Bibliographies thématiques / Aminopeptidase N

Littérature scientifique sur le sujet « Aminopeptidase N »

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Publié le 4 juin 2021

Mis à jour le 29 mai 2022

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Articles de revues sur le sujet "Aminopeptidase N":

Jóźwik, Artur, Ewa Polawska, Nina Strzałkowska, Krzysztof Niemczuk, Małgorzata Łysek-Gładysińska, Agnieszka Kamińska et Monika Michalczuk. « Effect of linseed, rapeseed, and vitamin E long term supplementation on the activity of the lysosomal enzymes in ostrich liver ». Bulletin of the Veterinary Institute in Pulawy 57, n^o 4 (1 décembre 2013) : 573–78. http://dx.doi.org/10.2478/bvip-2013-0098.

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Abstract The aim of the study was to assess the activity of lysosomal enzymes: aminopeptidases, including alanine aminopeptidase (AlaAP), leucine aminopeptidase (LeuAP), arginine aminopeptidase (ArgAP), and glycosidases, such as β-galactosidase (BGAL), β-glucuronidase (BGRD), β-glucosidase (BGLU), N-acetyl-β-hexosaminidase (HEX), α-glucosidase (AGLU) and α-mannosidase (MAN) in the liver of ostriches (n = 80) fed diet supplemented with linseed (4% and 8%) and rapeseed (5% and 10%), with low and high level of vitamin E. (40 and 100 mg). The results indicate that higher level of vitamin E or 4% linseed supplementation in ostrich diet generally increase the activity of glycosidase enzymes and decrease the activity of aminopeptidases in the liver. The 8% linseed and rapeseeds feeding in decreased the activity of AlaAP, LeuAP, and ArgAP and increased only the activity of BGLU.

Varona, Adolfo, Lorena Blanco, José I. López, Javier Gil, Ekaitz Agirregoitia, Jon Irazusta et Gorka Larrinaga. « Altered levels of acid, basic, and neutral peptidase activity and expression in human clear cell renal cell carcinoma ». American Journal of Physiology-Renal Physiology 292, n^o 2 (février 2007) : F780—F788. http://dx.doi.org/10.1152/ajprenal.00148.2006.

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Peptides play important roles in cell regulation and signaling in many tissues and are regulated by peptidases, most of which are highly expressed in the kidney. Several peptide convertases have a function in different tumor stages, and some have been clearly characterized as diagnostic and prognostic markers for solid tumors, including renal cancer; however, little is known about their in vivo role in kidney tumors. The present study compares the activity of a range of peptidases in human tumor samples and nontumor tissue obtained from clear cell renal cell carcinoma (CCRCC) patients. To cover the complete spectrum and subcellular distribution of peptide-converting activity, acid, neutral, basic, and omega activities were selected. CCRCC displays a selective and restricted pattern of peptidase activities. Puromycin-sensitive aminopeptidase activity in the tumor increases [tumor (t) = 10,775 vs. nontumor (n) = 7,635 units of peptidase (UP)/mg protein; P < 0.05], whereas aminopeptidase N decreases (t = 6,664 vs. n = 33,381 UP/mg protein; P < 0.001). Aminopeptidase B activity of the particulate fraction in tumors decreases (t = 2,399 vs. n = 13,536 UP/mg protein; P < 0.001) compared with nontumor tissues, and aspartyl-aminopeptidase activity decreases significantly in CCRCC (t = 137 vs. n = 223 UP/mg protein; P < 0.05). Soluble and particulate pyroglutamyl peptidase I activities, aminopeptidase A activity, and soluble aminopeptidase B activity do not vary in renal cancer. The relative expression for the aforementioned peptidases, assayed using quantitative RT-PCR, increases in CCRCC for aminopeptidases B (1.5-fold) and A (19-fold), aspartyl-aminopeptidase (3.9-fold), puromycin-sensitive aminopeptidase (2.5-fold), and pyroglutamyl peptidase I (7.6-fold). Only aminopeptidase N expression decreases in tumors (1.3-fold). This peptidase activity profile in the neoplastic kidney suggests a specific role for the studied convertases and the possible involvement of an intracrine renin-angiotensin system in the pathogenesis of CCRCC.

Veillard, Florian, Barbara Potempa, Marcin Poreba, Marcin Drag et Jan Potempa. « Gingipain aminopeptidase activities in Porphyromonas gingivalis ». Biological Chemistry 393, n^o 12 (1 décembre 2012) : 1471–76. http://dx.doi.org/10.1515/hsz-2012-0222.

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Abstract Bestatin, a specific inhibitor of metalloaminopeptidases, inhibits the growth of Porphyromonas gingivalis. To identify its target enzyme, a library of fluorescent substrates was used but no metalloaminopeptidase activity was found. The aminopeptidase activity of P. gingivalis was bestatin-insensitive and directed exclusively toward N-terminal arginine and lysine substrates. Class-specific inhibitors and gingipain-null mutants showed that gingipains were the only enzymes responsible for this activity. The kinetic constants obtained for Rgps were comparable to those of human aminopeptidases but Kgp aminopeptidase activity was weaker. This finding reveals a new role for gingipains as aminopeptidases in the degradation of proteins and peptides in P. gingivalis.

