Ksp-cadherin is a functional cell–cell adhesion molecule related to LI-cadherin

Mw, Wendeler; Praus, Michael; Jung, R.; Hecking, M; C, Metzig; Geßner, Reinhard

doi:10.1016/j.yexcr.2003.11.022

Cited by 29 publications

(37 citation statements)

References 36 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Furthermore, Ksp-and LI-cadherin are expressed in highly resorptive epithelia of the kidney and the intestine, respectively [34,35]. They mediate cell-cell adhesion, induce a particular cellular phenotype and are not linked via β-catenin to the actin cytoskeleton [36,37]. To address the question of a common phylogenetic origin of both genes indicated by protein structure comparison, we analyzed in detail the mouse Ksp-and LI-cadherin genes as well as their chromosomal environment.…”

Section: Discussionmentioning

confidence: 99%

“…To isolate the mouse Ksp-cadherin gene, two PCR-labeled probes derived from the mouse Ksp-cadherin cDNA [37] were used for the screening of macroarrays from a mouse cosmid library. Three cosmid clones (MPMGc121-P1413Q3, -E13108Q2, and -D02293Q2) each containing the complete genomic sequence of the Ksp-cadherin gene were isolated.…”

Section: Gene Structure Comparison Of Ksp-and Li-cadherinmentioning

confidence: 99%

“…2). The position of the exon-intron boundaries were localized by comparing the genomic sequence of Ksp-cadherin with the corresponding cDNA sequences [37,43]. When in doubt, the general rules for splice site consensus sequences were used to define their EC1-EC7, extracellular cadherin homology repeats; TM, transmembrane domain; CP, cytoplasmic region.…”

Section: Gene Structure Comparison Of Ksp-and Li-cadherinmentioning

confidence: 99%

“…Both proteins consist of seven extracellular cadherin repeats and a rather short cytoplasmic domain comprising only about 25 amino acids. Their cytoplasmic domains share no homology to that of classical cadherins and appear not to bind to β-catenin [36,37]. Neither Ksp-nor LI-cadherin contain an N-terminal propeptide, which is a characteristic feature of immature classical cadherins [38].…”

Section: Introductionmentioning

confidence: 99%

“…In addition, as draft genome assemblies have become available for several teleost fish species, we sought to clarify the evolution of Ksp-and LI-cadherin genes by exploiting this information. [37] were generated by PCR labeling (DIG PCR Labeling Kit; Roche, Mannheim, Germany) using specific forward (5′-GCACTTCTGCCACTGTTGTGATCC-3′ and 5′-TGGAGGAGACGTGCACTAC-3′) and reverse primers (5′-CCACCTTGCGCATACATTG-3′ and 5′-TGATCCT-GCTAGGTCAACAGCCAGC-3′), respectively. Probes were detected with anti-digoxigenin Fab fragments conjugated to alkaline phosphatase, and visualized by incubation with the chemiluminescent substrate CSPD ® (Roche, Germany) according to the manufacturer's protocol.…”

Section: Introductionmentioning

confidence: 99%

See 4 more Smart Citations

Unique gene structure and paralogy define the 7D-cadherin family

Wendeler

Jung

Himmelbauer

et al. 2006

Cell. Mol. Life Sci.

View full text Add to dashboard Cite

Abstract. Cadherins are Ca 2+ -dependent transmembrane glycoproteins crucial for cell-cell adhesion in vertebrates and invertebrates. Classification of this superfamily due to their phylogenetic relationship is currently restricted to three major subfamilies: classical, desmosomal and protocadherins. Here we report evidence for a common phylogenetic origin of the kidney-specific Ksp-(Cdh16) and the intestine-specific LI-cadherin (Cdh17). Both genes consist of 18 exons and the positions of their exon-intron boundaries as well as their intron phases are perfectly conserved. We found an extensive paralogy of more than 40 megabases in mammals as well as teleost fish species encompassing the Ksp-and LI-cadherin genes. A comparable paralogy was not detected for other cadherin gene loci. These findings suggest that the Ksp-and LI-cadherin genes originated by chromosomal duplication early during vertebrate evolution and support our assumption that both proteins are paralogues within a separate cadherin family that we have termed 7D-cadherins.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Gene Structure Comparison Of Ksp-and Li-cadherinmentioning

confidence: 99%

Section: Gene Structure Comparison Of Ksp-and Li-cadherinmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Unique gene structure and paralogy define the 7D-cadherin family

Wendeler

Jung

Himmelbauer

et al. 2006

Cell. Mol. Life Sci.

View full text Add to dashboard Cite

show abstract

Quantitative and Robust Assay to Measure Cell–Cell Contact Assembly and Maintenance

Nola

Erasmus

Braga

2011

Methods in Molecular Biology

View full text Add to dashboard Cite

Epithelial junction formation and maintenance are multistep processes that rely on the clustering of macromolecular complexes. These events are highly regulated by signalling pathways that involve Rho small GTPases. Usually, when analysing the contribution of different components of Rho-dependent pathways to cell-cell adhesion, the localisation of adhesion receptors at junctions is evaluated by immunofluorescence. However, we find that this method has limitations on the quantification (dynamic range), ability to detect partial phenotypes and to differentiate between the participation of a given regulatory protein in assembly and/or maintenance of cell-cell contacts.In this chapter, we describe a suitable method, the aggregation assay, in which we adapted a quantitative strategy to allow objective and reproducible detection of partial phenotypes. Importantly, this methodology estimates the ability of cells to form junctions and their resistance to mechanical shearing forces (stabilisation).

show abstract