Abstract |
We have previously shown that C-CAM1 cell adhesion molecule can suppress the growth of prostate cancer cells in vivo. In this study, we determined the minimal domain of C-CAM1 that is required for its tumor-suppressive activity. DU145 prostate cancer cells were infected with recombinant adenoviruses containing various C-CAM1 mutant genes, and the effects of the mutant C-CAM1 proteins on the growth of DU145 cells were assessed in a nude-mice xenograft model. Deletion of C-CAM1's cytoplasmic domain, which is not required for its adhesion activity, abolished the growth-suppressive activity, whereas deletion of the adhesion domain did not. This observation suggests that C-CAM1's extracellular domain may be not essential for its tumor suppressive activity. Indeed, we found that expression of the C-CAM1 cytoplasmic domain alone led to growth suppression of DU145 cells. These results suggest that the cytoplasmic domain of C-CAM1 is necessary and sufficient for its growth-suppressive function.
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Authors | V T Estrera, W Luo, D Phan, K Earley, D C Hixson, S H Lin |
Journal | Biochemical and biophysical research communications
(Biochem Biophys Res Commun)
Vol. 263
Issue 3
Pg. 797-803
(Oct 05 1999)
ISSN: 0006-291X [Print] United States |
PMID | 10512760
(Publication Type: Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, U.S. Gov't, P.H.S.)
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Copyright | Copyright 1999 Academic Press. |
Chemical References |
- Antigens, CD
- CD66 antigens
- Carcinoembryonic Antigen
- Ceacam1 protein, mouse
- Ceacam2 protein, mouse
- Cell Adhesion Molecules
- Glycoproteins
- Recombinant Proteins
- Adenosine Triphosphatases
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Topics |
- Adenosine Triphosphatases
(chemistry, genetics, physiology)
- Adenoviridae
- Animals
- Antigens, CD
- Carcinoembryonic Antigen
- Cell Adhesion
- Cell Adhesion Molecules
(chemistry, genetics, physiology)
- Cell Aggregation
- Cell Division
- Cloning, Molecular
- Cytoplasm
(metabolism)
- Genetic Vectors
- Glycoproteins
- Humans
- Male
- Mice
- Mice, Nude
- Mutagenesis, Site-Directed
- Prostatic Neoplasms
(pathology, physiopathology)
- Recombinant Proteins
(chemistry, metabolism)
- Transfection
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