Matsas, R., S. L. Stephenson, J. Hryszko, A. J. Kenny et A. J. Turner. « The metabolism of neuropeptides. Phase separation of synaptic membrane preparations with Triton X-114 reveals the presence of aminopeptidase N ». Biochemical Journal 231, n^o 2 (15 octobre 1985) : 445–49. http://dx.doi.org/10.1042/bj2310445.

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The property of solutions of Triton X-114 to separate into detergent-rich and detergent-poor phases at 30 degrees C has been exploited to investigate the identities of the aminopeptidases in synaptic membrane preparations from pig striatum. When titrated with an antiserum to aminopeptidase N (EC 3.4.11.2), synaptic membranes solubilized with Triton X-100 revealed that this enzyme apparently comprises no more than 5% of the activity releasing tyrosine from [Leu]enkephalin. When assayed in the presence of puromycin, this proportion increased to 20%. Three integral membrane proteins were fractionated by phase separation in Triton X-114. Aminopeptidase activity, endopeptidase-24.11 and peptidyl dipeptidase A partitioned predominantly into the detergent-rich phase when kidney microvillar membranes were so treated. However, only 5.5% of synaptic membrane aminopeptidase activity partitioned into this phase, although the other peptidases behaved predictably. About half of the aminopeptidase activity in the detergent-rich phase could now be titrated with the antiserum, showing that aminopeptidase N is an integral membrane protein of this preparation. Three aminopeptidase inhibitors were investigated for their ability to discriminate between the different activities revealed by these experiments. Although amastatin was the most potent (IC50 = 5 × 10(−7) M) it failed to discriminate between pure kidney aminopeptidase N, the total activity of solubilized synaptic membranes and that in the Triton X-114-rich phase. Bestatin was slightly more potent for total activity (IC50 = 6.3 × 10(−6) M) than for the other two forms (IC50 = 1.6 × 10(−5) M). Puromycin was a weak inhibitor, but was more selective. The activity of solubilized membranes was more sensitive (IC50 = 1.6 × 10(−5) M) than that of the pure enzyme or the Triton X-114-rich phase (IC50 = 4 × 10(−4) M). We suggest that the puromycin-sensitive aminopeptidase activity that predominates in crude synaptic membrane preparations may be a cytosolic contaminant or peripheral membrane protein rather than an integral membrane component. Aminopeptidase N may contribute to the extracellular metabolism of enkephalin and other susceptible neuropeptides in the brain.

Galán-Ocaña, A., M. J. Ramírez-Expósito, J. M. Martínez-Martos, S. Tellado et C. Azorit. « Regulation of aminopeptidases by the renin - angiotensin system : monitoring seasonal variations in red deer and fallow deer from a Mediterranean ecosystem ». Animal Production Science 52, n^o 8 (2012) : 761. http://dx.doi.org/10.1071/an12023.

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The circulating renin–angiotensin system (RAS) is well known for its systemic role in the regulation of blood pressure, renal hemodynamics and fluid homeostasis. However, in mammals several organs also contain a local RAS, including male and female reproductive tissues. In the present study we analysed serum from a free-living population of red deer (Cervus elaphus hispanicus) and fallow deer (Dama dama) to determine the activity of four RAS-regulating aminopeptidases (aminopeptidase A, aspartyl aminopeptidase, aminopeptidase N and aminopeptidase B) as part of a study of annual cycles of growth and condition. Our aim was to detect seasonal variations in the activities of these aminopeptidases and their relationship to the reproductive behaviour of both species in a Mediterranean environment. In both males and females there was a maximum peak of activity in autumn. A second peak was detected in spring for males while in females activity was also higher in summer. These changes may be related to a different endocrine status according to their seasonal cycle, the decreased photoperiod in autumn and the normal timing of the seasonal growth cycle. Thus, changes in the activity of RAS-regulating aminopeptidases could reflect the functional role of angiotensins through the annual cycle of both species, also suggesting an important role of these peptide hormones in the regulation of these biological processes.

Jackson, M. C., Y. Choudry, A. Bourne, J. F. Woodley et A. J. Kenny. « A fluorimetric assay for aminopeptidase W ». Biochemical Journal 253, n^o 1 (1 juillet 1988) : 299–302. http://dx.doi.org/10.1042/bj2530299.

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A novel two-step enzyme-linked assay for aminopeptidase W is described and validated by comparison with other assays. L-alpha-Glutamyl-L-tryptophan (Glu-Trp) is a favoured substrate for this enzyme. With the use of glutamate dehydrogenase (EC 1.4.1.2) in a second step, the assay measured the release of free glutamate from L-alpha-glutamyl-L-tryptophan by the increase in NADH fluorescence. In the presence of 5 mM-1,10-phenanthroline and 50 microM-cilastatin the contribution of other membrane peptidases, in particular aminopeptidases N and A and microsomal dipeptidase in kidney, was very small. Residual cytosolic activities hydrolysing Glu-Trp were sensitive to inhibition by 2.5 mM-N-ethylmaleimide. The activity of aminopeptidase W was unaffected by these inhibitors. There was good correlation between the fluorimetric assay and those in which the free tryptophan released by kidney membrane fractions was determined by h.p.l.c. or the aminopeptidase W was measured immunoradiometrically with a monoclonal antibody.

