Hostname: page-component-76fb5796d-skm99 Total loading time: 0 Render date: 2024-04-27T02:40:52.464Z Has data issue: false hasContentIssue false
  • English
  • Français

Metabolic control of insulin gene expression and biosynthesis

Published online by Cambridge University Press:  28 February 2007

Kevin Docherty ,
Andrew R. Clark ,
Valerie Scott  and
Stuart W. Knight
Kevin Docherty
Affiliation:
Department of Medicine, University of Birmingham, Queen Elizabeth Hospital, Birmingham B15 2TH
Andrew R. Clark
Affiliation:
Department of Medicine, University of Birmingham, Queen Elizabeth Hospital, Birmingham B15 2TH
Valerie Scott
Affiliation:
Department of Medicine, University of Birmingham, Queen Elizabeth Hospital, Birmingham B15 2TH
Stuart W. Knight
Affiliation:
Department of Medicine, University of Birmingham, Queen Elizabeth Hospital, Birmingham B15 2TH
Rights & Permissions [Opens in a new window]

Abstract

An abstract is not available for this content so a preview has been provided. As you have access to this content, a full PDF is available via the ‘Save PDF’ action button.
Image of the first page of this content. For PDF version, please use the ‘Save PDF’ preceeding this image.'
Type
Symposium on ‘Endocrine Pancreas and Control of Glucose Homeostasis’
Information
Proceedings of the Nutrition Society , Volume 50 , Issue 3 , December 1991 , pp. 553 - 558
Copyright
Copyright © The Nutrition Society 1991

