Results 201 to 210 of about 27,424 (235)
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Enkephalin Metabolism by Microglia Aminopeptidase N (CD13)

Journal of Neurochemistry, 1995
Abstract: Rat microglia in culture showed a high capacity to degrade neuropeptides compared with other glial cells. Leu‐enkephalin was readily hydrolyzed to free tyrosine and Gly‐Gly‐Phe‐Leu. Inhibition experiments and immunostaining revealed that aminopeptidase N (CD13) on the surface of microglia was responsible for enkephalin cleavage. Endopeptidase‐
R, Lucius, J, Sievers, R, Mentlein
openaire   +2 more sources

Cell-Membrane-Localizing Fluorescence Probes for Aminopeptidase N

ACS Sensors, 2023
Aminopeptidase N (APN), a transmembrane ectoenzyme, plays multifunctional roles in cell survival and migration, angiogenesis, blood pressure regulation, and viral uptake. Abnormally high levels of the enzyme can be found in some tumors and injured liver and kidney.
Yun Jae Yang, Mingchong Dai, Kyo Han Ahn
openaire   +2 more sources

Human aminopeptidase N is encoded by 20 exons

Mammalian Genome, 1996
Aminopeptidase ...
Lerche, C   +4 more
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Human aortic endothelial cell aminopeptidase N

Immunopharmacology, 1996
Aminopeptidase N (AmN) (EC 3.4.11.2) may function in part to degrade peptide hormones (Bausback and Ward, 1986; Kenny et al., 1989; Palmeiri et al., 1985; Ryan et al., 1993). AmN is capable of degrading angiotensin III, Lys-bradykinin, enkephalins and some enkephalin higher homologs (Bausback and Ward, 1986).
A, Papapetropoulos   +6 more
openaire   +2 more sources

Discovery of Bioluminogenic Probes for Aminopeptidase N Imaging

Analytical Chemistry, 2014
To find an approach that can image the hydrolysis activity of aminopeptidase N (APN) both in vitro and in vivo, three bioluminescent probes have been well designed and synthesized herein. All of them can be recognized and hydrolyzed by APN to produce bioluminescence emission in the presence of firefly luciferase.
Jing, Li   +7 more
openaire   +2 more sources

Identification of placental leucine aminopeptidase and triton-slowed aminopeptidase N in serum of pregnant women

Clinica Chimica Acta, 2009
Previously, we found characteristic triton-slowed bands of aminopeptidase N (APN) in cholestatic serum by triton-polyacrylamide gel electrophoresis (triton-PAGE) [Makoto Kawai, Yukichi Hara, Triton-polyacrylamide gel electrophoresis and leucine aminopeptidase activity staining detect Triton-slowed bands including high-molecular-mass aminopeptidase N ...
Makoto, Kawai   +3 more
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Pericytes and periendothelial cells of brain parenchyma vessels co‐express aminopeptidase N, aminopeptidase A, and nestin

Journal of Neuroscience Research, 1999
Within the parenchyma of the CNS, the endothelium of all vessels is surrounded by a layer of cells, pericytes in capillaries and periendothelial or intima smooth muscle cells in other vessels. The origin of these cell types, their relationship, and their role are unclear.
Alliot, F   +3 more
openaire   +3 more sources

Design of Aminopeptidase N Inhibitors as Anti-cancer Agents

Journal of Medicinal Chemistry, 2018
Aminopeptidase N (APN) is an important metalloenzyme. It regulates multivariate cellular functions by different mechanisms such as enzymatic cleavage of peptides. This may play a role in endocytosis and regulate signal transduction. APN, a member of the M1 zinc metallopeptidase family, plays crucial roles in a variety of functions such as migration and
Sk. Abdul Amin   +2 more
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Aminopeptidase N/CD13 and haematopoietic cells

Haema, 2003
Several cell-surface antigens defined by the cluster of differentiation (CD) nomenclature have been defined as proteins with enzymatic activity. An important example is CD13, aminopeptidase N (APN ; EC 3.4.11.2). It is a zinc-dependent membrane-bound ectopeptidase that cleaves N-terminal neutral amino acids of various peptides.
Gabrilovac, Jelka   +2 more
openaire   +1 more source

Proteolytic Fragmentation of Aminopeptidase N

Biochemical Society Transactions, 1999
Lisa D. Other, Nigel M. Hooper
openaire   +1 more source

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