CD13; aminopeptidase-N; aminopeptidase-M; gp150; microsomal aminopeptidase; alanine aminopeptidase (ANPEP, PEPN)
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Function
- broad specificity aminopeptidase
- role in final digestion of peptides generated from hydrolysis of proteins by gastric & pancreatic proteases
- may be involved in metabolism of regulatory peptides of diverse cell types (see expression)
- found to cleave antigen peptides bound to MHC class II molecules of presenting cells
- degrades neurotransmitters at synaptic junctions
- implicated as a regulator of IL-8 bioavailability in the endometrium
- may contribute to the regulation of angiogenesis
- may undergo proteolysis & give rise to a soluble form
- release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide; Xaa is preferably Ala, but may be most amino acids including Pro (slow action); when a terminal hydrophobic residue is followed by Pro, the two may be released as an intact Xaa-Pro dipeptide
Cofactor: binds 1 Zn+2 per subunit (putative)
Structure
- homodimer
- N- & O-glycosylated
- amino acids 260-353 are essential to mediate susceptibility to infection with HCoV-229E
- belongs to the peptidase M1 family
Compartment
- cell membrane, cytoplasm
- plasma membrane, exoplasmic face
- bile, concentration in human hepatic bile 17.3- 57.6 ug/mL
Expression
- brush border membranes of small intestine
- renal proximal tubules
- placenta
- CNS synaptic membranes
- granulocytes
- macrophages
- endothelial cells
- bile duct canaliculi
- fibroblasts
- osteoclasts
- perineurium of peripheral nerves
- some large granular lymphocytes
- estradiol & IL-8 decrease enzymatic activity in vitro in endometrial stromal cells by 40% & 30%, respectively
Pathology
- defects associated with various leukemias/lymphomas
- plays a role in tumor invasion
- found to serve as a receptor for tumor-homing peptides, more specifically NGR peptides, thus could serve as a target for delivering drugs into tumors
- human coronavirus 229E (HCoV-229E) infection
- serves as receptor for HCoV-229E spike glycoprotein
- interacts with the S1 domain of HCoV-229E spike protein
- mediates as human cytomegalovirus (HCMV) infection sulfated (putative)
- autoantibodies associated with chronic graft versus host disease
- may play role in pathogenesis of cholesterol gallstone disease
More general terms
More specific terms
References
- ↑ Taylor A. Aminopeptidases: structure and function. FASEB J. 1993 Feb 1;7(2):290-8. Review. PMID: https://www.ncbi.nlm.nih.gov/pubmed/8440407
- ↑ PROSITE :accession PS00142
- ↑ Cotran et al Robbins Pathologic Basis of Disease, W.B. Saunders Co, Philadelphia, PA 1989 pg 165
- ↑ http://www.pathologyoutlines.com/cdmarkers.html 15 October 2002
- ↑ UniProt http://www.uniprot.org/uniprot/P15144.html