Abstract
The ability of identical signals to interact with specific tissues in the same animal and result in the expression of different genes, is a fundamental question in cell regulation. A suitable model system for investigating the tissue specific regulation of gene expression is found in comparing the dihydrotestosteone (DHT) response in ventral prostate with the seminal vesicle. The rat ventral prostate and the seminal vesicle both contain the same genome, posses nuclear DHT receptors, and respond to DHT with the production of markedly different secretory products (figure 1). Upon DHT stimulation, the ventral prostate produces several specific secretory proteins. Similarly, the seminal vesicle produces its own unique tissue specific secretory proteins (figure 2). These tissue specific secretory proteins are all under control of the androgen receptor. Evidently there is another formes) of regulation which determines what genes are activated when the cells are stimulated with androgen. We hypothesize that this regulation is brought about by alterations in the three dimensional conformation of the genome within the nucleus. It is believed that the genomic configuration within the nucleus is determined in part by the binding of DNA loop domains to the nuclear matrix proteins. If the ventral prostate and seminal vesicle each possess unique conformations of their DNA, it is possible that the androgen receptor is able to bind and activate tissue specific transcription on different locations of the DNA depending on the tissue. Since the nuclear matrix is the organizing structure of the DNA in the nucleus, tissue specificity in three dimensional DNA organization may be caused by a unique nuclear matrix composition. We propose that the nuclear matrix is tissue specific and is involved in the regulation of gene expression.
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Alexander, R.B., Greene, G.L., and Barrack, E.R. Estrogen receptors in the nuclear matrix: direct demonstration using monoclonal antireceptor antibody. Endocrinology 120(5):1851–1857, 1987.
Allen, S.L., Berezney, R., and Coffey, D.S. Phosphorylation of nuclear matrix proteins in isolated regenerating rat liver nuclei. BBRC 75:111–116, 1977.
Barrack, E.R. and Coffey, D.S. The specific binding of estrogens and androgens to the nuclear matrix of sex hormone responsive tissues. J. Biol. Chem. 255:7265–7275, 1980.
Berezney, R. and Coffey, D.S. Identification of a nuclear protein matrix. Biochem. Biophys. Res. Comm. 60:1410–1417, 1974.
Bladon, T., Brasch, K., Brown, D.L., and Setterfield, G. Changes in structure and protein composition of bovine lymphocyte nuclear matrix during concanavalin-A-induced mitogenesis. Biochem. Cell Biol. 66:40–53, 1988.
Buttyan, R. and Olsson, C.A. Prediction of transcriptional activity based on gene association with the nuclear matrix. BBRC 138(3):1334–1340, 1986.
Carmo-Fornesca, M. Androgen-dependent nuclear proteins in rat ventral prostate are glycoproteins associated with the nuclear matrix. Cell Biology International Reports 12(8):607–620, 1988.
Chung, L. W. K, and Coffey, D.S. Biochemical characterization of prostatic nuclei: I. Androgeninduced changes in nuclear proteins. Biochimica. et. Biophysica. Acta. 247:570–583, 1971.
Ciejek, E.M., Tsai, M.J., O’Malley, B.W. Actively ttranscribed genes are associated with the 41. van Eekelen, C.A. and van Venrooij, W.J. hnRNA and its attachment to a nuclear protein Matrix. J. Cell Biol. 88:554–563, 1981. Nuclear Matrix. Nature 306:607-9, 1983.
Covey, L., Choi, Y., and Prives, C. Association of Simian virus 40 T antigen with the nuclear matrix in transformed and revertant mouse cells. Mol. Cell Biol. 4:1385–1392, 1984.
Donnelly, B.J., Lakey, W.H., and McBlain, W.H. Androgen binding sites on nuclear matrix of normal and hyperplastic human prostate. J. Urol. 131:806–811, 1984.
Eisenman, R.N., Tachibana, C.Y., Abrams, H.D., and Hann, S.R. V-myc and c-myc encoded proteins are associated with the nuclear matrix. Mol. Cell Biol. 5:114–26, 1985.
Epperly, M., Donofrio, J., Barham, S.S., and Veneziale, C.M. Nuclear protein matrix of seminal vesicle epithelium. J. Steroid Biochem. 20(3):691–697, 1984.
Fey, E.G., Ornelles, D.A., and Penman, S. Association of RNA with the cytoskeleton and the nuclear matrix. J. Cell Sci. Suppl. 5:99–119, 1986.
Fey, E. G. and Penman, S. Nuclear matrix proteins reflect cell type of origin in cultured human cells. PNAS 85:121–125, 1988.
Fey, E.G., Wan, K.M., and Penman, S. Epithelial cytoskeletal framework and nuclear matrixintermediate filament scaffold: Three-dimensional organization and protein composition. J. Cell Biol. 98:1973–1984, 1984.
Goueli, S.A. and Ahmed, K. Phosphorylation of prostatic nuclear matrix proteins is under androgenic control. Arch. Biochem. Biophys. 234(2):646–650, 1984.
Henry, S.M. and Hodge, L.D. Nuclear Matrix: A cell-cycle-dependent site of increased intranuclear protein phosphorylation. Eur. J. Biochem. 133(1):23–29, 1983.
Kandala, J.C., Kistler, W.S., and Kistler, M.K. Methylation of the rat seminal vesicle secretory protein IV gene. JBC 260(29):15959–15964, 1985.
Kishimoto, R., Gomi, T., Izaike, Y., Hagai, K., and Nakagawa, H. A novel nuclear protein in rat ventral prostate androgen-dependent and age-related change. Biochimica. et. Biophysica. Acta. 718:165–171, 1982.
