High impact information on CDH2

• The extracellular domain of dg3 shows 39.4% protein sequence identity with bovine N-cadherin and 28.4% identity with the other major desmosomal glycoprotein, dg1, or desmoglein [1].
• This showed 43% identity with that of the N terminus of the calcium-dependent cell adhesion molecule, N-cadherin [2].
• Genes that were expressed at significantly higher levels (>1.5-fold; P < 0.05) in tissues from Johne's disease-infected animals relative to noninfected animals included those encoding tumor necrosis factor receptor-associated protein 1 (TRAF1), interleukin-1alpha (IL-1alpha), MCP-2, N-cadherin, and beta1 integrin (CD29) [3].
• The GalNAcPTase is known to be associated with the adhesion molecule N-cadherin in embryonic avian retinas and with E-cadherin in mammalian pancreatic islet cells [4].
• The N-cadherin (N-cad) and Connexin43 (Cx43) expression level of rOB cells cultured with SHya remarkably increased after 2h [5].

Biological context of CDH2

• However, inhibition of cell-to-cell contact by N-cadherin is not effective on up regulation of viral transcription [6].

Anatomical context of CDH2

• A novel function of N-cadherin and Connexin43: marked enhancement of alkaline phosphatase activity in rat calvarial osteoblast exposed to sulfated hyaluronan [5].

Analytical, diagnostic and therapeutic context of CDH2

• Northern blot analysis with the corresponding cDNA probe showed a wide distribution of bovine N-cadherin among non-neuronal, as well as neuronal tissues, while P-cadherin was most abundant in kidney among all the bovine tissues tested, but was undetectable in placenta [7].

References