scholarly journals Quaternary benzo[c]phenanthridine alkaloids as inhibitors of aminopeptidase N and dipeptidyl peptidase IV

2002 ◽  
Vol 16 (1) ◽  
pp. 84-87 ◽  
Author(s):  
Aleksi Šedo ◽  
Květoslava Vlašicová ◽  
Petr Barták ◽  
Radim Vespalec ◽  
Jaroslav Vičar ◽  
...  
Keyword(s):  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv ◽  
Aminopeptidase N

Modulation of cytokine production and silica-induced lung fibrosis by inhibitors of aminopeptidase N and of dipeptidyl peptidase-IV-related proteases

Life Sciences ◽  
2009 ◽  
Vol 84 (1-2) ◽  
pp. 1-11 ◽  
Author(s):  
Ulrike C. Kühlmann ◽  
Caroline E. Chwieralski ◽  
Sybille van den Brule ◽  
Christoph Röcken ◽  
Dirk Reinhold ◽  
...  
Keyword(s):  
Lung Fibrosis ◽  
Cytokine Production ◽  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv ◽  
Aminopeptidase N

scholarly journals Membrane peptidases in the pig choroid plexus and on other cell surfaces in contact with the cerebrospinal fluid

1989 ◽  
Vol 259 (1) ◽  
pp. 69-80 ◽  
Author(s):  
A Bourne ◽  
K Barnes ◽  
B A Taylor ◽  
A J Turner ◽  
A J Kenny
Keyword(s):  
Cerebrospinal Fluid ◽  
Choroid Plexus ◽  
Subcellular Fractionation ◽  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv ◽  
Aminopeptidase N ◽  
Endothelial Lining ◽  
Electron Microscopic ◽  
Endopeptidase 24.11 ◽  
Carboxypeptidase M

A comprehensive survey of 11 peptidases, all of which are markers for renal microvillar membranes, has been made in membrane fractions prepared from pig choroid plexus. Two fractionation schemes were explored, both depending on a MgCl2-precipitation step, the preferred one having advantages in speed and yield of the activities. The specific activities of the peptidases in the choroid-plexus membranes were, with the exception of carboxypeptidase M, lower than in renal microvillar membranes: those of aminopeptidase N, peptidyl dipeptidase A (‘angiotensin-converting enzyme’) and gamma-glutamyltransferase were 3-5-fold lower, those of aminopeptidase A and endopeptidase-24.11 were 12-15 fold lower, and those of dipeptidyl peptidase IV and aminopeptidase W were 50-70-fold lower. Carboxypeptidase M had a similar activity in both membranes. Alkaline phosphatase and (Na+ + K+)-activated ATPase were more active in the choroid-plexus membranes. No activity for microsomal dipeptidase, aminopeptidase P and carboxypeptidase P could be detected. Six of the peptidases and (Na+ + K+)-activated ATPase were also studied by immunoperoxidase histochemistry at light- and electron-microscopic levels. Endopeptidase-24.11 and (Na+ + K+)-activated ATPase were uniquely located on the brush border, and the other two peptidases appeared to be much more abundant on the endothelial lining of microvessels. Dipeptidyl peptidase IV and aminopeptidase W were also detected in microvasculature. Pial membranes associated with the brain and spinal cord also stained positively for endopeptidase-24.11, aminopeptidase N and peptidyl dipeptidase A. The immunohistochemical studies indicated the subcellular fractionation did not discriminate between membranes derived from epithelial cells (i.e. microvilli) and those from endothelial cells. The possible significance of these studies in relation to neuropeptide metabolism and the control of cerebrospinal fluid production is discussed.

Expression of aminopeptidase N and dipeptidyl peptidase IV in the healthy and asthmatic bronchus

1997 ◽  
Vol 56 ◽  
pp. 154-155
Author(s):  
Vincent H.J. van der Velden ◽  
Annet Wierenga-Wolf ◽  
Petra W.C. Adriaansen-Soeting ◽  
Gertrude M. Möller ◽  
Henk C. Hoogsteden ◽  
...  
Keyword(s):  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv ◽  
Aminopeptidase N

Caveolae/lipid rafts in fibroblast-like synoviocytes: ectopeptidase-rich membrane microdomains

2001 ◽  
Vol 354 (1) ◽  
pp. 47-55 ◽  
Author(s):  
Dagmar RIEMANN ◽  
Gert H. HANSEN ◽  
Lise-Lotte NIELS-CHRISTIANSEN ◽  
Evy THORSEN ◽  
Lissi IMMERDAL ◽  
...  
Keyword(s):  
Cell Activation ◽  
Hot Spot ◽  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv ◽  
Cell Interactions ◽  
Aminopeptidase N ◽  
Membrane Microdomains ◽  
Cholesterol Depletion ◽  
Fibroblast Like Synoviocytes ◽  
Cell Cell

