Classic Cadherins represent a family of calcium-dependent homophilic cell-cell adhesion molecules. They confer strong adhesiveness to animal cells when they are anchored to the actin cytoskeleton via their cytoplasmic binding partners, catenins. The cadherin/catenin adhesion system plays key roles in the morphogenesis and function of the vertebrate and invertebrate nervous systems. Furthermore, this system is involved in synaptic plasticity. Recent studies on the role of individual cadherin subtypes at synapses indicate that individual cadherin subtypes play their own unique role to regulate synaptic activities. Type II (atypical) cadherins are defined based on their lack of an HAV cell adhesion recognition sequence specific to type I cadherins. 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. Cadherin-12 also known as CDH12, is a type II classical cadherin from the cadherin superfamily of integral membrane proteins that mediate calcium-dependent cell-cell adhesion. Cadherin-12 appears to be expressed specifically in the brain and its temporal pattern of expression would be consistent with a role during a critical period of neuronal development, perhaps specifically during synaptogenesis.
Cadherin-16(CDH16) is a single-pass type I membrane protein which contains six cadherin domains. Mature cadherin proteins consist of a large N-terminal extracellular domain, a single membrane-spanning domain, and a small highly conserved C-terminal cytoplasmic domain. Cadherins are calcium-dependent cell adhesion proteins and may contribute to the sorting of heterogeneous cell types. They preferentially interact with themselves in a homophilic manner in connecting cells. Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain. CDH16 is exclusively expressed in kidney, where the protein functions as the principal mediator of homotypic cellular recognition. It plays a role in the morphogenic direction of tissue development. CDH16 is composed of an extracellular domain containing 6 cadherin domains, a transmembrane region and a truncated cytoplasmic domain. However, it lacks the prosequence and tripeptide HAV adhesion recognition sequence typical of most classical cadherins.
Cadherin-17 is a single-pass type I membrane protein that belongs to the cadherin superfamily. Cadherin-17 consists of one extracellular region containing seven cadherin domains and one transmembrane region but it lacks the conserved cytoplasmic domain. Cadherin-17 is expressed in the gastrointestinal tract and pancreatic duct. Cadherins are calcium dependent cell adhesion proteins and preferentially interact with each other in a homophilic manner in connecting cells. Cadherin-17 may have a role in the morphological organization of liver and intestine and involved in intestinal peptide transport.
Cadherin-3 (CDH3) is a single-pass type I membrane protein that belongs to the cadherin superfamily. CDH3 is a calcium-dependent cell-cell adhesion glycoprotein comprised of five extracellular cadherin repeats, a transmembrane region, and a highly conserved cytoplasmic tail. CDH3 is expressed in some normal epithelial tissues and in some carcinoma cell lines. CDH3 preferentially interacts with themselves in a homophilic manner in connecting cells. CDH3 is involved in loss of heterozygosity events in breast and prostate cancer. Mutations in CDH3 have been associated with congential hypotrichosis with juvenile macular dystrophy.
Cadherin-6 (CDH6) is a type-II classic cadherin cell-cell adhesion molecules, which are expressed in graded or areal patterns, as well as layer-specific patterns, in the cortical plate. Human Cadherin-6 is synthesized as a 790 aa type I transmembrane glycoprotein that contains a 18 aa signal peptide, a 35 aa propeptide, a 562 aa extracellular region, a 21 aa transmembrane segment, and a 154 aa cytoplasmic domain. There are five cadherin domains of approximately 110 aa each in the extracellular region. Cadherin-6 has high expression in kidney, brain, and cerebellum, and may contribute to the formation of the segmental structure of the early brain, as well as the development of renal proximal tubules. Weak expression is also detected in lung, pancreas, gastric mucosa and cytotrophoblasts. As a classic cadherin, Cadherin-6 will form homodimers and promote intercellular adhesion with itself and, possibly, Cadherin-9 and -14.
Cadherin-8 (CDH8) is a type II classical cadherin from the cadherin superfamily. Member of the Cadherin superfamily are integral membrane proteins that mediate calcium-dependent cell-cell adhesion. Cadherin proteins are composed of a large N-terminal extracellular domain, a single membrane-spanning domain, and a small highly conserved C-terminal cytoplasmic domain. Cadherins are calcium dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells. The extracellular domain of CDH8 contains five cadherin domains. CDH8 is expressed in brain and is putatively involved in synaptic adhesion, axon outgrowth and guidance.
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