Lea, O. A., Petrusz, P., and French, F.S. Prostatein: A major secretory protein of the rat ventral prostate. JBC 254(13):6196–6202, 1979.
Long, B.H. and Schrier, W.H. Isolation from friend erythroleukemia cells of an RNase-sensitive nuclear matrix fibril fraction containing hnRNA and snRNA. Biol. Cell 48:99–108, 1983.
Miller, T.E., Huang, C.Y., and Pogo, A.O. Rat liver nuclear skeleton and ribonucleoprotein complexes containing hnRNA. J. Cell Biol. 76:675–691, 1978.
Mirkovitch, J., Mirault, M-E., Laemmli, U.K Organization of the higher order chromatin loop: Specific DNA attachment sites on nuclear scaffold. Cell 39:223–232, 1984.
Mowszowicz, I., Doukani, A., and Giacomini, M. Binding of the androgen receptor to the nuclear matrix of human foreskin. J. Steroid Biochem. 29:715–719, 1988.
Moy, B.C. and Tew, K.D. Differences in the nuclear matrix phosphoproteins of a wild-type and nitrogen mustard-resistant rat breast carcinoma Cell Line. Cancer Res. 46(9):4672–4676,1986.
O’Farrell, P.H. High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem. 250:4007–4021, 1975.
Ostrowski, M.C., Kistler, M.K, and Kistler, W. S. Purification and cell-free synthesis of a major protein from rat seminal vesicle secretion. JBC 254(2):383–390, 1979.
Pardoll, D.M. Vogelstein, V., and Coffey, D.S. A fixed site of DNA replication in eukaryotic cells. Cell 19:527–36, 1980.
Peters, K.E. and Commings, D.E. Two dimensional gel electrophoresis of rat liver nuclear washes, nuclear matrix, and hnRNA proteins. J. Cell Biol. 86:135–155, 1980.
Pienta, K.J., Partin, A.W., and Coffey, D.S. Cancer as a disease of DNA organization and dynamic cell structure. Can. Res. 49:2525–2532, 1989.
Robinson S.I., Nelkin, B.D., Vogelstein, B. The ovalbumin gene is associated with the nuclear matrix of chicken oviduct cells. Cell 28:99–106, 1982.
Robinson, S.I., Small, D., Idzerda, R., McKnight, G.S., and Vogelstein, B. The association of transcriptionally active genes with the nuclear matrix of the chicken oviduct. Nucleic Acids Res. 11:5113–30, 1983.
Sarnow, P., Hearing, O., Anderson, C., Reich, N., and Levine, A.J. Identification and characterization of an immunologically conserved adenovirus early region 11,000 Mr Protein and its association with the nuclear matrix. J. Mol. Biol. 162:565–83, 1982.
Sevaljevic, L., Brajanovic, N., and Trajkovic, D. Cortisol-induced stimulation of nuclear matrix protein phosphorylation. Mol. Biol. Rep. 8(4):225–232, 1982.
Small, D., Nelkin, B., and Vogelstein, B. Nucleic Acids Res. 13:2413, 1985.
Small, D. and Vogelstein, B. The anatomy of supercoiled loops in the drosophila 7F locus. Nucleic Acids Res. 21:7703–7713, 1985.
Staufenbiel, M. and Deppert, W. Different structural systems of the nucleus are targets for SV40 large T antigen. Cell 33:173–181, 1983.
Stuurman, N., Van Driel, R., De Jong, L., Meijne, A.M.L., and Van Renswoude, J. The protein composition of the nuclear matrix of Murine P19 embryonal carcinoma cells is differentiationstage dependent. Exp. Cell Res. 180:46–466, 1989.
Teraoka, H., Ohmura, Y., and Tsukada, K. The nuclear matrix from rat liver is capable of phosphorylating exogenous tyrosine-containing substrates. Biochem.Int. 18(6):1203–1210, 1989.
van Eekelen, C.A. and van Venrooij, W.J. hnRNA and its attachment to a nuclear protein matrix. J. Cell Biol. 88:554–563, 1981.
Venkatraman, J.Y., Howell, G.M., and Lefebvre, Y.A. Androgen-dependent peptides of the rat ventral prostate nuclear envelope. BBRC 125(2):469–474, 1984.
Viskochil, D.H., Perry, S.T., Lea, O.A., Stafford, D.W., Wilson, E.M., and French, F.S. Isolation of two genomic sequences encoding the Mr=14,000 subunit of rat prostatein. JBC 258(14):8861–8866, 1983.
Vogelstein, B., Pardoll, D.M., and Coffey, D.S. Supercoiled loops and eukaryotic DNA replication. Cell 22:79–85, 1980.
Wagner, C.L. and Kistler W.S. Analysis of the major large polypeptides of rat seminal vesicle secretion: SVS I,II, and III. Biol. Reprod. 36:501–510,1987.
White, R. & Parker, M. Developmental changes in DNA methylation around prostatic steroidbinding protein genes. JBC 258(14):8943–8, 1983.
Zehnbauer, B.A. and Vogelstein, B. BioEssays 2:52–54,1985.
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Getzenberg, R.H., Coffey, D.S. (1991). Tissue Specificity and Cell Death are Associated with Specific Alterations in Nuclear Matrix Proteins. In: Karr, J.P., Coffey, D.S., Smith, R.G., Tindall, D.J. (eds) Molecular and Cellular Biology of Prostate Cancer. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-3704-5_1
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DOI: https://doi.org/10.1007/978-1-4615-3704-5_1
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