Membrane metalloendopeptidase
Sign in to saveAlso known as CALLA, Neutral endopeptidase, neprilysin, skin fibroblast elastase, membrane metallo-endopeptidase variant 2, neprilysin-390, common acute lymphocytic leukemia antigen, neprilysin-411
Neprilysin (; also known as membrane metallo-endopeptidase (MME), neutral endopeptidase (NEP), cluster of differentiation 10 (CD10) and common acute lymphoblastic leukemia antigen (CALLA)) is an enzyme that in humans is encoded by the MME gene. Neprilysin is a zinc-dependent metalloprotease that cleaves peptides at the amino side of hydrophobic residues and inactivates several peptide hormones including glucagon, enkephalins, substance P, neurotensin, oxytocin, and bradykinin. It also degrades the amyloid beta peptide whose abnormal folding and aggregation in neural tissue has been implicated
Protein · UniProt
Neprilysin
- Gene
- MME
- Organism
- Homo sapiens (Human)
- Length
- 750 aa
- Molecular mass
- 85,514 Da
- Evidence
- 1: Evidence at protein level
Thermolysin-like specificity, but is almost confined on acting on polypeptides of up to 30 amino acids (PubMed:15283675, PubMed:6208535, PubMed:6349683, PubMed:8168535). Biologically important in the destruction of opioid peptides such as Met- and Leu-enkephalins by cleavage of a Gly-Phe bond (PubMed:17101991, PubMed:6349683). Catalyzes cleavage of bradykinin, substance P and neurotensin peptides (PubMed:6208535). Able to cleave angiotensin-1, angiotensin-2 and angiotensin 1-9 (PubMed:15283675, PubMed:6349683). Involved in the degradation of atrial natriuretic factor (ANF) and brain natriur…
Swiss-Prot (reviewed) · via UniProt
Clinical Trials
47 registered- PHASE2COMPLETEDAn 8-week Study to Evaluate the Dose Response of AHU377 in Combination With Valsartan 320 mg in Patients With Mild-to-moderate Systolic HypertensionNovartis Pharmaceuticals · NCT01281306
- PHASE4TERMINATEDPulmonary Artery Pressure Reduction With ENTresto (Sacubitril/Valsartan)Brigham and Women's Hospital · NCT02788656
- PHASE4COMPLETEDThe Effects of Neprilysin on Glucagon-like Peptide-1Nicolai Jacob Wewer Albrechtsen · NCT03717688
- PHASE4RECRUITINGTreatment of Moderate Ischemic Mitral Regurgitation in Patients With Coronary Artery DiseaseChina National Center for Cardiovascular Diseases · NCT06917664
- PHASE2COMPLETEDPDD in Type 2 Diabetes w/wo Diastolic DysfunctionMayo Clinic · NCT03744975
- UNKNOWNProspective Monitoring of Angiotensin Receptor Neprilysin Inhibitor in Older Adults With Heart Failure and FrailtyBrigham and Women's Hospital · NCT04743063
Wikidata facts
- Instance of
- protein
Show 3 more facts
- found in taxon
- Homo sapiens
- exact match
- purl.uniprot.org/uniprot/P08473
- Commons category
- CD10 (Nephrilysin)
via Wikidata · CC0
~8 min read
Encyclopedic overview
10 sectionsContents
- Amyloid beta regulation
- Signaling peptides
- Inhibitors
- Immunochemistry
- In lymphomas and leukemias
- In epithelial tumors
- In other tumors
- See also
- References
- External links
Neprilysin (; also known as membrane metallo-endopeptidase (MME), neutral endopeptidase (NEP), cluster of differentiation 10 (CD10) and common acute lymphoblastic leukemia antigen (CALLA)) is an enzyme that in humans is encoded by the MME gene. Neprilysin is a zinc-dependent metalloprotease that cleaves peptides at the amino side of hydrophobic residues and inactivates several peptide hormones including glucagon, enkephalins, substance P, neurotensin, oxytocin, and bradykinin. It also degrades the amyloid beta peptide whose abnormal folding and aggregation in neural tissue has been implicated as a cause of Alzheimer's disease. Synthesized as a membrane-bound protein, the neprilysin ectodomain is released into the extracellular domain after it has been transported from the Golgi apparatus to the cell surface.
Neprilysin is expressed in a wide variety of tissues and is particularly abundant in the kidneys. It is also a common acute lymphocytic leukemia antigen that is an important cell surface marker in the diagnosis of human acute lymphocytic leukemia (ALL). This protein is present on leukemic cells of pre-B phenotype, which represent 85% of cases of ALL.
Excerpted from Wikipedia’s “Membrane metalloendopeptidase” article, available under the CC BY-SA 4.0 licence.