Title: Cadherins
Literature References: Family of calcium-dependent cell adhesion molecules thought to be key regulators of morphogenesis in vertebrates. Transmembrane glycoproteins; mol wt ~120-140 kDa. Mediate tissue development by connecting cells bearing identical cadherin types via homophilic interactions. Loss of cadherin function has been associated with tumor metastasis. Two subfamilies have been identified: classic cadherins and the desmosomal cadherins, known as desmocollins and desmogleins, which differ from the classic cadherins primarily in the structure of the cytoplasmic domains. A number of classic cadherins have been identified; nomenclature is based on the cell from which they were first identified, e.g. E-, N- and P-cadherins from epithelial, neural, and placental cells, resp. Among subclasses, ~50% of amino acids are conserved within a particular species. Classic cadherins are complexed with cytoplasmic proteins known as catenins which anchor them to the actin-based cytoskeleton and are required for adhesive function. Review of discovery and characterization of cadherins: M. Takeichi, Development 102, 639-655 (1988); idem, Annu. Rev. Biochem. 59, 237-252 (1990); of properties and role in morphogenesis: idem, Science 251, 1451-1455 (1991); J. Behrens, Acta Anat. 149, 165-169 (1994). Review of interaction with catenins: R. Kemler, Trends Genet. 9, 317-321 (1993); L. Hinck et al., Trends Biochem. Sci. 19, 538-542 (1994). Review of role in tumor metastasis: M. Takeichi, Curr. Opin. Cell Biol. 5, 806-811 (1993); W. Birchmeier, J. Behrens, Biochim. Biophys. Acta 1198, 11-26 (1994); O. W. Blaschuk et al., Endocrine 3, 83-89 (1995). Review of desmosomal cadherins: P. J. Koch, W. W. Franke, Curr. Opin. Cell Biol. 6, 682-687 (1994).
Cadinenes Cadmium Acetate Cadmium Bromide Cadmium Carbonate Cadmium Chloride

Principal interactions of structural proteins at cadherin-based adherens junction. Actin filaments are linked to α-actinin and to membrane through vinculin. The head domain of vinculin associates to E-cadherin via α-, β-, and γ-catenins. The tail domain of vinculin binds to membrane lipids and to actin filaments.

Cadherins (named for "calcium-dependent adhesion") are a class of type-1 transmembrane proteins. They play important roles in cell adhesion, forming adherens junctions to bind cells within tissues together. They are dependent on calcium (Ca2+) ions to function, hence their name.

The cadherin superfamily includes cadherins, protocadherins, desmogleins, and desmocollins, and more.[1][2] In structure, they share cadherin repeats, which are the extracellular Ca2+-binding domains. There are multiple classes of cadherin molecule, each designated with a prefix (in general, noting the type of tissue with which it is associated). It has been observed that cells containing a specific cadherin subtype tend to cluster together to the exclusion of other types, both in cell culture and during development.[3] For example, cells containing N-cadherin tend to cluster with other N-cadherin-expressing cells. However, it has been noted that the mixing speed in the cell culture experiments can have an effect on the extent of homotypic specificity.[4] In addition, several groups have observed heterotypic binding affinity (i.e., binding of different types of cadherin together) in various assays.[5][6] One current model proposes that cells distinguish cadherin subtypes based on kinetic specificity rather than thermodynamic specificity, as different types of cadherin homotypic bonds have different lifetimes.[7]