Martínez-Martos, José Manuel, María Correa-Rodríguez, Alma Rus, Francisco Molina, María Jesús Ramírez-Expósito et María Encarnación Aguilar-Ferrandiz. « Altered Serum Oxytocinase and Enkephalin-Degrading Aminopeptidase Activities in Patients With Fibromyalgia ». Biological Research For Nursing 21, n^o 4 (26 mai 2019) : 431–39. http://dx.doi.org/10.1177/1099800419854207.

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Objectives: Fibromyalgia (FM) is a chronic pain condition of unclear etiology. We have analyzed, for the first time, the activity of a broad spectrum of aminopeptidases (APs) in patients with FM and controls to investigate whether they are involved in the pathophysiology of this syndrome. Method: In this case–control study, we fluorometrically measured specific AP activities in serum samples of 75 patients with FM and 29 healthy controls. The predictive value of AP activities in FM was determined by receiver operating characteristic (ROC) analysis. Results: Oxytocinase activity was higher in patients with FM than in controls ( p < .001). A subgroup of patients with FM ( n = 18; 24%) showed low levels of enkephalin-degrading aminopeptidase (EDA) activity when compared with the healthy controls ( p < .001) and with the rest of FM patients ( p < .001). There were no significant differences in the activity levels of aminopeptidase A, aminopeptidase B, aspartyl aminopeptidase, insulin-regulated aminopeptidase, pyroglutamyl aminopeptidase, or aminopeptidase N between FM patients and controls. According to ROC analysis, oxytocinase activity may be a good marker for differentiating individuals with FM from healthy subjects. Conclusions: Our findings show that serum oxytocinase activity is increased in patients with FM, which could alter the metabolism of peptides with analgesic effects such as oxytocin and enkephalins. The determination of serum oxytocinase activity may aid in FM diagnosis. Additionally, we have identified a subpopulation of FM patients with abnormally low serum EDA activity.

ZHANG, Zhen-Zhong, Satoru NIRASAWA, Yoshiaki NAKAJIMA, Michiteru YOSHIDA et Kiyoshi HAYASHI. « Function of the N-terminal propeptide of an aminopeptidase from Vibrio proteolyticus ». Biochemical Journal 350, n^o 3 (8 septembre 2000) : 671–76. http://dx.doi.org/10.1042/bj3500671.

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An aminopeptidase from Vibrio proteolyticus was translated as a preproprotein consisting of four domains: a signal peptide, an N-terminal propeptide, a mature region and a C-terminal propeptide. Protein expression and analysis of the activity results demonstrated that the N-terminal propeptide was essential to the formation of the active enzyme in Escherichia coli. Urea dissolution of inclusion bodies and dialysis indicated that the N-terminal propeptide could facilitate the correct folding of the enzyme in vitro. Using l-Leu-p-nitroanilide as the substrate, the kinetic parameters (kcat and Km) of the pro-aminopeptidase and processed aminopeptidases were analysed. The results suggested that the N-terminal propeptide inhibited enzyme activity of the mature region. In contrast, the C-terminal propeptide did not show evidence of forming an active enzyme, of correctly folding in vitro or of inhibiting the active region.

Cunningham, Eithne, Marcin Drag, Pawel Kafarski et Angus Bell. « Chemical Target Validation Studies of Aminopeptidase in Malaria Parasites Using α-Aminoalkylphosphonate and Phosphonopeptide Inhibitors ». Antimicrobial Agents and Chemotherapy 52, n^o 9 (5 mai 2008) : 3221–28. http://dx.doi.org/10.1128/aac.01327-07.

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ABSTRACT During its intraerythrocytic phase, the most lethal human malarial parasite, Plasmodium falciparum, digests host cell hemoglobin as a source of some of the amino acids required for its own protein synthesis. A number of parasite endopeptidases (including plasmepsins and falcipains) process the globin into small peptides. These peptides appear to be further digested to free amino acids by aminopeptidases, enzymes that catalyze the sequential cleavage of N-terminal amino acids from peptides. Aminopeptidases are classified into different evolutionary families according to their sequence motifs and preferred substrates. The aminopeptidase inhibitor bestatin can disrupt parasite development, suggesting that this group of enzymes might be a chemotherapeutic target. Two bestatin-susceptible aminopeptidase activities, associated with gene products belonging to the M1 and M17 families, have been described in blood-stage P. falciparum parasites, but it is not known whether one or both are required for parasite development. To establish whether inhibition of the M17 aminopeptidase is sufficient to confer antimalarial activity, we evaluated 35 aminoalkylphosphonate and phosphonopeptide compounds designed to be specific inhibitors of M17 aminopeptidases. The compounds had a range of activities against cultured P. falciparum parasites with 50% inhibitory concentrations down to 14 μM. Some of the compounds were also potent inhibitors of parasite aminopeptidase activity, though it appeared that many were capable of inhibiting the M1 as well as the M17 enzyme. There was a strong correlation between the potencies of the compounds against whole parasites and against the enzyme, suggesting that M17 and/or M1 aminopeptidases may be valid antimalarial drug targets.

