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.

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.

Detection of dipeptidyl peptidase IV in glioma C6 and neuroblastoma SK-N-SH cell lines

1995 ◽  
Vol 73 (1-2) ◽  
pp. 113-115 ◽  
Author(s):  
Aleksi Sedo ◽  
Roberto P. Revoltella
Keyword(s):  
Cell Surface ◽  
Cell Line ◽  
Cell Lines ◽  
Neuroblastoma Cell ◽  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv ◽  
Human Neuroblastoma Cell ◽  
Fluorescent Substrate ◽  
Human Neuroblastoma ◽  
Dpp Iv

The dipeptidyl peptidase IV (DPP-IV) activity of the rat glioma cell line C6 and the human neuroblastoma cell line SK-N-SH was investigated. DPP-IV fluorescent substrate was cleaved by both cell lines. The pH reaction optimum determined was typical for DPP-IV described in other cell models. The reaction was inhibited by specific inhibitors diprotins A and B. Enzyme activity was localized, both on the cell surface and intracellularly. Most of the DPP-IV activity was membrane bound. However, soluble intra-cellular activity was found in both cell lines. Secreted activity was not detected in either cell line. In the C6 line, but not in the SK-N-SH line, we demonstrated depression of the ratio of cell surface to total cell DPP-IV activity at higher cell densities, indicating possible enzyme redistribution during cell growth in culture. Identification of DPP-IV activity is the first step in our study of the role of DPP-IV in the neural system.Key words: dipeptidyl peptidase IV, glioma, neuroblastoma.

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

Human luteal cells express dipeptidyl peptidase IV on the cell surface.

1992 ◽  
Vol 75 (5) ◽  
pp. 1352-1357
Author(s):  
H Fujiwara ◽  
M Maeda ◽  
K Imai ◽  
M Fukuoka ◽  
K Yasuda ◽  
...  
Keyword(s):  
Cell Surface ◽  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv ◽  
Luteal Cells
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