Immunocytochemical and biochemical detection of the urokinase-type plasminogen activator receptor (uPAR) in the rat tooth germ and in lipid rafts of PMA-stimulated dental epithelial cells

2013 ◽  
Vol 140 (6) ◽  
pp. 649-658 ◽  
Author(s):  
A. Germar ◽  
K. Barth ◽  
W. Schwab
Keyword(s):  
Epithelial Cells ◽  
Plasminogen Activator ◽  
Lipid Rafts ◽  
Tooth Germ ◽  
Type Plasminogen Activator ◽  
Urokinase Type Plasminogen Activator ◽  
Plasminogen Activator Receptor ◽  
Biochemical Detection

scholarly journals Urokinase type plasminogen activator receptor expression in colorectal neoplasms

Gut ◽  
1998 ◽  
Vol 43 (6) ◽  
pp. 798-805 ◽  
Author(s):  
S Suzuki ◽  
Y Hayashi ◽  
Y Wang ◽  
T Nakamura ◽  
Y Morita ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Plasminogen Activator ◽  
Receptor Expression ◽  
Colorectal Adenomas ◽  
Severe Dysplasia ◽  
Cellular Expression ◽  
Type Plasminogen Activator ◽  
Urokinase Type Plasminogen Activator ◽  
Plasminogen Activator Receptor ◽  
Invasive Carcinomas

Background—The urokinase type plasminogen activator receptor (uPAR) may play a critical role in cancer invasion and metastasis.Aims—To study the involvement of uPAR in colorectal carcinogenesis.Methods—The cellular expression and localisation of uPAR were investigated in colorectal adenomas and invasive carcinomas by in situ hybridisation, immunohistochemistry, and northern and western blot analyses.Results—uPAR mRNA expression was found mainly in the cytoplasm of dysplastic epithelial cells of 30% of adenomas with mild (19%), moderate (21%), and severe (47%) dysplasia, and in that of carcinomatous cells of 85% of invasive carcinomas: Dukes’ stages A (72%), B (93%), and C (91%). Some stromal cells in the adjacent neoplastic epithelium were faintly positive. Immunoreactivity for uPAR was detected in dysplastic epithelial cells of 14% of adenomas and in carcinomatous cells of 49% of invasive carcinomas. uPAR mRNA and protein concentrations were significantly higher in severe than in mild or moderate dysplasia (p<0.05); they were notably higher in Dukes’ stage A than in severe dysplasia (p<0.05), and significantly higher in Dukes’ stage B than in stage A (p<0.05), but those in stage B were not different from those in stage C or in metastatic colorectal carcinomas of the liver.Conclusions—Colorectal adenoma uPAR, expressed essentially in dysplastic epithelial cells, was upregulated with increasing severity of atypia, and increased notably during the critical transition from severe dysplasic adenoma to invasive carcinoma. These findings implicate uPAR expression in the invasive and metastatic processes of colorectal cancer.

scholarly journals Two alternatively spliced mouse urokinase receptor mRNAs with different histological localization in the gastrointestinal tract.

1991 ◽  
Vol 115 (6) ◽  
pp. 1763-1771 ◽  
Author(s):  
P Kristensen ◽  
J Eriksen ◽  
F Blasi ◽  
K Danø
Keyword(s):  
Epithelial Cells ◽  
Plasminogen Activator ◽  
Type Plasminogen Activator ◽  
Urokinase Type Plasminogen Activator ◽  
Alternatively Spliced ◽  
Plasminogen Activator Receptor ◽  
Membrane Anchoring ◽  
Luminal Epithelial Cells ◽  
Receptor Mrnas

Two mouse urokinase-type plasminogen activator receptor (muPAR) cDNAs were isolated: muPAR1 is homologous to the human urokinase-type plasminogen activator receptor while muPAR2 codes for a 199 residue protein sharing the first 133 residues with muPAR1. Mouse genomic DNA sequencing indicates that the two different mRNAs arise by alternative splicing. In situ hybridization showed differential expression of the two mRNAs in mouse gastric mucosa. muPAR1 mRNA is located in luminal epithelial cells situated close to urokinase-type plasminogen activator-producing connective tissue cells of the lamina propria, pointing to plasmin generation controlled by the cooperation of different cells that may play a role in the release of gastric epithelial cells. muPAR2 mRNA is expressed in the basal epithelial cells, and the deduced protein sequence includes the receptor ligand binding domain, but omits the region involved in glycolipid-mediated membrane anchoring, suggesting that muPAR2 may code for a secreted uPA binding protein.

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