Wanat, Weronika, Michał Talma, Małgorzata Pawełczak et Paweł Kafarski. « Phosphonic Acid Analogues of Phenylglycine as Inhibitors of Aminopeptidases : Comparison of Porcine Aminopeptidase N, Bovine Leucine Aminopeptidase, Tomato Acidic Leucine Aminopeptidase and Aminopeptidase from Barley Seeds ». Pharmaceuticals 12, n^o 3 (17 septembre 2019) : 139. http://dx.doi.org/10.3390/ph12030139.

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The inhibitory activity of 14 racemic phosphonic acid analogs of phenylglycine, substituted in aromatic rings, towards porcine aminopeptidase N (pAPN) and barley seed aminopeptidase was determined experimentally. The obtained patterns of the inhibitory activity against the two enzymes were similar. The obtained data served as a basis for studying the binding modes of these inhibitors by pAPN using molecular modeling. It was found that their aminophosphonate fragments were bound in a highly uniform manner and that the difference in their affinities most likely resulted from the mode of substitution of their phenyl rings. The obtained binding modes towards pAPN were compared, with these predicted for bovine lens leucine aminopeptidase (blLAP) and tomato acidic leucine aminopeptidase (tLAPA). The performed studies indicated that the binding manner of the phenylglycine analogs to biLAP and tLAPA are significantly similar and differ slightly from that predicted for pAPN.

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Thèses sur le sujet "Aminopeptidase N":

Al-Lakkis, Mira. « Application des dérivés d'amino-benzosubérone : inhibition sélective des aminopeptidases mono ou bimétalliques ». Phd thesis, Université de Haute Alsace - Mulhouse, 2012. http://tel.archives-ouvertes.fr/tel-01060176.

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Les aminopeptidases sont des cibles thérapeutiques importantes pour plusieurs maladies, car elles sont impliquées dans divers processus physiologiques et pathologiques comme la progression tumorale, l'angiogenèse, et certaines infections (virales, bactériennes, et parasitaires). Il en existe deux classes : les aminopeptidases avec un ion métallique (Aminopeptidase N [APN ou CD13] et leukotrien A4 hydrolase [LTA4H]) et les aminopeptidases avec deux ions métalliques (Aminopeptidase de l'Aeromonas proteolytica [APaero], Leucine Aminopeptidase cytosolique [LAPc] et Méthionine aminopeptidase 1 ou 2 [MetAP]). Deux types de composés dérivés des amino-benzosubérones ont été envisagés pour inhiber sélectivement chacune de ces classes d'aminopeptidases. L'étude des relations structures-activités (RSA) nous a permis de découvrir une molécule très puissante et sélective de l'APN (Ki 60 pM). L'APN est une enzyme monométallique considérée aujourd'hui comme une nouvelle cible pour la lutte contre le cancer car son inhibition bloque le processus de l'angiogenèse et donc la progression tumorale. L'étude d'une nouvelle classe de molécules trisubstituées dérivées des aminobenzosubérones a abouti à la découverte d'une seconde molécule active et sélective des enzymes bimétalliques notamment l'APaero (Ki 10 nM).

Lai, Amy M. « Role of aminopeptidase N in wound healing ». Thesis, University of British Columbia, 2011. http://hdl.handle.net/2429/39957.

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The dynamics and complexity of tissue repair are dominated by specific and intricately coordinated cellular events. Disruptions at the level of cellular communication are associated with imbalanced extracellular matrix (ECM) synthesis/degradation leading to fibrosis and chronic wounds. Our group has demonstrated that 14-3-3 sigma (also known as stratifin) functions as a stimulator of matrix metalloproteinase-1 (MMP-1) through interactions with aminopeptidase N (APN) on the surface of dermal fibroblasts. In this doctoral research project, it is hypothesized that APN functions as a receptor for keratinocyte-derived paracrine signals that control the expression of key ECM components in dermal fibroblasts. Three specific objectives were accomplished in this project. Under Objective 1, the nature of APN expression in an environment of active epithelial-stromal communication was examined using an in vitro keratinocyte-fibroblast crosstalk model. The fibroblast expression of APN was significantly upregulated in the presence of keratinocyte-releasable soluble factors, of which stratifin was shown to be a potent stimulator. In light of the recent identification of APN as a receptor responsible for stratifin-mediated p38 MAPK activation leading to upregulation of MMP-1, the role of APN as a transmembrane mediator of signals that regulate ECM remodeling was investigated in Objective 2. Comparative analysis of the expression profiles of 118 ECM genes under conditions of keratinocyte stimulation and APN gene silencing revealed a group of key matrix proteases and adhesion molecules influenced by keratinocyte-derived signaling mediated through APN. The aim of Objective 3 was to explore the therapeutic potential of targeting APN in cutaneous tissue repair. Topical application of an APN-neutralizing antibody on full-thickness skin wounds in a murine model had a positive outcome in healing. Acceleration of wound closure was accompanied by increased collagen deposition and fibroblast contractility. Collectively, the findings presented herein confirmed our hypothesis that APN can be induced by keratinocytes and acts as a regulator of keratinocyte-derived stimuli in epidermal-dermal communication. Specifically, these findings support the receptor role of APN in mediating transmembrane signals derived from keratinocytes, and provide encouraging evidence for further investigations on the therapeutic use of APN agonist/antagonists in the field of tissue repair.

