|CD10||MME (membrane metallo-endopeptidase),CALLA(common acute lymphoblastic leukemia antigen), NEP (neutral endopeptidase ), gp100|
|Molecule Type||Antigen Expression||Molecular Weight|
Min / Max
|Non-lineage Restricted Molecule|
Type 2 glycoprotein
|100 / 100|
|CD10 is expressed on early B and T lymphoid precursors, B blasts, germinal center B cells, mature neutrophils, some granulocytes and bone marrow stromal cells. CD10 is also expressed on various epithelia with especially high expression on the brush border epithelium in the kidney and gut, on some smooth muscle and myoepithelial cells, brain and fibroblasts. CD10 is widely used as a marker of common pre-B acute lymphocytic leukemias and certain lymphomas. In contrast to the human, mouse CD10 is absent from B and T cells and granulocytes, but the expression pattern is similar to the human on bone marrow stromal cells and non-lymphoid tissues.|
|MOLECULAR FAMILY NAME: Belongs to the metalloendopeptidase M13 family.|
CD10 is a single-pass type 2 glycoprotein. It contains an extracellular C terminal domain which contains 4 N-linked glycosylation sites and 12 cysteines that form disulphide bonds required for enzymatic activity and the characteristic pentapeptide motif HEI/L/MXH associated with zinc binding and catalytic activity in a number of zinc-dependent metalloprotease, a transmembrane region that functions as a signal peptide and a short N-terminal cytoplasmic tail. CD10 is a member of a group of type-2 membrane metalloproteases that includes the leukocyte molecules CD13, CD26, CD73 and BP-1. The requirement for zinc binding, substrate binding and catalytic activity has been identified by alignment with the well-characterized bacterial metalloprotease thermolysin and by site-directed mutagenesis.
Exons 1 and 2 in the prime untranslated region may be alternatively spliced. The 5' untranslated region of CD10 is spliced resulting in 4 separate mRNA transcripts. The coding region initiates in exon 3 and is not affected by alternative splicing.
CD10 has 4 N-glycosylation sites.
|LIGANDS AND MOLECULES ASSOCIATED WITH CD10: No information.|
|CD10 is a regulator of B cell growth and proliferation by hydrolysis of peptides with proliferative/anti-proliferative effects. CD10 is a zinc-binding metalloprotease which is thought to downregulate cellular responses to peptide hormones. By hydrolysing peptide bonds on the amino side of hydrophobic amino acid, CD10 reduces the local concentration of peptide available for receptor binding and signal transduction. CD10 can cleave a variety of biologically active peptides including opioid enkephalins, fMLP, substance P, bombesin-like peptides, atrial natriuretic factor, endothelin, oxytocin, bradykinin and angiotensins I and II. CD10 on neutrophils limits their inflammatory responses by degrading peptides such as fMLP, substance P and enkephalins. CD10 on bone marrow stromal cells appears to regulate B cell development, since inhibition of CD10 enzyme activity in vivo enhances B cell maturation. Targeted disruption of the gene for CD10 suggests a role in the modulation of septic shock, since CD10-deficient mice, which are otherwise grossly normal, exhibit enhanced lethality to endotoxin.|
BIOCHEMICAL ACTIVITY: No information.
DISEASE RELEVANCE AND FUNCTION OF CD10 IN INTACT ANIMAL
CD10 is a useful marker for classification of B-lineage leukemias and lymphomas as well as renal and hepatocellular carcinoma and uterine mescenchymal neoplasms and is a prognostic marker of metaplastic breast carcinoma.
PROTEINS AND DNA ELEMENTS WHICH TRANSCRIPTION OF CD10: No information.
SUBSTRATES: No information.
ENZYMES WHICH MODIFY CD10: No information.
Database accession numbers
Revised June 25, 2008