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. 1985 Jan;5(1):253–258. doi: 10.1128/mcb.5.1.253

Blockage of tropoelastin secretion by monensin represses tropoelastin synthesis at a pretranslational level in rat smooth muscle cells.

S M Frisch, J M Davidson, Z Werb
PMCID: PMC366701  PMID: 3982417

Abstract

The blockage of protein secretion in the R22 cultured rat aortic smooth muscle cell strain with monensin repressed tropoelastin gene expression at the mRNA level by ca. 50-fold as measured by biosynthetic pulse-labeling, in vitro translation, and hybridization with a tropoelastin genomic DNA probe. These results suggest that tropoelastin gene expression is autoregulated, and they represent the first reported effect of monensin on gene expression.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Burnett W., Eichner R., Rosenbloom J. Correlation of functional elastin messenger ribonucleic acid levels and rate of elastin synthesis in the developing chick aorta. Biochemistry. 1980 Mar 18;19(6):1106–1111. doi: 10.1021/bi00547a010. [DOI] [PubMed] [Google Scholar]
  2. Cleveland D. W., Lopata M. A., MacDonald R. J., Cowan N. J., Rutter W. J., Kirschner M. W. Number and evolutionary conservation of alpha- and beta-tubulin and cytoplasmic beta- and gamma-actin genes using specific cloned cDNA probes. Cell. 1980 May;20(1):95–105. doi: 10.1016/0092-8674(80)90238-x. [DOI] [PubMed] [Google Scholar]
  3. Cleveland D. W., Pittenger M. F., Feramisco J. R. Elevation of tubulin levels by microinjection suppresses new tubulin synthesis. Nature. 1983 Oct 20;305(5936):738–740. doi: 10.1038/305738a0. [DOI] [PubMed] [Google Scholar]
  4. Cleveland D., Kirschner M. Autoregulatory control of the expression of alpha- and beta-tubulins: implications for microtubule assembly. Cold Spring Harb Symp Quant Biol. 1982;46(Pt 1):171–183. doi: 10.1101/sqb.1982.046.01.020. [DOI] [PubMed] [Google Scholar]
  5. Davidson J. M., Shibahara S., Schafer M. P., Harrison M., Leach C., Tolstoshev P., Crystal R. G. Sheep elastin genes. Isolation and preliminary characterization of a 9.9-kilobase genomic clone. Biochem J. 1984 Jun 15;220(3):643–652. doi: 10.1042/bj2200643. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Davidson J. M., Smith K., Shibahara S., Tolstoshev P., Crystal R. G. Regulation of elastin synthesis in developing sheep nuchal ligament by elastin mRNA levels. J Biol Chem. 1982 Jan 25;257(2):747–754. [PubMed] [Google Scholar]
  7. Hörlein D., McPherson J., Goh S. H., Bornstein P. Regulation of protein synthesis: translational control by procollagen-derived fragments. Proc Natl Acad Sci U S A. 1981 Oct;78(10):6163–6167. doi: 10.1073/pnas.78.10.6163. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Jones P. A., Scott-Burden T., Gevers W. Glycoprotein, elastin, and collagen secretion by rat smooth muscle cells. Proc Natl Acad Sci U S A. 1979 Jan;76(1):353–357. doi: 10.1073/pnas.76.1.353. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Kumamoto C. A., Oliver D. B., Beckwith J. Signal sequence mutations disrupt feedback between secretion of an exported protein and its synthesis in E. coli. 1984 Apr 26-May 2Nature. 308(5962):863–864. doi: 10.1038/308863a0. [DOI] [PubMed] [Google Scholar]
  10. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  11. Lehrach H., Diamond D., Wozney J. M., Boedtker H. RNA molecular weight determinations by gel electrophoresis under denaturing conditions, a critical reexamination. Biochemistry. 1977 Oct 18;16(21):4743–4751. doi: 10.1021/bi00640a033. [DOI] [PubMed] [Google Scholar]
  12. Lodish H. F., Kong N., Snider M., Strous G. J. Hepatoma secretory proteins migrate from rough endoplasmic reticulum to Golgi at characteristic rates. Nature. 1983 Jul 7;304(5921):80–83. doi: 10.1038/304080a0. [DOI] [PubMed] [Google Scholar]
  13. Mecham R. P., Griffin G. L., Madaras J. G., Senior R. M. Appearance of chemotactic responsiveness to elastin peptides by developing fetal bovine ligament fibroblasts parallels the onset of elastin production. J Cell Biol. 1984 May;98(5):1813–1816. doi: 10.1083/jcb.98.5.1813. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Miller J. S., Paterson B. M., Ricciardi R. P., Cohen L., Roberts B. E. Methods utilizing cell-free protein-synthesizing systems for the identification of recombinant DNA molecules. Methods Enzymol. 1983;101:650–674. doi: 10.1016/0076-6879(83)01046-0. [DOI] [PubMed] [Google Scholar]