Sansot, Jean-Luc. « Alanine aminopeptidase approches biochimique et toxicologique / ». Grenoble 2 : ANRT, 1986. http://catalogue.bnf.fr/ark:/12148/cb376010389.

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Golich, Frank Carl. « Structural and Functional Characterization of Aminopeptidase N (PEPN) from Escherichia coli ». Miami University / OhioLINK, 2006. http://rave.ohiolink.edu/etdc/view?acc_num=miami1143229893.

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Fiddler, Christine Alison. « Role of aminopeptidase N/CD13 in neutrophil migration and aggregation ». Thesis, University of Cambridge, 2015. https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.708480.

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Gillingham, Helen. « Role and regulation of aminopeptidase N (CD13) in HT1080 fibrosarcoma cells ». Thesis, University of Cambridge, 2012. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.610322.

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Roux, Lionel. « Conception et synthèse d'inhibiteurs de l'Aminopeptidase membranaire N ([EC. 3.4.11.2], APN ou CD13) ». Thesis, Mulhouse, 2010. http://www.theses.fr/2010MULH4691/document.

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La lutte contre le cancer est l'un des défis majeurs du XXème siècle. Pour que les tumeurs puissent se développer dans l'organisme, elles ont besoin d'un apport en nutriment par le biais de vaisseaux sanguins pour se faire, elles vont avoir recours au processus angiogénique. Lors de ce processus, les cellules endothéliales qui tapissent la paroi des vaisseaux sanguins vont se multiplier et créer de nouveaux vaisseaux sanguins qui vont permettre la vascularisation des tumeurs. L'angiogenèse constitue donc aujourd'hui un axe de recherche pour la lutte contre la progression tumorale et donc contre le cancer. Lors de ce développement tumoral, une enzyme, l'aminopeptidase neutre APN est surexprimée sur les parois des cellules endothéliales. Différentes études ont été menées et montrent que l'inhibition de cette enzyme bloque la progression tumorale. Mon travail au sein de l'équipe du Pr Céline Tarnus consistait en la conception et la synthèse d'inhibiteurs de l'APN. Une relation structure activité de nos composés vis-à-vis de l'APN a tout d'abord été effectuée. Le développement de synthèse du composé le plus actif ont été faite, puis la synthèse d'inhibiteurs d'APN ayant pour objectif l'utilisation de la BNCT a été abordée
The fight against the cancer is one of the most important struggles of this century. For the development of the tumors inside the body, they need to receive nutriments by the blood vessels and they use the angiogenic process. During this process, the endothelial cells being shown on the wall of the blood vessel will multiply and design new blood vessel, which will allow the tumor's vascularisation. Today, the angiogenesis is an axis of research for the fight against the cancer. During the tumoral development, the aminopeptidase N (APN) is overexpressed on the wall of endothelial cells. Various studies have shown that the inhibition of this enzyme stops the tumoral progression. My work in the Pr. Céline Tarnus Team consists in the conception and the synthesis of APN's inhibitors. In a first time, a structure activity relationship has been realized. Syntheses of a subnamolar compound have been developed, and then the synthesis of APN's inhibitors with the use of BNCT has been got onto

Al-Masri, Mounir. « Conception, synthèse et évaluation des dérivés d'aminobenzosubérone comme inhibiteurs potentiels des aminopeptidases de la famille M1 ». Thesis, Mulhouse, 2017. http://www.theses.fr/2017MULH2862.

