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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
Patients with acute myeloid leukemia (zeige BCL11A Proteine) 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 (zeige S100A12 Proteine) and IL-4 (zeige IL4 Proteine) 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
CD13 expression is associated with hepatoblastoma invasiveness and could be a novel prognostic marker for hepatoblastoma.
Data indicate that fluorogenic substrates can be successfully used to identify aminopeptidase N and to measure their activity in cell lysates.
Data show that CD13 anntigen and receptor tyrosine kinase-like orphan receptor 2 (ROR2 (zeige ROR2 Proteine)) identify a cardiac lineage precursor pool that is capable of successful engraftment into the porcine heart.
The substrate Angiotensin II, the enzymes aminopeptidases-A, B, M as well as IRAP (zeige IL1RN Proteine) were detected in the jejunal mucosa.
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.
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.
SPC (zeige SFTPC Proteine) 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.
results demonstrate that aminopeptidase N reduces basolateral Na(+)-K(+)-ATPase (zeige ATP1A1 Proteine) levels via ANG (zeige ANG Proteine) IV/AGTRIV signaling. This novel pathway may be important in renal adaptation to high salt
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.
Alanyl aminopeptidase expression is confined to mature zymogenic chief cells and its expression is lost en route to metaplasia.
CD13 negatively regulates TLR4 (zeige TLR4 Proteine) 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