Differential SP220K expression in renal carcinoma and oncocytoma cells.

Abstract

SP220K is a newly described serine proteinase which displays guanidinobenzoatase activity in its inactive form and gelatinolytic activity in its active form. SP220K expression was studied in 20 renal clear-cell carcinomas and in a series of renal oncocytomas, a rare benign tumor derived from the kidney tubule epithelium. We provide evidence that SP220K expression, as assessed by guanidinobenzoatase activity, gelatin zymography and Western blot immunodetection, was increased markedly in cancer basolateral membranes compared to kidney cortex controls, whereas no signal was detectable in basolateral membranes from the 5 renal oncocytomas studied. Cytoplasms of carcinoma cells were immunodetected consistently, whereas no expression was seen in oncocytic cells from any of the oncocytomas studied (12/12). Endothelial cells were immunodetected in all 3 tissue types. Our data favor a potential mechanistic relationship between expression of the matrix proteinase SP220K and invasive phenotype in kidney epithelium proliferative processes.

• Authors: S Thaon, C Ferrero, P Auberger, J F Michiels, D Droz, J Amiel, B Rossi, C Poustis-Delpont
• Journal: International journal of cancer (Int J Cancer) Vol. 72 Issue 5 Pg. 752-7 (Sep 04 1997) ISSN: 0020-7136 [Print] United States
• PMID: 9311589 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Carboxylic Ester Hydrolases
• guanidinobenzoate esterase
• Endopeptidases
• SP220K cell surface matrix proteinase
• Serine Endopeptidases
• Gelatinases

Topics

• Adenoma, Oxyphilic (enzymology, metabolism)
• Blotting, Western
• Carboxylic Ester Hydrolases (metabolism)
• Carcinoma, Renal Cell (enzymology, metabolism)
• Cell Membrane (enzymology)
• Cytoplasm (enzymology)
• Endopeptidases (metabolism)
• Gelatinases (metabolism)
• Humans
• Immunohistochemistry
• Kidney Cortex (enzymology)
• Kidney Neoplasms (enzymology, metabolism)
• Serine Endopeptidases (metabolism)