression of laminin-332 and its integrin receptors is also a hallmark of certain tumor types and is believed to promote invasion of colon, breast and skin cancer cells. Moreover, there is emerging evidence that laminin-332 and its protease degradation products are not only found at the leading front of several tumors but also likely induce and/or promote tumor cell migration. Thus, in this review, we focus specifically on the role of laminin-332 and its integrin receptors in adhesion, proliferation, and migration/invasion of cancer cells. Finally, we discuss strategies for the development of laminin-332-based antagonists for the treatment of malignant tumors.

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Polarized Expression of HD1: Relationship with the Cytoskeleton in Cultured Human Colonic Carcinoma Cells

Cited by 34 publications

References 42 publications

Intermediate filaments: A role in epithelial polarity

Intermediate filaments: A role in epithelial polarity

The association of the tetraspanin D6.1A with the α6β4 integrin supports cell motility and liver metastasis formation

Laminin-332-Integrin Interaction: A Target For Cancer Therapy?

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