Formation of heterotypic adherens-type junctions between L-CAM-containing liver cells and A-CAM-containing lens cells

Volk, Talila; Cohen, Orna; Geiger, Benjamin

doi:10.1016/0092-8674(87)90525-3

Cited by 114 publications

(63 citation statements)

References 28 publications

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“…These results also showed for the first time the existence of such heterotypic cadherin complexes with common plaque proteins but did not yet allow to distinguish between lateral heterocomplexes in the same membrane from transcellular heterotypic complexes of cadherins (e.g. Volk et al, 1987); that is, from the 'heterocadherins' in the sense used by Duguay et al (Duguay et al, 2003) [for the controversial literature on cadherin organization see Shapiro et al, and others (Shapiro et al, 1995;Leckband and Sivasankar, 2000;Boggon et al, 2002;Ahrens et al, 2003)]. By contrast, ezrin immunoprecipitates contained desmoyokin, periplakin and periaxin (Table 1; Fig.…”

Section: Biochemical Analysismentioning

confidence: 63%

A novel cell-cell junction system: thecortex adhaerensmosaic of lens fiber cells

Straub

Boda

Kühn

et al. 2003

Journal of Cell Science

109

111

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The anucleate prismoid fiber cells of the eye lens are densely packed to form a tissue in which the plasma membranes and their associated cytoplasmic coat form a single giant cell-cell adhesive complex, the cortex adhaerens. Using biochemical and immunoprecipitation methods in various species (cow, pig, rat), in combination with immunolocalization microscopy, we have identified two different major kinds of cortical complex. In one, the transmembrane glycoproteins N-cadherin and cadherin-11 [which also occur in heterotypic (`mixed') complexes] are associated with α- and β-catenin, plakoglobin (proportions variable among species), p120ctn and vinculin. The other complex contains ezrin, periplakin, periaxin and desmoyokin (and so is called the EPPD complex), usually together with moesin, spectrin(s) and plectin. In sections through lens fiber tissue, the short sides of the lens fiber hexagons appear to be enriched in the cadherin-based complexes, whereas the EPPD complexes also occur on the long sides. Moreover, high resolution double-label fluorescence microscopy has revealed, on the short sides, a finer, almost regular mosaicism of blocks comprising the cadherin-based, catenin-containing complexes, alternating with patches formed by the EPPD complexes. The latter, a new type of junctional plaque ensemble of proteins hitherto known only from certain other cell types, must be added to the list of major lens cortex proteins. We here discuss its possible functional importance for the maintenance of lens structure and functions, notably clear and sharp vision.

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Section: Biochemical Analysismentioning

confidence: 63%

A novel cell-cell junction system: thecortex adhaerensmosaic of lens fiber cells

Straub

Boda

Kühn

et al. 2003

Journal of Cell Science

109

111

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“…Chick retina cells mixed with both heart cells (35) and liver cells (36), even though the cells express different cadherins. Although N-and E-cadherindisplaying cells do not cross-react in cell aggregation assays at high mixing speeds (100 rpm) (14), chick lens cells expressing the N-CAD homologue intermixed with liver cells expressing the chicken E-CAD homologue and formed heterotypic cell-cell junctions (35,37). Substituting N-CAD for E-CAD in mouse hearts also resulted in normal development (38).…”

