Zebrafish E‐cadherin: Expression during early embryogenesis and regulation during brain development

Babb, Sherry G.; Barnett, Jessica; Doedens, Andrew L.; Cobb, Nicole; Liu, Qin; Sorkin, Barbara C.; Yelick, Pamela C.; Raymond, Pamela A.; Marrs, James A.

doi:10.1002/dvdy.1132

Cited by 43 publications

(48 citation statements)

References 34 publications

(37 reference statements)

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“…The best candidate to investigate in this context was E-cadherin (cdh1), since it has been shown to play a role in early zebrafish development and to be expressed in both tissues (Babb et al, 2001;Babb and Marrs, 2004;Montero et al, 2005;Solnica-Krezel, 2006;Ulrich et al, 2005). We down-regulated E-cadherin expression in both tissues, using a cdh1-specific morpholino oligonucleotide (MO) (Babb and Marrs, 2004).…”

Section: Reducing Ectoderm Aggregate Surface Tension Results In Phasementioning

confidence: 99%

Quantitative differences in tissue surface tension influence zebrafish germ layer positioning

et al. 2008

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Section: Reducing Ectoderm Aggregate Surface Tension Results In Phasementioning

confidence: 99%

Quantitative differences in tissue surface tension influence zebrafish germ layer positioning

et al. 2008

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“…Synthesis of digoxigenin-labeled cdh1, cdh2, cdh4, and chd11 RNA probes for in situ hybridization was described previously (Liu et al, 1999;Babb et al, 2001;Novince et al, 2003). Detailed procedures for in situ hybridization were reported previously (Liu et al, 1999).…”

Section: Methodsmentioning

confidence: 99%

“…terns of these cadherins have been examined in various tissues and organs, including the central nervous system (Bitzur et al, 1994;Franklin and Sargent, 1996;Kimura et al, 1996;Redies, 1997;Vallin et al, 1998;Liu et al, 1999;Babb et al, 2001), but there is little information on their distribution and function in the developing vertebrate limb.…”

Section: Introductionmentioning

confidence: 99%

Cadherin‐1, ‐2, and ‐11 expression and cadherin‐2 function in the pectoral limb bud and fin of the developing zebrafish

Liu¹,

Kerstetter²,

Azodi³

et al. 2003

Developmental Dynamics

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Cadherins are cell adhesion molecules that play important roles in development of a variety of organs, including the vertebrate limb. In this study, we analyze cadherin expression patterns in the embryonic zebrafish pectoral limb buds and larval pectoral fins by using both in situ hybridization and immunocytochemical methods. cadherin-1 is detected in the epidermis of the embryonic limb buds and the larval pectoral fins. Cadherin-2 is expressed in the pectoral limb bud mesenchyme and chondrogenic condensation. As development proceeds, cadherin-2 expression is detected in newly differentiated pectoral fin endoskeleton, but its expression is greatly down-regulated in the fin endoskeleton of larval zebrafish. cadherin-11 is found in the basal region of the embryonic limb buds and in the proximal endoskeleton of the larval pectoral fins. Interfering with cadherin-2 function using two specific antisense morpholino oligonucleotides disrupts formation of the chondrogenic condensation/endoskeleton, suggesting that cadherin-2 is crucial for the normal development of the zebrafish pectoral fins. Developmental Dynamics 228:734 -739, 2003.

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“…E-cadherin peptides containing the HAV sequence have been shown to induce epithelial cell invasion, implying that the adhesive region flanks the HAV sequence (32). However, there is doubt that this motif is crucial because many nonclassical cadherins, and some classical ones, do not have HAV but are still capable of trans adhesion (33,34).To characterize the role of the HAV motif and of the whole EC1 in adhesion we evaluated the capability of two mutant forms of E-cadherin to mediate adhesion in a set of well defined cell-cell aggregation assays. One mutant has had the conserved HAV motif reversed to VAH, and the other mutant has the entire EC1 domain deleted.…”

mentioning

confidence: 99%

mentioning

confidence: 99%

In the First Extracellular Domain of E-cadherin, Heterophilic Interactions, but Not the Conserved His-Ala-Val Motif, Are Required for Adhesion

Renaud-Young¹,

Gallin

2002

Journal of Biological Chemistry

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The classical cadherins, definitive proteins of the cadherin superfamily, are characterized functionally by their ability to mediate calcium-dependent cell aggregation in vitro. To test hypothetical mechanisms of adhesion, we have constructed two mutants of the chicken E-cadherin protein, one with the highly conserved HisAla-Val (HAV) sequence motif reversed to Val-Ala-His (VAH), the other lacking the first extracellular domain (EC1). The inversion of HAV to VAH has no effect on the capacity of E-cadherin to mediate adhesion. Deletion of EC1 completely eliminates the ability of E-cadherin to mediate homophilic adhesion, but the deletion mutant is capable of adhering heterophilically to both unmutated E-cadherin and to the HAV/VAH mutant. These results demonstrate that the conserved HAV sequence motif is not involved in cadherin-mediated adhesion as has been suggested previously and supports the idea that in the context of the cell surface, cadherin-mediated cell-cell adhesion involves an interaction of EC1 with other domains of the cadherin extracellular moiety and not the "linear zipper" model, which posits trans interactions only between EC1 on apposing cell surfaces.Classical cadherins were defined initially by their ability to mediate calcium-dependent cell-cell adhesion (1-5). Both the extracellular and the intracellular portions of the cadherin play critical roles in mediating adhesion (6). Perturbation and expression experiments have demonstrated that cadherin-mediated adhesion promotes a range of cellular processes subsequent to adhesion, including epithelial polarization (7, 8), blastula compaction (2), neurite outgrowth (9, 10), and formation of desmosomes (11, 12) and gap junctions (13-16).Classical cadherin proteins at the cell surface consist of five extracellular domains (ECs), 1 a transmembrane sequence, and a cytoplasmic domain (Fig. 1). Each cadherin extracellular domain shares a folding topology of seven ␤-strands arranged in two ␤-sheets forming a barrel with hydrophobic amino acid side chains largely sequestered within the interior (17-20). The amino and carboxyl termini emerge from opposite ends of each folded domain, maintaining an orientation with the amino terminus directed away from the cell. Conserved amino acid residues that are capable of coordinating calcium ions are present at the ends of each barrel (17)(18)(19)(20). Binding of calcium at these sites maintains the structural integrity of the cadherin ECs, giving the protein a rigid conformation that allows it to mediate cell-cell adhesion. A single amino acid substitution in a calcium binding site between EC1 and EC2 or between EC2 and EC3 can abolish adhesion and increase motility, whereas mutations in other calcium-binding elements do not affect these behaviors (21,22).Cadherins expressed on adjacent cells homoassociate through an antiparallel, trans, interaction of their extracellular regions. The bonds that they form across the intercellular space hold the plasma membranes of adjacent cells in close proximity. Adhesive strength...

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Zebrafish E‐cadherin: Expression during early embryogenesis and regulation during brain development

Cited by 43 publications

References 34 publications

Quantitative differences in tissue surface tension influence zebrafish germ layer positioning

Quantitative differences in tissue surface tension influence zebrafish germ layer positioning

Cadherin‐1, ‐2, and ‐11 expression and cadherin‐2 function in the pectoral limb bud and fin of the developing zebrafish

In the First Extracellular Domain of E-cadherin, Heterophilic Interactions, but Not the Conserved His-Ala-Val Motif, Are Required for Adhesion

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