MME
MME (membrane metalloendopeptidase, also known as neprilysin, NEP, CD10 and CALLA) is a type II transmembrane glycoprotein and neutral endopeptidase of the M13 family. It inactivates a range of signalling peptides at the cell surface and is a established cell-surface marker in acute lymphocytic leukaemia. Browse Assay Genie's current range of MME research reagents below, or read on for the biology behind the target.
MME is a neutral endopeptidase that cleaves peptides on the amino side of hydrophobic residues. Its specificity resembles that of thermolysin, but it acts almost exclusively on polypeptides of up to about 30 amino acids. In this way it inactivates several peptide hormones and neuropeptides, including glucagon, oxytocin, substance P, neurotensin and bradykinin. It is biologically important in the destruction of opioid peptides such as Met- and Leu-enkephalin, which it cleaves at a Gly-Phe bond.
The enzyme also acts on components of cardiovascular peptide signalling. It can cleave angiotensin-1, angiotensin-2 and angiotensin 1-9, and it is involved in the degradation of atrial natriuretic factor (ANF) and brain natriuretic factor (BNP(1-32)). In addition, MME displays UV-inducible elastase activity toward skin preelastic and elastic fibres. The MME protein belongs to the peptidase M13 family and is anchored in the cell membrane as a type II transmembrane glycoprotein. It is not restricted to one cell type and is found on a variety of normal tissues.
The name CD10 reflects its place among the CD molecules, while CALLA stands for common acute lymphocytic leukaemia antigen. The protein is present on leukaemic cells of pre-B phenotype, which represent 85% of cases of acute lymphocytic leukaemia (ALL), and it is an important cell-surface marker in diagnosing human ALL. HGNC classifies the MME gene in the groups CD molecules, M13 metallopeptidases and Elastases. The rat ortholog carries the same symbol, Mme.
MME (CD10, CALLA) is an important cell-surface marker for diagnosing human acute lymphocytic leukaemia and is present on leukaemic cells of pre-B phenotype.
MME helps destroy opioid peptides such as Met- and Leu-enkephalin and cleaves substance P and neurotensin, making it relevant to peptide inactivation studies.
The enzyme cleaves angiotensin peptides and contributes to the degradation of atrial natriuretic factor and brain natriuretic factor.
MME shows UV-inducible elastase activity toward skin preelastic and elastic fibres, linking the peptidase to extracellular matrix turnover.
MME is a cell-surface neutral endopeptidase that cleaves short peptides, generally up to about 30 amino acids, on the amino side of hydrophobic residues. Its substrates include enkephalins, substance P, neurotensin, bradykinin, oxytocin, glucagon, angiotensins, ANF and BNP.
CD10 is its cluster of differentiation designation. CALLA stands for common acute lymphocytic leukaemia antigen, reflecting its use as a leukaemia marker. Neprilysin and NEP describe the neutral endopeptidase activity, and the official gene name is membrane metalloendopeptidase.
MME is a common acute lymphocytic leukaemia antigen, present on leukaemic cells of pre-B phenotype, which represent 85% of ALL cases. It is also found on many normal tissues, so it is a marker rather than a leukaemia-specific protein.
Other M13 family peptidases, peptide substrates and cardiovascular signalling targets that connect to MME biology.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P08473; product specifications from Assay Genie datasheets.