Section: Discussionmentioning

confidence: 99%

Similarities between heterophilic and homophilic cadherin adhesion

Prakasam

Maruthamuthu

Leckband³

2006

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

102

107

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The mechanism that drives the segregation of cells into tissuespecific subpopulations during development is largely attributed to differences in intercellular adhesion. This process requires the cadherin family of calcium-dependent glycoproteins. A widely held view is that protein-level discrimination between different cadherins on cell surfaces drives this sorting process. Despite this postulated molecular selectivity, adhesion selectivity has not been quantitatively verified at the protein level. In this work, molecular force measurements and bead aggregation assays tested whether differences in cadherin bond strengths could account for cell sorting in vivo and in vitro. Studies were conducted with chicken N-cadherin, canine E-cadherin, and Xenopus C-cadherin. Both qualitative bead aggregation and quantitative force measurements show that the cadherins cross-react. Furthermore, heterophilic adhesion is not substantially weaker than homophilic adhesion, and the measured differences in adhesion do not correlate with cell sorting behavior. These results suggest that the basis for cell segregation during morphogenesis does not map exclusively to protein-level differences in cadherin adhesion.cell adhesion ͉ force probe ͉ selectivity ͉ surface forces apparatus B oth the formation of distinct tissues during morphogenesis and the maintenance of adult tissue structure are regulated by adhesive contacts between cells. One family of adhesion proteins, cadherins, is critical to several processes associated with the formation and maintenance of tissues. The genetic regulation of the spatiotemporal expression patterns of cadherins in vivo is believed to play a central role in embryogenesis, cell differentiation, and the maintenance of the multicellular structure of an organism (1-5). One prevalent hypothesis is that differences in adhesion between cells direct cell segregation during morphogenesis, analogous to liquid-liquid phase separation (6). A fundamental unresolved question is whether this sorting out is encoded by protein-specific or cell-specific differences in adhesion. A common hypothesis is that preferential binding between identical cadherins (homophilic) relative to heterophilic binding between dissimilar cadherins induces the cell segregation.Both the adhesive and the selectivity functions of classic cadherins map to the extracellular (EC) region (7), which comprises five tandemly arranged EC domains, EC1-5, numbered from the outermost domain (Fig. 1) (8). Classical cadherins also contain a transmembrane segment and a cytoplasmic domain. Cadherins form multiple bonds that require different EC domains (9-12). A common feature of the classical cadherins is that the N-terminal domains bind by inserting the tryptophan 2 (W2) residue from one protein into a hydrophobic pocket on an opposed N-terminal domain (13-16). However, given the weak adhesion between the outer domains (11, 12), it is questionable whether the tryptophan binding accounts for both cadherin selectivity and robust adhesion.The most extensively ci...

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“…Thus, in a dynamic modification of the "differential adhesion hypothesis" of tissue formation (Steinberg 1962), MSCs in culture or in the embryo may make Ca 2+ -dependent junctional contacts with other cells of the same or a different kind (for the possibility of heterotypic junction formations in cell culture, see Volk et al 1987) and may stabilize them or allow re-dissociation until a developmental optimum of cell sorting, aggregation, and positioning has been reached (e.g., Duguay et al 2003;Perez-Moreno et al 2003). However, although cell-cell interactions and cell sorting have so far been considered primarily as a short-distance nearest-neighbour relationship of recognition and association (e.g., Steinberg 1962;Takeichi 1988;Duguay et al 2003), our findings now demonstrate that cells can (via such processus adhaerentes) also attach to one or several distant cells and bring them into close-packed tissue-forming arrays.…”

Section: Discussionmentioning

confidence: 99%

Processus and recessus adhaerentes: giant adherens cell junction systems connect and attract human mesenchymal stem cells

et al. 2007

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Substrate-adherent cultured cells derived from human bone marrow or umbilical cord blood ("mesenchymal stem cells") are of special interest for regenerative medicine. We report that such cells, which can display considerable heterogeneity with respect to their cytoskeletal protein complement, are often interconnected by special tentacle-like cell processes contacting one or several other cells. These processus adhaerentes, studded with many (usually small) puncta adhaerentia and varying greatly in length (up to more than 400 μm long), either contact each other in the intercellular space ("ET touches") or insert in a tight-fitting manner into deep plasma membrane invaginations (recessus adhaerentes), thus forming a novel kind of long (up to 50 μm) continuous cuff-like junction (manubria adhaerentia). The cell processes contain an actin microfilament core that is stabilized with ezrin, α-actinin, and myosin and accompanied by microtubules, and their adhering junctions are characterized by a molecular complement comprising the transmembrane glycoproteins N-cadherin and cadherin-11, in combination with the cytoplasmic plaque proteins α-and β-catenin, together with p120 ctn , plakoglobin, and afadin. The processes are also highly dynamic and rapidly foreshorten as cell colonies approach a denser state of cell packing. These structures are obviously able to establish cell-cell connections, even over long distances, and can form deep-rooted and tight cell-cell adhesions. The possible relationship to similar cell processes in the embryonic primary mesenchyme and their potential in cell sorting and tissue formation processes in the body are discussed.

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Formation of heterotypic adherens-type junctions between L-CAM-containing liver cells and A-CAM-containing lens cells

Cited by 114 publications

References 28 publications

A novel cell-cell junction system: thecortex adhaerensmosaic of lens fiber cells

A novel cell-cell junction system: thecortex adhaerensmosaic of lens fiber cells

Similarities between heterophilic and homophilic cadherin adhesion

Processus and recessus adhaerentes: giant adherens cell junction systems connect and attract human mesenchymal stem cells

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