A SURVEY OF MEMBRANE PEPTIDASES IN 2 HUMAN COLONIC CELL-LINES, CACO-2 AND HT-29

被引:149
作者
HOWELL, S [1 ]
KENNY, AJ [1 ]
TURNER, AJ [1 ]
机构
[1] UNIV LEEDS,DEPT BIOCHEM & MOLEC BIOL,MEMBRANE PEPTIDASE RES GRP,LEEDS LS2 9JT,W YORKSHIRE,ENGLAND
关键词
D O I
10.1042/bj2840595
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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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页码:595 / 601
页数:7
相关论文
共 33 条
[1]   MEMBRANE PEPTIDASES IN THE PERIPHERAL NERVOUS-SYSTEM OF THE PIG - THEIR LOCALIZATION BY IMMUNOHISTOCHEMISTRY AT LIGHT AND ELECTRON-MICROSCOPIC LEVELS [J].
BARNES, K ;
BOURNE, A ;
COOK, PA ;
TURNER, AJ ;
KENNY, AJ .
NEUROSCIENCE, 1991, 44 (01) :245-261
[2]  
BESSEY OA, 1946, J BIOL CHEM, V164, P321
[3]  
Booth A G, 1974, Biochem J, V142, P575
[4]   MEMBRANE PEPTIDASES IN THE PIG CHOROID-PLEXUS AND ON OTHER CELL-SURFACES IN CONTACT WITH THE CEREBROSPINAL-FLUID [J].
BOURNE, A ;
BARNES, K ;
TAYLOR, BA ;
TURNER, AJ ;
KENNY, AJ .
BIOCHEMICAL JOURNAL, 1989, 259 (01) :69-80
[5]  
CHANTRET I, 1988, CANCER RES, V48, P1936
[6]   PROTEINS OF THE KIDNEY MICROVILLAR MEMBRANE - THE AMPHIPATHIC FORMS OF ENDOPEPTIDASE PURIFIED FROM PIG KIDNEYS [J].
FULCHER, IS ;
KENNY, AJ .
BIOCHEMICAL JOURNAL, 1983, 211 (03) :743-753
[7]   PROTEINS OF THE KIDNEY MICROVILLAR MEMBRANE - ENZYMATIC AND MOLECULAR-PROPERTIES OF AMINOPEPTIDASE-W [J].
GEE, NS ;
KENNY, AJ .
BIOCHEMICAL JOURNAL, 1987, 246 (01) :97-102
[8]   EXPRESSION AND INTRACELLULAR-TRANSPORT OF MICROVILLUS MEMBRANE HYDROLASES IN HUMAN INTESTINAL EPITHELIAL-CELLS [J].
HAURI, HP ;
STERCHI, EE ;
BIENZ, D ;
FRANSEN, JAM ;
MARXER, A .
JOURNAL OF CELL BIOLOGY, 1985, 101 (03) :838-851
[9]  
HAURI HP, 1986, MOL CELLULAR BASIS D, P421
[10]   PURIFICATION AND CHARACTERIZATION OF PIG-KIDNEY AMINOPEPTIDASE-P - A GLYCOSYL-PHOSPHATIDYLINOSITOL-ANCHORED ECTOENZYME [J].
HOOPER, NM ;
HRYSZKO, J ;
TURNER, AJ .
BIOCHEMICAL JOURNAL, 1990, 267 (02) :509-515