Abstract
Human endopeptidase 24.11 (EP) occurs in greatest abundance on terminally differentiated prostate cells; thus, loss of EP could mark dedifferentiation of prostate epithelium. To identify laboratory models that would permit continuous work on the biochemistry and hormonal regulation of EP, we examined the well-differentiated LNCaP and poorly differentiated PPC-1 human prostate cancer cell lines. Ultrastructural analysis revealed that LNCaP secretes electron-dense material that resembles the particulate matter of seminal plasma, which is associated with endopeptidase activity. LNCaP medium contained EP activity while PPC-1 medium did not. Whether the apparent deletion of EP from the PPC-1 cell line is characteristic of poorly differentiated prostate adenocarcinoma is not yet clear. However, it may be relevant to the carcinogenic process that EP can limit growth of lung small carcinomas by inactivating cell growth-promoting bombesin-like peptides. Because bombesin has been identified in aggressive human prostate cancers, loss of EP in PPC-1 could represent a necessary step in transformation to aggressive phenotype. The combination of LNCaP and PPC-1, which offers well-differentiated and poorly differentiated cancer phenotypes, appears well suited to studying the relevance of EP in prostate cancer biology.
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References
Aguayo SM, Schuyler WE, Murtagh JJJ, Roman J (1994) Regulation of lung branching morphogenesis by bombesin-like peptides and neutral endopeptidase. Am J Resp Cell Mol Biol 10:635
Brody L, Ronquist G, Gottfries A, Stegmayr B (1981) Ultrastructural localization of the prostasome: an organelle in human seminal plasma. Ups J Med Sci 88:63
Davis BK (1973) Occurrence of vesicles in rat seminal plasma. Experimentia 29:1484
Duggan KA, Jones DM, Ye VZC. Davis RE, MacDonald GJ (1995) Effects of endopeptidase 24.11 inhibition on plasma and tissue concentrations of vasoactive intestinal peptide. Clin Sci 89:267
Gnessi L, Ulisse S, Fabbri A, Jannini EA, Bonifacio V, Moretti C, Spera G, Isidori A (1989) Isolation of a human seminal plasma peptide with bombesin-like activity. Fertil Steril 51:1034
Hoosein NM, Logothetis CJ, Chung LWK (1993) Differential effects of peptide hormones bombesin, vasoactive intestinal polypeptide and somatostatin analog RC-160 on the invasive capacity of human prostatic carcinoma cells. J Urol 149:1209
Krongrad A, Bai G (1994) c-fos promoter insensitivity of phorbol ester and possible role of protein kinase C in androgenindependent cancer cells. Cancer Res 54:6073
Logothetis C, Hoosein N (1992) The inhibition of the paracrine progression of prostate cancer as an approach to early therapy of prostatic carcinoma. J Cell Biochem 16:128
Ronquist G, Brody I (1985) The prostasome: its secretion and function in man. Biochem Biophys Acta 822:203
Ronquist G, Fritz GG, Jansson A (1988) Prostasome membrane associated enzyme activities and semen parameters in men attending an infertility clinic. Urol Int 43:133
Ryan JW, Chung AY, Nearing JA, Valido FA, Shun-Cun C, Berryer P (1993) A radiochemical assay for aminopeptidase N. Anal Biochem 210:27
Ryan JW, Chung AYK, Berryer P (1996) A radioassay for endopeptidase 24.11. FASEB J 10:A670
Ryan US, Hart MA (1986) Electron microscopy of endothelial cells in culture. J Tissue Cult Meth 10:31
Shipp MA, Tarr GE, Chen CY, Switzer SN, Hersh LB, Stein H, Sunday ME, Reinherz EL (1991) CD/neutral endopeptidase 24.11 hydrolyses bombesin-like peptides and regulates the growth of small cell carcinomas of the lung. Proc Natl Acad Sci USA 88:10662
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Krongrad, A., Atochina, E., Ryan, J.W. et al. Endopeptidase 24.11 activity in the human prostate cancer cell lines LNCaP and PPC-1. Urol. Res. 25, 113–116 (1997). https://doi.org/10.1007/BF01037925
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DOI: https://doi.org/10.1007/BF01037925