Visualisation of transforming growth factor-β1, tissue kallikrein, and kinin and transforming growth factor-β receptors on human clear-cell renal carcinoma cells
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Rumesha Moodley
, Celia Snyman , Bharti Odhav und Kanti D. Bhoola
Abstract
Transforming growth factor-β1 (TGF-β1) has a biphasic effect on the growth of renal epithelial cells. In transformed cells, TGF-β1 appears to accelerate the proliferation of malignant cells. The diverse cellular functions of TGF-β1 are regulated by three high-affinity serine/threonine kinase receptors, namely TβRI, TβRII and TβRIII. The renal serine protease tissue kallikrein acts on its endogenous protein substrate kininogen to form kinin peptides. The cellular actions of kinins are mediated through B1 and B2 G protein-coupled rhodopsin receptors. Both kinin peptides and TGF-β1 are mitogenic, and therefore may play an important role in carcinogenesis. Experiments were designed to immunolabel tissue kallikrein, TGF-β1, TβRII, TβRIII and kinin receptors using specific antibodies on serial sections of normal kidney and clear-cell renal carcinoma (CCRC) tissue, which included both the tumour and the adjacent renal parenchyma. The essential result was the localisation of tissue kallikrein, kinin B1 and B2 receptors and TGF-β1 primarily on the cell membranes of CCRC cells. In the distal and proximal tubules of the renal parenchyma adjacent to the carcinoma (RPTAC), immunolabelling for tissue kallikrein was reduced, but the expression of kinin B1 and B2 receptors was enhanced. Immunolabelling for TβRII and TβRIII was more pronounced in the proximal tubules of the tissue adjacent to the carcinoma when compared to the normal kidney. The expression of tissue kallikrein, kinin receptors, and TβRII and TβRIII may be relevant to the parenchymal invasion and metastasis of clear-cell renal carcinoma.
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Artikel in diesem Heft
- Supplementary material to the paper “The connexin gene family in mammals”
- Nicking activity on pBR322 DNA of ribosome inactivating proteins from Phytolacca dioica L. leaves
- Identification of three novel mutations in the dihydropyrimidine dehydrogenase gene associated with altered pre-mRNA splicing or protein function
- The connexin gene family in mammals
- Hydrogen peroxide causes greater oxidation in cellular RNA than in DNA
- Homology modeling and SAR analysis of Schistosoma japonicum cathepsin D (SjCD) with statin inhibitors identify a unique active site steric barrier with potential for the design of specific inhibitors
- Interpretation of the reactivity of peroxidase compound II with phenols and anilines using the Marcus equation
- P. falciparum pro-histoaspartic protease (proHAP) protein peptides bind specifically to erythrocytes and inhibit the invasion process in vitro
- The snake venom metalloproteases berythractivase and jararhagin activate endothelial cells
- Visualisation of transforming growth factor-β1, tissue kallikrein, and kinin and transforming growth factor-β receptors on human clear-cell renal carcinoma cells
- cDNA cloning and heterologous expression of a wheat proteinase inhibitor of subtilisin and chymotrypsin (WSCI) that interferes with digestive enzymes of insect pests
- Proteolytic susceptibility of the serine protease inhibitor trappin-2 (pre-elafin): evidence for tryptase-mediated generation of elafin
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