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Les aminopeptidases de la famille M1 sont des protéases qui catalysent l’hydrolyse d’une liaison peptidique en position N-terminale. Ce sont des métalloprotéases avec un ion zinc dans leur site actif conservé dans tous les membres de cette famille de protéine. Ces enzymes sont impliqués dans de nombreux processus physiologiques normaux, mais également dans des désordres métaboliques, tels que la progression tumorale, des maladies auto-immunes, ainsi que dans des infections virales, bactériennes et parasitaires. Pour ces raisons, ces aminopeptidases sont considérées comme des cibles thérapeutiques potentielles pour traiter ou diagnostiquer diverses maladies. En 2006, le laboratoire a découvert le châssis moléculaire de type 3-amino-2-benzosubérone inhibant puissamment et sélectivement et un des membres de cette famille d’aminopeptidases, à savoir l’APN. La conception et la synthèse des dérivés de ce châssis moléculaire comme inhibiteurs potentiels et sélectifs pour cinq autres membres de la famille M1 (APN, ERAP1/2, IRAP et PfA-M1) est au cœur de ce travail. Des études pharmacologiques, pharmacocinétiques jusqu’aux essais précliniques ont été menées et leurs résultats seront présentés dans le cas de l’inhibition de PfA-M1
Aminopeptidases of the M1 family are proteases that catalyze the hydrolysis of a peptide bond in the N-terminal position. These are metalloproteases with a zinc ion in their active site conserved in all members of this protein family. These enzymes are involved in many normal physiological processes, but also in metabolic disorders, such as tumor progression, autoimmune diseases, as well as in viral, bacterial and parasitic infections. For these reasons, these aminopeptidases are considered potential therapeutic targets for treating or diagnosing various diseases. In 2006, the laboratory discovered the powerful and selectively inhibiting 3-amino-2-benzosuberone molecular chassis and one of the members of this family of aminopeptidases, namely the APN. The design and synthesis of derivatives of this molecular chassis as potential and selective inhibitors for five other members of the M1 family (APN, ERAP1 / 2, IRAP and PfA-M1) is at the heart of this work. Pharmacological, pharmacokinetic and preclinical studies have been conducted and their results will be presented in the case of PfA-M1 inhibition

Geisler, Michael. « Untersuchung der Regulation der Promotoraktivität von Aminopeptidase N (APN) in hämatopoietischen Zellen ». [S.l.] : [s.n.], 2005. http://deposit.ddb.de/cgi-bin/dokserv?idn=975657801.

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Frottin, Frédéric. « Analyse intégrative du rôle de l’excision de la méthionine N-terminale dans le cytoplasme des eucaryotes supérieurs ». Thesis, Paris 11, 2011. http://www.theses.fr/2011PA112045/document.

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Le premier acide aminé incorporé dans une chaîne polypeptidique naissante est toujours la méthionine. On identifie donc toujours ce premier résidu à la méthionine N-terminale. Cependant, les deux tiers des protéines accumulées à l’état stationnaire ne présentent plus leur méthionine initiatrice. Cet enlèvement résulte essentiellement d’une maturation protéolytique affectant chaque protéine. Ainsi, l’Excision de la Méthionine N-terminale (NME) concerne la majorité des protéines et ce dès que les premiers résidus émergent du ribosome. Ce mécanisme est retrouvé dans tous les compartiments cellulaires où une synthèse protéique a lieu : le cytoplasme, les plastes et les mitochondries. Les enzymes responsables du clivage de la méthionine initiatrice sont les METhionine AminoPeptidases (METAPs) ; les METAPs sont conservées dans le Règne vivant. Des études fonctionnelles de délétions géniques ont montré le caractère létal du maintien de la première méthionine dans tous les organismes. Il y a plus de dix ans, les METAPs ont été identifiées comme étant la cible de composés naturels ayant des effets anticellulaires. Aujourd’hui un nombre croissant d’études rapportent que la NME est une cible prometteuse pour le traitement de nombreuses pathologies. Néanmoins, les bases moléculaires qui expliquent le caractère essentiel de la NME restent très peu comprises, en particulier dans le cytoplasme des eucaryotes supérieurs. Grâce à un système inductible permettant de moduler finement la NME cytoplasmique dans la plante modèle Arabidopsis thaliana et différentes approches incluant des analyses protéomiques et métabolomiques, j’ai pu étudier les événements moléculaires précoces associés à l’inhibition de la NME cytoplasmique. J’ai également caractérisé la contribution relative des deux types de METAP cytoplasmiques au processus. Dans ce contexte, j’ai pu démontrer chez A. thaliana que la NME cytoplasmique agit sur deux voies de signalisation fréquemment dérégulées lors de conditions pathologiques : le statut des composés thiolés et la protéolyse. La diminution de la NME cytoplasmique induit une protéolyse accrue principalement via une augmentation du nombre de protéines destinées à une dégradation rapide. Ainsi, l’activité de la NME, en modulant la sensibilité de nombreuses protéines à subir la protéolyse, est un élément fondamental de la régulation de la demi-vie protéique. Finalement, mes résultats simialires obtenus également chez les Archées, levures et les lignées de cellules humaines suggèrent l’existence d’un mécanisme ubiquitaire associé à la NME
The first amino acid incorporated in nascent polypeptide chain is always methionine so called N-terminale methionine. However, in a given proteome, more than fifty percent of proteins have not this first methionine. Indeed, the early proteolytic event affecting a majority of proteins is N-terminal Methionine Excision (NME) as soon as few residues exit from the ribosome. Enzymes ensuring NME process are conserved along species. This mechanism takes place in all compartments where protein synthesis occurs including cytoplasm, plastids and mitochondria and the enzymes responsible of N-methionine excision are METhionine AminoPeptidases (METAP). Early functional studies of gene deletion has quickly showed that NME is an essential process. Ten years ago, METAPs have been identified as the molecular target of natural compounds with anticancer activities. Now, a growing number of studies suggest that NME is a promising target for treatment of various deseases. Nevertheless, molecular mechanisms making NME an essential process is poorly understood in particular in higher eukaryote cytoplasms.Using a dedicated inducible system in the model organism Arabidopsis thaliana and multiple approaches, including proteomics and metabolomics, I examined the earliest molecular events associated with the inhibition of this process and the contribution of both METAP to NME process. In this context, I demonstrated that cytoplasmic NME in A. thaliana orchestrates a cross-talk between two fundamental signaling pathways frequently deregulated in pathological conditions: thiol status and proteolysis. In these studies, we demonstrated that developmental defects induced by cytoplasmic NME inhibition are associated with an increase of the proteolytic activity due to an increase of the proteins available for rapid degradation. Thus, NME activity that modifies the availability of several proteins for degradation is an integral and fundamental element protein turnover regulation. Finally my preliminary results obtained in Archea, Fungi and human cells seem to suggest the existence of a ubiquitous mechanism associated with NME process

