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Open AccessJournal Article

Establishment and characterization of a human prostatic carcinoma cell line (PC-3).

M E Kaighn, +4 more
- 01 Jul 1979 - 
- Vol. 17, Iss: 1, pp 16-23
TLDR
The establishment, characterization, and tumorigenicity of a new epithelial cell line (PC-3) from a human prostatic adenocarcinoma metastatic to bone is reported, which should be useful in investigating the biochemical changes in advanced prostatic cancer cells and in assessing their response to chemotherapeutic agents.
Abstract
The establishment, characterization, and tumorigenicity of a new epithelial cell line (PC-3) from a human prostatic adenocarcinoma metastatic to bone is reported The cultured cells show anchorage-independent growth in both monolayers and in soft agar suspension and produce subcutaneous tumors in nude mice Culture of the transplanted tumor yielded a human cell line with characteristics identical to those used initially to produce the tumor PC-3 has a greatly reduced dependence upon serum for growth when compared to normal prostatic epithelial cells and does not respond to androgens, glucocorticoids, or epidermal or fibroblast gowth factors Karyotypic analysis by quinacrine banding revealed the cells to be completely aneuploid with a modal chromosome number in the hypotriploid range At least 10 distinctive marker chromosomes were identified The overall karyotype as well as the marker chromosomes are distinct from those of the HeLa cell Electron microscopic studies revealed many features common to neoplastic cells of epithelial origin including numerous microvilli, junctional complexes, abnormal nuclei and nucleoli, abnormal mitochondria, annulate lamellae, and lipoidal bodies Overall, the functional and morphologic characteristics of PC-3 are those of a poorly-differentiated adenocarcinoma These cells should be useful in investigating the biochemical changes in advanced prostatic cancer cells and in assessing their response to chemotherapeutic agents

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Measles Virus Infects both Polarized Epithelial and Immune Cells by Using Distinctive Receptor-Binding Sites on Its Hemagglutinin

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