  15. Moolenaar W. H., Tsien R. Y., van der Saag P. T., de Laat S. W. Na+/H+ exchange and cytoplasmic pH in the action of growth factors in human fibroblasts. Nature. 1983 Aug 18;304(5927):645–648. doi: 10.1038/304645a0. [DOI] [PubMed] [Google Scholar]
  16. Mrsny R. J., Meizel S. Potassium ion influx and Na+,K+-ATPase activity are required for the hamster sperm acrosome reaction. J Cell Biol. 1981 Oct;91(1):77–82. [PMC free article] [PubMed] [Google Scholar]
  17. Neblock D. S., Berg R. A. Lysosomotropic agents ammonium chloride and chloroquine inhibit both the synthesis and secretion of procollagen by freshly isolated embryonic chick tendon cells. Biochem Biophys Res Commun. 1982 Apr 14;105(3):902–908. doi: 10.1016/0006-291x(82)91055-5. [DOI] [PubMed] [Google Scholar]
  18. Pelham H. R., Jackson R. J. An efficient mRNA-dependent translation system from reticulocyte lysates. Eur J Biochem. 1976 Aug 1;67(1):247–256. doi: 10.1111/j.1432-1033.1976.tb10656.x. [DOI] [PubMed] [Google Scholar]
  19. Rigby P. W., Dieckmann M., Rhodes C., Berg P. Labeling deoxyribonucleic acid to high specific activity in vitro by nick translation with DNA polymerase I. J Mol Biol. 1977 Jun 15;113(1):237–251. doi: 10.1016/0022-2836(77)90052-3. [DOI] [PubMed] [Google Scholar]
  20. Rio D., Robbins A., Myers R., Tjian R. Regulation of simian virus 40 early transcription in vitro by a purified tumor antigen. Proc Natl Acad Sci U S A. 1980 Oct;77(10):5706–5710. doi: 10.1073/pnas.77.10.5706. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Rucker R. B., Tinker D. Structure and metabolism of arterial elastin. Int Rev Exp Pathol. 1977;17:1–47. [PubMed] [Google Scholar]
  22. Shibahara S. U., Davidson J. M., Smith K., Crystal R. G. Modulation of tropoelastin production and elastin messenger ribonucleic acid activity in developing sheep lung. Biochemistry. 1981 Nov 10;20(23):6577–6584. doi: 10.1021/bi00526a009. [DOI] [PubMed] [Google Scholar]
  23. Tartakoff A. M. Perturbation of vesicular traffic with the carboxylic ionophore monensin. Cell. 1983 Apr;32(4):1026–1028. doi: 10.1016/0092-8674(83)90286-6. [DOI] [PubMed] [Google Scholar]
  24. Thomas P. S. Hybridization of denatured RNA and small DNA fragments transferred to nitrocellulose. Proc Natl Acad Sci U S A. 1980 Sep;77(9):5201–5205. doi: 10.1073/pnas.77.9.5201. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Tolan D. R., Amsden A. B., Putney S. D., Urdea M. S., Penhoet E. E. The complete nucleotide sequence for rabbit muscle aldolase A messenger RNA. J Biol Chem. 1984 Jan 25;259(2):1127–1131. [PubMed] [Google Scholar]
  26. Tolstoshev P., Berg R. A., Rennard S. I., Bradley K. H., Trapnell B. C., Crystal R. G. Procollagen production and procollagen messenger RNA levels and activity in human lung fibroblasts during periods of rapid and stationary growth. J Biol Chem. 1981 Mar 25;256(6):3135–3140. [PubMed] [Google Scholar]
  27. Werb Z., Bainton D. F., Jones P. A. Degradation of connective tissue matrices by macrophages. III. Morphological and biochemical studies on extracellular, pericellular, and intracellular events in matrix proteolysis by macrophages in culture. J Exp Med. 1980 Dec 1;152(6):1537–1553. doi: 10.1084/jem.152.6.1537. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Werb Z., Banda M. J., Jones P. A. Degradation of connective tissue matrices by macrophages. I. Proteolysis of elastin, glycoproteins, and collagen by proteinases isolated from macrophages. J Exp Med. 1980 Nov 1;152(5):1340–1357. doi: 10.1084/jem.152.5.1340. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. de Clerck Y. A., Jones P. A. The effect of ascorbic acid on the nature and production of collagen and elastin by rat smooth-muscle cells. Biochem J. 1980 Jan 15;186(1):217–225. doi: 10.1042/bj1860217. [DOI] [PMC free article] [PubMed] [Google Scholar]

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