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Livres sur le sujet "Aminopeptidase N":

name, No. Ectopeptidases : CD13/aminopeptidase N and CD26/dipeptidylpeptidase IV in medicine and biology. New York, NY : Kluwer Academic/Plenum, 2003.

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See, Hilario. Purification of the major stilbene disulfonate- and concanavalin A-binding protein (GP130) of the porcine renal brush border membrane and its identification as aminopeptidase N. Ottawa : National Library of Canada, 1990.

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Langner, Jürgen, et Siegfried Ansorge. Ectopeptidases : CD13/Aminopeptidase N and CD26/Dipeptidylpeptidase IV in Medicine and Biology. Springer, 2012.

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(Editor), Jürgen Langner, et Siegfried Ansorge (Editor), dir. Ectopeptidases : CD13/Aminopeptidase N and CD26/Dipeptidylpeptidase IV in Medicine and Biology. Springer, 2002.

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Chapitres de livres sur le sujet "Aminopeptidase N":

Sjöström, Hans, Ove Norén et Jørgen Olsen. « Structure and Function of Aminopeptidase N ». Dans Cellular Peptidases in Immune Functions and Diseases 2, 25–34. Boston, MA : Springer US, 2002. http://dx.doi.org/10.1007/0-306-46826-3_2.

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Olsen, Jørgen, Klaus Kokholm, Ove Norén et Hans Sjöström. « Structure and Expression of Aminopeptidase N ». Dans Advances in Experimental Medicine and Biology, 47–57. Boston, MA : Springer US, 1997. http://dx.doi.org/10.1007/978-1-4757-9613-1_7.

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Petrovic, Nenad, Wolfgang Schacke et Linda H. Shapiro. « CD13/Aminopeptidase N in Tumor Growth and Angiogenesis ». Dans Aminopeptidases in Biology and Disease, 179–200. Boston, MA : Springer US, 2004. http://dx.doi.org/10.1007/978-1-4419-8869-0_9.

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Fournié-Zaluski, Marie-Claude, et Bernard P. Roques. « New Selective Aminopeptidase N Inhibitors as Potential Therapeutics ». Dans Ectopeptidases, 51–94. Boston, MA : Springer US, 2002. http://dx.doi.org/10.1007/978-1-4615-0619-5_3.

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Delmas, Bernard, Jacqueline Gelfi, Hans Sjöström, Ove Noren et Hubert Laude. « Further Characterization of Aminopeptidase-N as a Receptor for Coronaviruses ». Dans Coronaviruses, 293–98. Boston, MA : Springer US, 1994. http://dx.doi.org/10.1007/978-1-4615-2996-5_45.

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Sato, Ryoichi. « Aminopeptidase N as a Receptor for Bacillus Thuringiensis Cry Toxins ». Dans Advances in Microbial Control of Insect Pests, 1–13. Boston, MA : Springer US, 2002. http://dx.doi.org/10.1007/978-1-4757-4437-8_1.

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Kolb, Andreas F., Annette Hegyi, Julia Maile, Angelien Heister, Margitta Hagemann et Stuart G. Siddell. « Molecular Analysis of the Coronavirus-Receptor Function of Aminopeptidase N ». Dans Advances in Experimental Medicine and Biology, 61–67. Boston, MA : Springer US, 1998. http://dx.doi.org/10.1007/978-1-4615-5331-1_8.

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Tresnan, Dina B., et Kathryn V. Holmes. « Feline Aminopeptidase N is a Receptor for All Group I Coronaviruses ». Dans Advances in Experimental Medicine and Biology, 69–75. Boston, MA : Springer US, 1998. http://dx.doi.org/10.1007/978-1-4615-5331-1_9.

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Löhn, M., C. Mueller, K. Thiele, T. Kähne, D. Riemann et J. Langner. « Aminopeptidase N-Mediated Signal Transduction and Inhibition of Proliferation of Human Myeloid Cells ». Dans Advances in Experimental Medicine and Biology, 85–91. Boston, MA : Springer US, 1997. http://dx.doi.org/10.1007/978-1-4757-9613-1_12.

