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J ten Kate

Publications and source records attributed to J ten Kate.

27 records · Page 2Linked to original sources
PubMed1989

Distribution of adenosine deaminase-complexing protein in murine tissues.

It has been suggested that mouse and rat lack adenosine deaminase-complexing protein because in these species exclusively the small molecular weight form of adenosine deaminase (ADA-S) is found. This suggestion is based on the assumption that the adenosine deaminase binding capacity is an inherent functional characteristic of adenosine deaminase-complexing protein. We report on the presence of adenosine deaminase-complexing protein immunoreactivity in mouse and rat determined with a species cross-reactive polyclonal anti-adenosine deaminase-complexing protein serum. In the mouse the tissue and subcellular distribution and the electrophoretic mobility in starch and polyacrylamide gels of the protein correspond with those of adenosine deaminase-complexing protein, but it does not bind the small molecular weight form of adenosine deaminase. Furthermore, in human, mouse, and rat kidney cortex adenosine deaminase and adenosine deaminase-complexing protein did not colocalize by immunohistochemistry. It is suggested that the function of adenosine deaminase-complexing protein is not adenosine deaminase-related.

Adenosine Deaminase↗
PubMed1989

Distribution of adenosine deaminase complexing protein (ADCP) in human tissues.

The normal distribution of adenosine deaminase complexing protein (ADCP) in the human body was investigated quantitatively by ADCP-specific radioimmunoassay (RIA) and qualitatively by immunohistochemistry. In these studies we used a specific rabbit anti-human ADCP antiserum. In all 19 investigated tissues, except erythrocytes, ADCP was found by RIA in the soluble and membrane fractions. From all tissues the membrane fractions contained more ADCP (expressed per mg protein) than the soluble fractions. High membrane ADCP concentrations were found in skin, renal cortex, gastrointestinal tract, and prostate. Immunoperoxidase staining confirmed the predominant membrane-associated localization of the protein. In serous sweat glands, convoluted tubules of renal cortex, bile canaliculi, gastrointestinal tract, lung, pancreas, prostate gland, salivary gland, gallbladder, mammary gland, and uterus, ADCP immunoreactivity was found confined to the luminal membranes of the epithelial cells. These data demonstrate that ADCP is present predominantly in exocrine glands and absorptive epithelia. The localization of ADCP at the secretory or absorptive apex of the cells suggests that the function of ADCP is related to the secretory and/or absorptive process.

Adenosine Deaminase↗
PubMed1989

Expression of c-myc proto-oncogene in normal human intestinal epithelium.

We studied the expression of the human c-myc proto-oncogene in normal human colon epithelium by both in situ hybridization and immunohistochemistry. c-myc was found to be expressed uniformly throughout the entire thickness of the colon epithelium. The present findings do not support the contention that the c-myc proto-oncogene is primarily expressed in proliferating intestinal epithelial cell compartments.

Cell Division↗
PubMed1986

Adenosine deaminase complexing protein (ADCP) immunoreactivity in colorectal adenocarcinoma.

Immunoreactive adenosine deaminase complexing protein (ADCP) was studied in 91 human colorectal adenocarcinomas. The expression of ADCP was correlated with that of secretory component (SC) and carcinoembryonic antigen (CEA), with the histological grade and the Dukes' stage of the carcinomas. The histological grade was scored semi-quantitatively according to 5 structural and 4 cytological variables. ADCP expression was observed in 3 different staining patterns, namely: (1) diffuse cytoplasmic (77% of the carcinomas); (2) granular cytoplasmic (13%); and (3) membrane-associated (66%). These patterns were observed alone or in combination. Eleven percent of the carcinomas exhibited no ADCP immunoreactivity. Linear regression analysis showed that the expression of ADCP correlates with that of SC and CEA. However, no significant correlation emerged between the histological parameters or the Dukes' stage and any of the immunohistological parameters. Comparison of the histological characteristics of carcinomas exhibiting little or no ADCP immunoreactivity with those showing extensive immunoreactivity, showed that membranous ADCP immunoreactivity occurs more frequently in well-differentiated carcinomas. Structural parameters showed a better correlation with membranous ADCP expression than the cytological variables. It is concluded that membranous expression of ADCP and CEA are indicators of a high level of differentiation as reflected primarily in the structural characteristics of the tumor.

Adenocarcinoma↗
PubMed1984

Quantitative changes in adenosine deaminase isoenzymes in human colorectal adenocarcinomas.

Several reports have suggested that a decrease or absence of adenosine deaminase complexing protein (ADCP) is consistently associated with cancer. However, in other studies, decreased as well as increased ADCP levels were found. In the present study, we investigated ADCP levels in 37 colorectal adenocarcinomas and correlated the results with clinicopathological characteristics in individual carcinomas. The levels of adenosine deaminase (EC 3.5.4.4) and soluble ADCP were determined in tissue samples by, respectively, a spectrophotometric assay and an ADCP specific radioimmunoassay. The values in the individual tumors were compared with their histological characteristics, such as degree of differentiation, nuclear grading, and the preoperative plasma carcinoembryonic antigen levels in the patients. It was found that ADCP was decreased in about a third of the tumors but unaltered or even increased in others. However, there was an overall 40% increase of the adenosine deaminase activity in the tumors compared to normal tissue. There seems to be no simple correlation between any of the clinicopathological parameters and the ADCP or adenosine deaminase levels. Methods detecting ADCP at single cell level might be helpful in exploring its potential use as a cancer-associated marker.

Adenocarcinoma↗
PubMedDate not supplied

c-Ha-ras oncogene transfection does not affect NK cell sensitivity of human colorectal carcinoma cell lines.

BACKGROUND, MATERIALS AND METHODS: To investigate whether a c-Ha-ras oncogene, pointmutated in codon 12, modulates NK sensitivity of human colorectal tumor cells, this oncogene was introduced in two colorectal carcinoma cell lines, i.e. CaCo2 and SW480. RESULTS: Although transfection with this oncogene increased the levels of c-Ha-ras mRNA (4- to 5-fold) and induced phenotypic and genotypic changes, respectively, in the CaCo2 and SW480 cell lines, the susceptibility to NK cell lysis was only marginally affected. However, CaCo2 and SW480 cell lines transfected with a plasmid containing the wild type of the c-Ha-ras gene were found to be more sensitive to NK cells. CONCLUSIONS: The present study suggests that the sensitivity of human colorectal carcinoma cells to NK cell activity in vitro depends only marginally on the expression of the c-Ha-ras oncogene.

Adenocarcinoma↗