CD10 (neprilysin, neutral endopeptidase, enkephalinase, common acute lymphoblastic leukemia antigen, CALLA, atriopeptidase, MME, EPN)
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Function
- thermolysin-like specificity
- preferential cleavage of polypeptides between hydrophobic residues, particularly with Phe or Tyr at P1
- substrates are polypeptides < 5 kD
- endorphins, enkephalins, cleavage of a Gly-Phe bond
- substance P, kinins
- somatostatin
- atrial natriuretic factor (ANF)
- amyloid A4 peptide
- degrades amyloid beta-peptide (A4 amyloid peptide)[7][8][9] of senile plaques in Alzheimer's disease;[5]
- it is thought that neprilysin & insulin-degrading enzyme may be major enzymes degrading the amyloid beta-peptide[6]
Cofactor: binds 1 Zn+2 per subunit
Structure
belongs to the peptidase M13 family
Compartment
- plasma membrane
- internal membranes
- axonally transported; present in presynaptic membrane[7]
Expression
- widely distributed
- follicular center cells, pre-B cells, granulocytes cortical thymocytes, lympho-hematopoietic precursors
- endometrial stroma, male GU epithelium, mesonephric remnants, liver, brush border in small bowel mucosa, placenta choroid plexus, brain, ovary, adrenal cortex
Pathology
- expressed in many tumors including: follicular center cell lymphomas pre-B ALL ~75% CML in blast crisis ~90% hepatocellular carcinoma (canalicular pattern) ~68% sensitive, >95% specific with canalicular pattern mesonephric tumors renal cell carcinoma urothelial carcinoma prostate carcinoma pancreatic carcinoma uterine carcinoma endometrial stromal tumors smooth muscle tumors sarcomas melanomas microvillous inclusion disease
- myeloid & erythroid precursors & female genital tract tumors stain negatively with antibody
More general terms
References
- ↑ Cotran et al Robbins Pathologic Basis of Disease, W.B. Saunders Co, Philadelphia, PA 1989 pg 165
- ↑ UniProt http://www.uniprot.org/uniprot/Q00973.html
- ↑ Journal Watch 20(5):38, 2000 Iwata N, Tsubuki S, Takaki Y, Watanabe K, Sekiguchi M, Hosoki E, Kawashima-Morishima M, Lee HJ, Hama E, Sekine-Aizawa Y, Saido TC. Identification of the major Abeta1-42-degrading catabolic pathway in brain parenchyma: suppression leads to biochemical and pathological deposition. Nat Med. 2000 Feb;6(2):143-50. PMID: https://www.ncbi.nlm.nih.gov/pubmed/10655101
- ↑ Selkoe DJ. Clearing the brain's amyloid cobwebs. Neuron. 2001 Oct 25;32(2):177-80. Review. <PubMed> PMID: https://www.ncbi.nlm.nih.gov/pubmed/11683988
- ↑ 5.0 5.1 <Internet> http://www.pathologyoutlines.com/cdmarkers.html 15 October 2002
- ↑ 6.0 6.1 Greg Gole, UCLA Sepulveda VA, 02/12/2004, personal communication
- ↑ 7.0 7.1 7.2 Iwata N, Mizukami H, Shirotani K, Takaki Y, Muramatsu S, Lu B, Gerard NP, Gerard C, Ozawa K, Saido TC. Presynaptic localization of neprilysin contributes to efficient clearance of amyloid-beta peptide in mouse brain. J Neurosci. 2004 Jan 28;24(4):991-8. PMID: https://www.ncbi.nlm.nih.gov/pubmed/14749444
- ↑ 8.0 8.1 Marr RA, Guan H, Rockenstein E, Kindy M, Gage FH, Verma I, Masliah E, Hersh LB. Neprilysin regulates amyloid Beta peptide levels. J Mol Neurosci. 2004;22(1-2):5-11. PMID: https://www.ncbi.nlm.nih.gov/pubmed/14742905
- ↑ 9.0 9.1 Atlas of genetics & cytogenetics in oncology & haematology http://atlasgeneticsoncology.org/genes/MMEID41386ch3q25.html