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Thiele, Katja, Dagmar Riemann, Astrid Kehlen, Matthias Löhn, Lotte K. Vogel et Jürgen Langner. « Two Transfected Endothelial Cell Lines Expressing High Levels of Membrane Bound or Soluble Aminopeptidase N ». Dans Advances in Experimental Medicine and Biology, 81–84. Boston, MA : Springer US, 1997. http://dx.doi.org/10.1007/978-1-4757-9613-1_11.

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Actes de conférences sur le sujet "Aminopeptidase N":

James, J., M. Valuparampil Varghese, O. Rafikova et R. Rafikov. « Aminopeptidase-N Triggers Uncontrolled Proliferation of Pulmonary Artery Smooth Muscle Cells ». Dans American Thoracic Society 2021 International Conference, May 14-19, 2021 - San Diego, CA. American Thoracic Society, 2021. http://dx.doi.org/10.1164/ajrccm-conference.2021.203.1_meetingabstracts.a3644.

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Katsumata, M., et S. Wilkinson. « Diurnal variations of activities of disaccharidases and aminopeptidase N in growing barrows ». Dans 6th EAAP International Symposium on Energy and Protein Metabolism and Nutrition. The Netherlands : Wageningen Academic Publishers, 2019. http://dx.doi.org/10.3920/978-90-8686-891-9_90.

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Wickström, Malin, Kristina Viktorsson, Lovisa Lundholm, Reidun Aesoy, Helen Nygren, Linda Sooman, Mårten Fryknäs, Rolf Lewensohn, Rolf Larsson et Joachim Gullbo. « Abstract B187 : Role of aminopeptidase N in the activation of the alkylating prodrug J1 ». Dans Abstracts : AACR-NCI-EORTC International Conference : Molecular Targets and Cancer Therapeutics--Nov 15-19, 2009 ; Boston, MA. American Association for Cancer Research, 2009. http://dx.doi.org/10.1158/1535-7163.targ-09-b187.

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Huang, Qing, Yong Wang, Wenjie Zhu, Shibin Ai, Elfed Lewis et Minghong Yang. « Aminopeptidase N (CD13) Modified Gold Films for the Affinity Quantitative Detection of CNGRC-coupled Derivative ». Dans 2019 18th International Conference on Optical Communications and Networks (ICOCN). IEEE, 2019. http://dx.doi.org/10.1109/icocn.2019.8934768.

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Laitinen, Sara, Malin Wickstrom, Peder Fredlund Fuchs, Par Gerwins, Rolf Larsson et Joachim Gullbo. « Abstract B6 : Aminopeptidase N-activated prodrug melphalan-flufenamide (J1) inhibits angiogenesis in vitro and in vivo. » Dans Abstracts : AACR-NCI-EORTC International Conference : Molecular Targets and Cancer Therapeutics--Nov 12-16, 2011 ; San Francisco, CA. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1535-7163.targ-11-b6.

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Kadefors, Måns, Sara Rolandsson Enes, Maria Weitoft, Stefan Scheding et Gunilla Westergren-Thorsson. « Late Breaking Abstract - Aminopeptidase N/CD13 distinguishes two populations of colony-forming mesenchymal stromal cells in human lung tissue ». Dans ERS International Congress 2020 abstracts. European Respiratory Society, 2020. http://dx.doi.org/10.1183/13993003.congress-2020.4467.

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Rapports d'organisations sur le sujet "Aminopeptidase N":

Yeager, Curtis. Identification of Aminopeptidase N as a Cellular Receptor for Human Coronavirus-229E. Fort Belvoir, VA : Defense Technical Information Center, avril 1992. http://dx.doi.org/10.21236/ad1011150.

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Wong, Eric A., et Zehava Uni. Nutrition of the Developing Chick Embryo : Nutrient Uptake Systems of the Yolk Sac Membrane and Embryonic Intestine. United States Department of Agriculture, juin 2012. http://dx.doi.org/10.32747/2012.7697119.bard.

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We have examined the developmental changes in composition, amount, and uptake of yolk nutrients (fat, protein, water and carbohydrates) and the expression ofnutrient transporters in the yolk sac membrane (YSM) from embryonic day 11 (Ell) to 21 (E21) and small intestine from embryonic day 15 (E15) to E21 in embryos from young (22-25 wk) and old (45-50 wk) Cobb and Leghorn breeder flocks. The developmental expression profiles for the peptide transporter 1 (PepTl), the amino acid transporters, EAAT3, CAT-1 and BOAT, the sodium glucose transporter (SGLTl), the fructose transporter (GLUT5), the digestive enzymes aminopeptidase N (APN) and sucraseisomaltase (SI) were assayed by the absolute quantification real time PCR method in the YSM and embryonic intestine. Different temporal patterns of expression were observed for these genes. The effect of in ovo injection of peptides (the dipeptide Gly-Sar, purified peptides, trypsin hydrolysate) on transporter gene expression has been examined in the embryonic intestine. Injection of a partial protein hydrolysate resulted in an increase in expression of the peptide transporter PepT2. We have initiated a transcriptome analysis of genes expressed in the YSM at different developmental ages to better understand the function of the YSM.