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Human CD13 Protein expressed in Human Cells - ABIN3216379
Yeager, Ashmun, Williams, Cardellichio, Shapiro, Look, Holmes: Human aminopeptidase N is a receptor for human coronavirus 229E. in Nature 1992
Show all 6 Pubmed References
Crosslinking of CD13 by mAb C or E is required to inhibit adhesion, as monovalent Fab (show FANCB Proteins) fragments are not sufficient. Thus, C and E antibodies recognize a distinct epitope on CD13, and binding to this epitope interferes with both CD13-mediated cell adhesion and enzymatic activity.
Data indicate the expression of aminopeptidase N (CD13) in small cell lung cancer (SCLC) tumor and suggest pre-therapeutic CD13 analysis for testing as investigational predictive biomarker for patient selection.
CD13 may be a marker for onychofibroblasts within nail (show CD244 Proteins) matrix onychodermis
This is the first report presenting CD13 and FLI1 (show FLI1 Proteins) as important mediators of resistance to BRAF (show BRAF Proteins) inhibition with potential as drug targets in BRAF (show BRAF Proteins) inhibitors refractory melanoma.
CD13 enrichment was correlated with early recurrences, and poor prognosis in patients with hepatocellular carcinoma.
Patients with acute myeloid leukemia (show BCL11A Proteins) developing leukemia-specific acute hypoxic respiratory failure within 15 days had higher CD13 expression by leukemic cells.
Data suggest that CNGRC-GG-D(KLAKLAK)2 peptide actively participates in the downregulation of aminopeptidase N/CD13.
CGRP (show S100A12 Proteins) and IL-4 (show IL4 Proteins) positively regulated APN/CD13 expression and activity in psoriatic fibroblasts.
this study shows that CD13 significantly contributes to tissue infiltration by monocytic myeloid-derived suppressor cells and monocytes, thereby contributing to the pathogenesis of hepatic inflammation
data reveal a novel role for CD13 in inducing homotypic aggregation in neutrophils, which results in a transmigration deficiency; this mechanism may be relevant to neutrophil micro-aggregation in vivo
Genetic ablation of APN expression had no effect on infectability by porcine epidemic diarrhea virus, demonstrating that APN is not essential for porcine epidemic diarrhea virus cell entry.
pAPN is not a functional receptor for porcine epidemic diarrhea virus, but promotes the infection of PEDV through its protease activity.
The C-terminal domain of the S1 domain of porcine epidemic diarrhea virus is bound to swine pAPN.
Data indicate that fluorogenic substrates can be successfully used to identify aminopeptidase N and to measure their activity in cell lysates.
SPC (show SFTPC Proteins) subdomain of APN plays a key role in cell entry of PEDV and its expression permits PEDV growth
Porcine epidemic diarrhea virus recognizes protein receptor aminopeptidase N from pig and human and sugar coreceptor N-acetylneuraminic acid.
These data demonstrate that pAPN, the cellular receptor for porcine epidemic diarrhea virus, mediates polarized virus infection.
It was concluded that the difference in F4 binding to ANPEP is due to modifications in its carbohydrate moieties.
The region aa 673-722 of the C subunit of porcine aminopeptidase N is indicated to play a key role in swine transmissible gastroenteritis virus binding.
The binding ability of four truncated porcine aminopeptidase N proteins to transmissible gastroenteritis virus (TGEV), a porcine coronavirus, was analyzed by ELISA and immunoblotting.
we concluded that APN plays a significant role in the regulation of several sperm functions and early embryonic development. In addition, increased APN activity could potentially lead to several adverse consequences related to male fertility.
These studies identified CD13 as a novel negative regulator of mast cell activation in vitro and in vivo.
14-3-3epsilon might directly bind to CD13, which transmits its signal in chondrocytes to induce a catabolic phenotype similar to that observed in osteoarthritis.
Alanyl aminopeptidase expression is confined to mature zymogenic chief cells and its expression is lost en route to metaplasia.
CD13 negatively regulates TLR4 (show TLR4 Proteins) signaling, thereby balancing the innate response by maintaining the inflammatory equilibrium critical to innate immune regulation.
The impact of loss of CD13 on a model of ischemic skeletal muscle injury, was investigated.
Molecular mechanisms regulating CD13-mediated adhesion.
CD13 is essential for proper trafficking of the inflammatory cells necessary to prime and sustain the reparative response, thus promoting optimal post-infarction healing.
Tyrosine phosphorylation of CD13 regulates inflammatory cell-cell adhesion and monocyte trafficking.
This indicates that Anpep plays a critical role in the proteolytic remodelling of mammary tissue during adult mammary development.
APN activity is not responsible for betulinic acid-inhibited growth factor-induced angiogenesis in endothelial cells
Aminopeptidase N is located in the small-intestinal and renal microvillar membrane, and also in other plasma membranes. In the small intestine aminopeptidase N plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. Its function in proximal tubular epithelial cells and other cell types is less clear. The large extracellular carboxyterminal domain contains a pentapeptide consensus sequence characteristic of members of the zinc-binding metalloproteinase superfamily. Sequence comparisons with known enzymes of this class showed that CD13 and aminopeptidase N are identical. The latter enzyme was thought to be involved in the metabolism of regulatory peptides by diverse cell types, including small intestinal and renal tubular epithelial cells, macrophages, granulocytes, and synaptic membranes from the CNS. Human aminopeptidase N is a receptor for one strain of human coronavirus that is an important cause of upper respiratory tract infections. Defects in this gene appear to be a cause of various types of leukemia or lymphoma.
, alanyl aminopeptidase
, aminopeptidase M
, aminopeptidase N
, microsomal aminopeptidase
, myeloid plasma membrane glycoprotein CD13
, membrane alanine aminiopeptidase
, aminopeptidase n
, aminopeptidase N/CD13
, membrane protein p161
, cluster of differentiation antigen 13 (CD13)
, kidney Zn peptidase
, kidney aminopeptidase M
, leucine arylaminopeptidase 1
, membrane alanine aminopeptidase
, alanyl (membrane) aminopeptidase (aminopeptidase N, aminopeptidase M, microsomal aminopeptidase, CD13, p150)
, aminopeptidase Ey
, alanyl (membrane) aminopeptidase
, alanyl aminopeptidase, membrane L homeolog