Disease relevance of ANPEP

• A good correlation was observed between the capacity of CCV, FIPV, and TGEV to recognize the different interspecies APN chimeras and their ability to infect cells derived from the relevant species [1].
• We report that cells refractory to canine coronavirus (CCV) and feline infectious peritonitis virus (FIPV) became susceptible when transfected with a chimeric aminopeptidase-N (APN) cDNA containing a canine domain between residues 643 and 841 [1].
• The human/canine APN chimera was also able to confer susceptibility to the porcine transmissible gastroenteritis virus (TGEV), whereas its human/porcine homolog failed to confer susceptibility to CCV and FIPV [1].
• Interspecies aminopeptidase-N chimeras reveal species-specific receptor recognition by canine coronavirus, feline infectious peritonitis virus, and transmissible gastroenteritis virus [1].
• Degradation and debittering of a tryptic digest from beta-casein by aminopeptidase N from Lactococcus lactis subsp. cremoris Wg2 [2].

High impact information on ANPEP

• From reversed-phase high-performance liquid chromatography tryptic mapping, leucyl aminopeptidase M digestion, and microsequence analysis, it is clear that diiodination of the tyrosine residues is not favored for the beta-subunit with the exception of beta-Tyr-7, whereas diiodination was observed with alpha-Tyr-21 and alpha-Tyr-92/93 [3].
• Digestion of this peptide with aminopeptidase M and carboxypeptidase B yielded a tetrapeptide (residues 6 through 9) [4].
• Aromatic and aliphatic substituents placed at this position strongly interact with the LAP S1' binding pocket, while a significant increase in binding affinity toward APN was observed for compounds containing aromatic versus leucine side chains at the P1' position [5].
• A role for aminopeptidase N in Na(+)-dependent amino acid transport in bovine renal brush-border membranes [6].
• On the basis of its N-terminal amino acid sequence, the 120-kDa biotin-containing protein is totally distinct from the 120-kDa aminopeptidase N reported to be a receptor for Cry1Ac toxin [7].

Biological context of ANPEP

• PsA inhibited the APN activity with an IC50 of 18 microM in a non-competitive manner [8].
• The oligopeptides produced in the tryptic digest before and after aminopeptidase N treatment were identified by analysis of the N- and C-terminal amino acid sequences and amino acid compositions of the isolated peptides and by on-line liquid chromatography-mass spectrometry [2].
• Incubation of purified peptides with aminopeptidase N resulted in complete hydrolysis of many peptides, while others were only partially hydrolyzed or not hydrolyzed [2].
• The Arg-Phe-[3H]anilide:AmN reaction obeyed first-order enzyme kinetics when human serum, human seminal plasma, guinea pig serum, or homogeneous porcine kidney AmN was used as enzyme source and substrate was within the concentration range of 1-200 nM [9].
• Gestational age x feeding interactions indicated increased activities of aminopeptidase N and reduced lactase activities only in F8 and reduced dipeptidylpeptidase IV activities only in P8 [10].

Anatomical context of ANPEP

• These results imply that anti-angiogenic activity of BetA occurs through a modulation of mitochondrial function rather than APN activity in endothelial cells [11].
• The results obtained in the rabbit pulmonary artery show that MEN 10,208 is degraded by local amastatin-sensitive enzymes (possibly aminopeptidase M), which may convert the linear octapeptide MEN 10,208 to the heptapeptide MEN 10,207 by removing the N-terminal Thr from the amino acid sequence of MEN 10,208 [12].
• DEXA reduced aminopeptidase N activities in the jejunum of formula-fed calves, but increased the peptidase activities mainly of colostrum-fed calves in the ileum [13].
• The inhibitory effect of carb-cys conjugates was evaluated towards isolated aminopeptidase N and aminopeptidase-N-like activity of excised vaginal mucosa covered with native mucus, respectively [14].
• The methodology included a modified acetylcholinesterase (AChE) reaction as a selective marker for pre-Sertoli cells and a modified microsomal aminopeptidase (MAP) reaction as a selective marker for the epithelia of rete testis and straight testicular tubules [15].

Associations of ANPEP with chemical compounds

• Compound 1 potently inhibited APN activity with a K(i) value of 3.5 microM [16].
• Interestingly, the permeability coefficient of Met-Enk was increased 4-fold in the presence of specific inhibitors of APM and ACE [17].
• The effect of specific inhibitors of APM, ACE and NEP on the permeability of [Met5]enkephalin (Met-Enk) and a conformationally constrained and enzymatically stable analog, DPDPE, also was determined [17].
• We have confirmed that alleged substrates such as angiotensin III and Met-Lys- and Lys-bradykinin are bound by AmN with high affinities (Km values, 5.7, 9.1, and 14.3 microM) [9].
• Purified milk proteins (alpha-lactalbumin, beta-lactoglobulin, and beta-casein) were hydrolyzed in 0.1 M Hepes buffer (pH 7.5) containing pronase E, aminopeptidase M, and prolidase at 37 degrees C for 20 h [18].

Other interactions of ANPEP

• They varied in size and morphology and contained Mg2+,Ca2+-activated ATPase, aminopeptidase A, alanyl aminopeptidase, gamma-glutamyl transpeptidase and dipeptidyl peptidase IV activities [19].

Analytical, diagnostic and therapeutic context of ANPEP

• To determine optimal conditions for treatment of donor eyes before transplantation, activities of key proteases (aminopeptidase M, dipeptidylpeptidase II and IV and gamma-glutamyltranspeptidase) as indicators of RPE cell quality (viability and functional state) were measured [20].
• Fractionation of the plasma membranes by centrifugation on a Percoll density gradient resulted in clear separation of the basolateral membranes (BLM) from the brush-border membranes (BBM), with Na+,K+-ATPase and aminopeptidase M as their respective marker enzymes [21].

References