|CD325||CDH2 (cadherin 2), NCAD, CDHM, CDw325, N-cadherin|
|Molecule Type||Antigen Expression||Molecular Weight|
Min / Max
|Non-lineage Restricted Molecule|
Type 1 glycoprotein
|140 / 140|
|CD325 is expressed on endothelial cells, stem cells, muscle cells, osteoblast, neurons and bone marrow stromal cells. Expression is on some neoplastic epithelial cells, fibroblasts, leukocytes, brain and skeletal and cardiac myocyte. Expression is mostly present on cells that do not express CD234 and P-cadherin. Molt-3 T lymphoblastic leukemia cells express CD325. |
|MOLECULAR FAMILY NAME: Belongs to the cadherin superfamily.|
CD325 is a single-pass type-1 740 aa glycoprotein. It contains a 25 aa signal sequence, a 134 aa propeptide, a 555 aa extracellular domain which contains 5 cadherin domains, 4 potential N-linked glycosylation sites and binds a single Ca2+ ion, a 21 aa transmembrane domain and a 157 aa intracellular cytoplasmic domain. The encoded protein is a calcium-dependent cell-cell adhesion glycoprotein.
POST-TRANSCRIPTIONAL MODIFICATION: No information.
CD325 has 4 N-linked glycosylation sites.
|LIGANDS AND MOLECULE ASSOCIATED WITH CD325|
CD325 is associated with N-cadherin, catenins, FGFR, PS1. CD325 exhibits homophilic binding.
|CD325 forms a complex with catenins that is linked to the actin cytoskeleton. The catenin complex plays an important role in synaptic development and the structural and functional plasticity of neurons. Electrical activity regulates the ditribution of CD325 at synapases by mobilizing CD325 and catenins to the synapase. CD325 is one of the first cadherins recruited to the site of synapse formation and homophilic interactions across the synaptic gap are thought to stabilize the early synapse. As synapase mature, CD 325 accumulates at excitatory but not at inhibitory synapses. At least two studies have shown antibody to the CD325 extracellular domain can inhibit the induction of long-term potentiation. Cadherins are calcium dependent cell adhesion proteins and are known to play major roles during embryonic development and in the maintenance of solid tissue architecture. They preferentially interact with themselves in a homophilic manner in connecting cells. Expression of CD325 is on the surface of malignant T cells and tumors and was found to modulate adhesion of T cells to Caco-2 epithelial cell in vitro. Malignant T cell s has been linked to disease aggressiveness, specifically the ability to invade and form metastases. CD325 is involved in cell-cell cell-matrix adhesion, cell growth and differentiation and may be involved in the neuronal recognition mechanism. CD325 may contribute to the sorting of heterogeneous cell types. The protein functions during gastrulation and is required for establishment of left-right asymmetry. At certain central nervous system synapses, presynaptic to postsynaptic adhesion is mediated at least in part by this gene product.|
BIOCHEMICAL ACTIVITY: No information.
DISEASE RELEVANCE AND FUNCTION OF CD325 IN INTACT ANIMAL
Indications show that CD325 has a direct involvement in the differentiation program of early hematopoietic progenitors. CD325 can also mediate adhesive interactions within the bone marrow as demonstrated by inhibition of homotypic interactions of bone marrow cells with CD325 antibodies. There is a strong suggestion that CD325 is involved in the development and retention of early hematopoietic progenitors within the bone marrow microenvironment. It has been suggested that CD325 is implicated in learning and memory as well as neurodegenerative disease and may contribute to memory impairment associated with Alzheimer's disease. CD325 is proteolytically cleaved by presenilin 1, a protein implicated in Alzheimer's disease. CD325 is expressed on the surface of malignant T cells suggesting a role for N-cadherin in promoting malignant T-cell adhesion to epithelia as well as their capacity to invade and metastasize to inflammatory sites. CD325 null mice die in embryos around day 10 of development, indicating that the presence of this cadherin is essential for embryonic development.
PROTEINS AND DNA ELEMENTS WHICH REGULATE TRANSCRIPTION OF CD325: No information.
SUBSTRATES: No information.
ENZYMES WHICH MODIFY CD325: No information.
For further information see Puch, S. et al (2001) J. Cell Sci. 114: 1567-1577.
Database accession numbers
Revised June 25, 2008