Membrane peptidases play important roles in cell activation, proliferation and communication. Human fibroblast-like synoviocytes express considerable amounts of aminopeptidase N/CD13, dipeptidyl peptidase IV/CD26, and neprilysin/CD10, transmembrane proteins previously proposed to be involved in the regulation of intra-articular levels of neuropeptides and chemotactic mediators as well as in adhesion and cell–cell interactions. Here, we report these peptidases in synoviocytes to be localized predominantly in glycolipid- and cholesterol-rich membrane microdomains known as ‘rafts’. At the ultrastructural level, aminopeptidase N/CD13 and dipeptidyl peptidase IV/CD26 were found in caveolae, in particular in intracellular yet surface-connected vesicle-like structures and ‘rosettes’ made up of several caveolae. In addition, clusters of peptidases were seen at the cell surface in flat patches ranging in size from about 60 to 160nm. Cholesterol depletion of synoviocytes by methyl-β-cyclodextrin disrupted > 90% of the caveolae and reduced the raft localization of aminopeptidase N/CD13 without affecting Ala-p-nitroanilide-cleaving activity of confluent cell cultures. In co-culture experiments with T-lymphocytes, cholesterol depletion of synoviocytes greatly reduced their capability to induce an early lymphocytic expression of aminopeptidase N/CD13. We propose caveolae/rafts to be peptidase-rich ‘hot-spot’ regions of the synoviocyte plasma membrane required for functional cell–cell interactions with lymphocytes. The peptidases may act in concert with other types of proteins such as receptors and signal transducers localized in these specialized membrane domains.

Dual Inhibition of Dipeptidyl Peptidase IV and Aminopeptidase N Suppresses Inflammatory Immune Responses

2007 ◽  
Vol 1110 (1) ◽  
pp. 402-409 ◽  
Author(s):  
D. REINHOLD ◽  
A. BITON ◽  
A. GOIHL ◽  
S. PIEPER ◽  
U. LENDECKEL ◽  
...  
Keyword(s):  
Immune Responses ◽  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv ◽  
Aminopeptidase N ◽  
Dual Inhibition

scholarly journals A survey of membrane peptidases in two human colonic cell lines, Caco-2 and HT-29

1992 ◽  
Vol 284 (2) ◽  
pp. 595-601 ◽  
Author(s):  
S Howell ◽  
A J Kenny ◽  
A J Turner
Keyword(s):  
Cell Surface ◽  
Cell Lines ◽  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv ◽  
Aminopeptidase N ◽  
Endopeptidase 24.11 ◽  
Passage Number ◽  
Aminopeptidase P ◽  
Carboxypeptidase M ◽  
Ht 29

The expression of cell-surface peptidases was examined in two human colon carcinoma cell lines, Caco-2 and HT-29. Enzymic assays revealed the presence of eight cell-surface peptidases on a Caco-2 cell line (passage number 82-88), namely aminopeptidase N, dipeptidyl peptidase IV, peptidyl dipeptidase A (angiotension-converting enzyme), aminopeptidase P, aminopeptidase W, endopeptidase-24.11, gamma-glutamyl transpeptidase and membrane dipeptidase. The presence of dipeptidyl peptidase IV and endopeptidase-24.11 was also confirmed immunochemically. After 15 days culture, the activities of aminopeptidase P, peptidyl dipeptidase A and alkaline phosphatase activities on Caco-2 cells reached a plateau, and that of membrane dipeptidase began to decline. In contrast, aminopeptidase N, dipeptidyl peptidase IV and endopeptidase-24.11 activities were still rising after 26 days in culture. Caco-2 cells of passage number 181-183 were found to lack endopeptidase-24.11, but maintained dipeptidyl peptidase IV expression. Two populations of HT-29 cells were surveyed. Both the standard, undifferentiated population and a differentiated population expressed only three peptidases: dipeptidyl peptidase IV, aminopeptidase W and carboxypeptidase M. In the differentiated HT-29 cells the activity of dipeptidyl peptidase IV after 14-21 days was beginning to plateau whereas aminopeptidase W activity was still rising and that of carboxypeptidase M had begun to decline. These differences in activity profiles observed among this group of cell-surface peptidases indicate that these cell lines, especially Caco-2, are useful models to study the regulation of their expression.

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