Abstract | BACKGROUND: METHODS: Using quantitative RT-PCR, we have determined the mRNA levels for prostasin and PN-1 in colorectal cancer tissue (n = 116), severe dysplasia (n = 13), mild/moderate dysplasia (n = 93), and in normal tissue from the same individuals. In addition, corresponding tissues were examined from healthy volunteers (n = 23). A part of the cohort was further analysed for the mRNA levels of the two variants of HAI-1, here denoted HAI-1A and HAI-1B. mRNA levels were normalised to beta-actin. Immunohistochemical analysis of prostasin and HAI-1 was performed on normal and cancer tissue. RESULTS: The mRNA level of prostasin was slightly but significantly decreased in both mild/moderate dysplasia (p < 0.001) and severe dysplasia (p < 0.01) and in carcinomas (p < 0.05) compared to normal tissue from the same individual. The mRNA level of PN-1 was more that two-fold elevated in colorectal cancer tissue as compared to healthy individuals (p < 0.001) and elevated in both mild/moderate dysplasia (p < 0.01), severe dysplasia (p < 0.05) and in colorectal cancer tissue (p < 0.001) as compared to normal tissue from the same individual. The mRNA levels of HAI-1A and HAI-1B mRNAs showed the same patterns of expression. Immunohistochemistry showed that prostasin is located mainly on the apical plasma membrane in normal colorectal tissue. A large variation was found in the degree of polarization of prostasin in colorectal cancer tissue. CONCLUSION: These results show that the mRNA level of PN-1 is significantly elevated in colorectal cancer tissue. Future studies are required to clarify whether down-regulation of prostasin activity via up regulation of PN-1 is causing the malignant progression or if it is a consequence of it.
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Authors | Joanna Selzer-Plon, Jette Bornholdt, Stine Friis, Hanne C Bisgaard, Inger Mb Lothe, Kjell M Tveit, Elin H Kure, Ulla Vogel, Lotte K Vogel |
Journal | BMC cancer
(BMC Cancer)
Vol. 9
Pg. 201
(Jun 25 2009)
ISSN: 1471-2407 [Electronic] England |
PMID | 19555470
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Chemical References |
- Amyloid beta-Protein Precursor
- Protease Nexins
- Protein Isoforms
- Proteinase Inhibitory Proteins, Secretory
- RNA, Messenger
- Receptors, Cell Surface
- SERPINE2 protein, human
- SPINT1 protein, human
- Serpin E2
- Serine Endopeptidases
- prostasin
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Topics |
- Aged
- Alternative Splicing
- Amyloid beta-Protein Precursor
(biosynthesis)
- Carcinoma
(metabolism)
- Cohort Studies
- Colorectal Neoplasms
(metabolism)
- Female
- Gene Expression Regulation, Neoplastic
- Humans
- Male
- Middle Aged
- Protease Nexins
- Protein Isoforms
- Proteinase Inhibitory Proteins, Secretory
(biosynthesis)
- RNA, Messenger
(metabolism)
- Receptors, Cell Surface
(biosynthesis)
- Serine Endopeptidases
(biosynthesis)
- Serpin E2
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