Results 21 to 30 of about 27,424 (235)

Aminopeptidases do not directly degrade tau protein

Molecular Neurodegeneration, 2010
Background Tau hyperphosphorylation and aggregation to form intracellular neurofibrillar tangles is prevalent in a number of tauopathies. Thus there is current interest in the mechanisms involved in Tau clearance. It was recently reported that Tau can be
Hersh Louis B, Guan Hanjun, Chow K
doaj   +1 more source

A Radiochemical Assay for Aminopeptidase N

Analytical Biochemistry, 1993
We developed an assay for aminopeptidase N (AmN) in which substrate, Arg-Phe-[3H]anilide (24.9 Ci/mmol), can be used at concentrations (1-200 nM) well below Km (12 microM) and at or below enzyme concentration ([E]). Such reaction conditions simulate those in vivo where peptide hormones in picomolar concentrations (> [E]. Arg-Phe-[3H]anilide can be used
J W, Ryan, A Y, Chung, J A, Nearing, F A, Valido, C, Shun-Cun, P, Berryer   +5 more
openaire   +2 more sources

Expression of Aminopeptidase N on Human Choriocarcinoma Cells and Cell Growth Suppression by the Inhibition of Aminopeptidase N Activity [PDF]

Japanese Journal of Cancer Research, 1994
We previously found that an aminopeptidase inhibitor, ubenimex (bestatin), had a growth‐suppressive effect on Choriocarcinoma cell lines in vitro. To clarify the mechanism of this action, we investigated the expression of aminopeptidase N (AP‐N/CD13) on Choriocarcinoma cells and other human tumor cells. Two Choriocarcinoma cell lines, NaUCC‐4 and Be Wo,
Ino, Kazuhiko, Goto, Setsuko, Okamoto, Tomomitsu, Nomura, Seiji, Nawa, Akihiro, Isobe, Ken‐ichi, Mizutani, Shigehiko, Tomoda, Yutaka   +7 more
openaire   +2 more sources

The Effect of Different Species Aminopeptidase N Structure on the Activity Screening of Aminopeptidase N Inhibitor

Biological and Pharmaceutical Bulletin, 2010
Aminopeptidase N (APN) is a transmembrane metallopeptidase, which participates in the tumor progress such as proliferation, attachment, angiogenesis and tumor invasion. All of this makes APN as a good chemical therapeutic anti-tumor target. In the present study, we got a novel compound 16l which markedly inhibited the enzyme activity of porcine APN ...
Wang, Xuejian, Zhang, Lei, Yang, Kanghui, Zhang, Cai, Zhang, Jian, Fang, Hao, Xu, Wenfang   +6 more
openaire   +3 more sources

Further Characterization of Aminopeptidase-N as a Receptor for Coronaviruses [PDF]

, 1994
We recently reported that porcine aminopeptidase-N (pAPN) acts as a receptor for transmissible gastroenteritis virus (TGEV). In the present work, we addressed the question of whether TGEV tropism is determined only by the virus-receptor interaction. To this end, different non-permissive cell lines were transfected with the porcine APN cDNA and tested ...
Delmas, Bernard, Gelfi, Jacqueline, Sjöström, H., Noren, O., Laude, Hubert   +4 more
openaire   +3 more sources

Urinary aminopeptidase activities as early and predictive biomarkers of renal dysfunction in cisplatin-treated rats. [PDF]

PLoS ONE, 2012
This study analyzes the fluorimetric determination of alanyl- (Ala), glutamyl- (Glu), leucyl-cystinyl- (Cys) and aspartyl-aminopeptidase (AspAp) urinary enzymatic activities as early and predictive biomarkers of renal dysfunction in cisplatin-treated ...
Andrés Quesada, Félix Vargas, Sebastián Montoro-Molina, Francisco O'Valle, María Dolores Rodríguez-Martínez, Antonio Osuna, Isabel Prieto, Manuel Ramírez, Rosemary Wangensteen   +8 more
doaj   +1 more source

Functional residues at the active site of aminopeptidase N [PDF]

European Journal of Biochemistry, 1991
Sequence analysis of aminopeptidase N has shown that this zinc exopeptidase contains a consensus sequence (Val‐Xaa‐Xaa‐His‐Glu‐Xaa‐Xaa‐His), generally found at the active site of zinc endopeptidases [Jongeneel, C. V., Bouvier, J. and Bairoch, A. (1989) FEBS Lett. 242, 211–214].
A, Helene, A, Beaumont, B P, Roques
openaire   +2 more sources

Impaired angiogenesis in aminopeptidase N-null mice [PDF]

Proceedings of the National Academy of Sciences, 2007
Aminopeptidase N (APN, CD13; EC 3.4.11.2) is a transmembrane metalloprotease with several functions, depending on the cell type and tissue environment. In tumor vasculature, APN is overexpressed in the endothelium and promotes angiogenesis. However, there have been no reports ofin vivoinactivation of the APN gene to validate these findings.
Roberto, Rangel, Yan, Sun, Liliana, Guzman-Rojas, Michael G, Ozawa, Jessica, Sun, Ricardo J, Giordano, Carolyn S, Van Pelt, Peggy T, Tinkey, Richard R, Behringer, Richard L, Sidman, Wadih, Arap, Renata, Pasqualini   +11 more
openaire   +2 more sources

Gene cloning and sequencing of aminopeptidase N3, a putative receptor for Bacillus thuringiensis insecticidal Cry1Ac toxin in Helicoverpa armigera (Lepidoptera: Noctuidae)

European Journal of Entomology, 2005
A cDNA encoding aminopeptidase N3 was cloned by degenerated PCR and RACE techniques. The full-length of APN3harm is 3486bp. Open reading frame is 3042bp in length, encoding 1014 amino acid residues.
Gui-Rong WANG, Ge-Mei LIANG, Kong-Ming WU, Yu-Yuan GUO   +3 more
doaj   +1 more source

Biliary aminopeptidase-N and the cholesterol crystallization defect in cholelithiasis

, 1995
Several biliary proteins have cholesterol crystallisation promoting activity. One of these glycoproteins is aminopeptidase-N, a canalicular ectoenzyme. This study attempted to localise aminopeptidase-N along the biliary tree, to assess its concentration ...
Mingrone, G., Greco, A., Núñez, L., Pimentel González, Eduardo Fernando, Garrido Negri, Jorge, Nervi Oddone, Flavio, Rigotti Rivera, Attilio Gianpietro, Puglielli, L., Amigo Boker, Ludwig Peter, Raddatz Echavarría, Alejandro, González, S., Miquel Poblete, Juan Francisco   +11 more
core   +1 more source