References

Ashcroft, S. J. (1980). Glucoreceptor mechanisms and the control of insulin release and biosynthesis. Diabetologia 18, 5–15.CrossRefGoogle ScholarPubMed
Boam, D. S. W., Clark, A. R. & Docherty, K. (1990). Positive and negative regulation of the human insulin gene by multiple transacting factors. Journal of Biological Chemistry 265, 8285–8296.CrossRefGoogle Scholar
Boam, D. S. W. & Docherty, K. (1989). A tissue specific nuclear factor binds to multiple sites in the human insulin gene enhancer. Biochemical Journal 264, 233–239.CrossRefGoogle ScholarPubMed
Brundstedt, J. & Chan, S. J. (1982). Direct effect of glucose on the preproinsulin mRNA level in isolated pancreatic islets. Biochemical and Biophysical Research Communications 106, 1383–1389.CrossRefGoogle Scholar
Clark, A. R. & Docherty, K. (1992). The insulin gene. In Insulin, From Molecular Biology to Pathophysiology, pp. 37–63 [Asheroft, F. M. and Ashcroft, S. J., editors]. Oxford: Oxford University Press Ltd.CrossRefGoogle Scholar
Edlund, T., Walker, M. D., Barr, P. J. & Rutter, W. J. (1985). Cell specific expression of the rat insulin gene: evidence for the role of two distinct 5' flanking sequences. Science 230, 912–916.CrossRefGoogle Scholar
German, M. S., Moss, L. G. & Rutter, W. J. (1990). Regulation of insulin gene expression by glucose and calcium in transfected primary islet cultures. Journal of Biological Chemistry 265, 22063–22066.CrossRefGoogle ScholarPubMed
Giddings, S. J., Chirgwin, J. & Permutt, M. A. (1981). The effects of fasting and feeding on preproinsulin messenger RNA in rats. Journal of Clinical Investigation 67, 952–960.CrossRefGoogle ScholarPubMed
Gold, G., Qian, R. -L. & Grodsky, G. M. (1988). Insulin biosynthesis in HIT cells: effects of glucose, forskolin. IBMX, and dexamethasone. Diabetes 37, 160–165.CrossRefGoogle ScholarPubMed
Grimaldi, K. A., Siddle, K. & Hutton, J. C. (1987). Biosynthesis of insulin secretory granule membrane proteins: control by glucose. Biochemical Journal 245, 567–573.CrossRefGoogle ScholarPubMed
Guest, P. C., Bailyes, E. M., Rutherford, N. G. & Hutton, J. C. (1991). Insulin secretory granule biogenesis: co-ordinate regulation of the biosynthesis of the majority of constituent proteins. Biochemical Journal 274, 73–78.CrossRefGoogle ScholarPubMed
Guest, P. C., Rhodes, C. J. & Hutton, J. C. (1989). Regulation of the biosynthesis of insulin secretory granule proteins. Biochemical Journal 257, 431–437.CrossRefGoogle ScholarPubMed
Hammonds, P., Schofield, P. N. & Ashcroft, S. J. H. (1987). Glucose regulates preproinsulin messenger RNA levels in a clonal cell line of simian virus 40-transformed B cells. FEBS Letters 213, 149–154.CrossRefGoogle Scholar
Hinnesbusch, A. (1988). Mechanisms of gene regulation in the general control of amino acid biosynthesis in Saccaromyces cerevisiae. Microbiology Reviews 52, 248–273.CrossRefGoogle Scholar
Itoh, N. (1990). The translational control of proinsulin synthesis by glucose. In Molecular Biology of the Islets of Langerhans, pp. 49–65 [Okamoto, H., editor]. Cambridge: Cambridge University Press.CrossRefGoogle Scholar
Itoh, N. & Okamoto, H. (1980). Translational control of proinsulin synthesis by glucose. Nature 283, 100–102.CrossRefGoogle ScholarPubMed
Karlsson, O., Thor, S., Norberg, T., Ohlsson, H. & Edlund, T. (1990). Insulin gene enhancer binding protein Isl-1 is a member of a novel class of proteins containing both a homeo-and Cys-His domain. Nature 344, 879–882.CrossRefGoogle ScholarPubMed
Karlsson, O., Walker, M. D., Rutter, W. J. & Edlund, T. (1989). Individual protein-binding domains of the insulin gene enhancer positively activate β cell specific transcription. Molecular and Cellular Biology 9, 823–827.Google ScholarPubMed
Knight, S. W. & Docherty, K. (1991). The identification of specific protein-RNA interactions within the 5' untranslated region of human insulin mRNA. Biochemical Society Transactions 19, 120S.CrossRefGoogle Scholar
Koranyi, L. I., Bourey, R. E., Slentz, C. A., Holloszy, J. O. & Permutt, M. A. (1991). Coordinate reduction of rat pancreatic islet glucokinase and proinsulin mRNA by exercise training. Diabetes 40, 401–404.CrossRefGoogle ScholarPubMed
Murre, C., McCaw, P. S. & Baltimore, D. (1989). A new DNA binding and dimerization motif in immunoglobulin enhancer binding, daughterless, MyoD, and myc proteins. Cell 56, 777–783.CrossRefGoogle ScholarPubMed
Nelson, C., Shen, L.-P., Meister, A., Fodor, E. & Rutter, W. J. (1990). Pan: a transcriptional regulator that binds chymotrypsin, insulin, and AP-4 enhancer motifs. Genes and Development 4, 1035–1043.CrossRefGoogle Scholar
Nielsen, D. A., Welsh, M., Casadaban, M. J. & Steiner, D. F. (1985). Control of insulin gene expression in pancreatic β-cells and in insulin-producting cell line. RIN-SF cells. Journal of Biological Chemistry 260, 13585–13589.CrossRefGoogle ScholarPubMed
Permutt, M. A. & Kipnis, D. M. (1972). Insulin biosynthesis. I. On the mechanism of glucose stimulation. Journal of Biological Chemistry 247, 1194–1199.CrossRefGoogle ScholarPubMed
Philippe, J. & Missotten, M. (1990a). Functional characterisation of a CAMP-responsive element of the rat insulin I gene. Journal of Biological Chemistr 265, 1465–1469.CrossRefGoogle Scholar
Philippe, J. & Missotten, M. (1990b). Dexamethasone inhibits insulin biosynthesis by destabilising insulin messenger ribonucleic acid in hamster insulinoma cells. Endocrinolog 127, 1640–1645.CrossRefGoogle Scholar
Rouault, T. A., Tang, C. K., Kaptain, S., Burgess, W. H., Haile, D. J., Samaniego, F., McBride, O. W., Harford, J. B. & Klausner, R. D. (1990). Cloning of the cDNA encoding an RNA regulatory protein - the human iron responsive element binding protein. Proceedings of the National Academy of Sciences, USA 87, 7958–7962.CrossRefGoogle ScholarPubMed
Scott, V., Clark, A. R., Hutton, J. C. & Docherty, K. (1991). Two proteins act as the IUFI insulin gene enhancer binding factor. FEBS Letters 290, 27–30.CrossRefGoogle Scholar
Shibasaki, Y., Sakura, H., Takaku, F. & Kasuga, M. (1990). Insulin enhancer binding protein has helix-loop-helix structure. Biochemical and Biophysical Research Communications 170, 314–321.CrossRefGoogle ScholarPubMed
Soares, M. B., Schon, E., Henderson, A., Karathanasis, S. K., Cate, R., Zeitlin, S., Chirgwin, J. & Efstradiatis, A. (1985). RNA-mediated gene duplication: the rat preproinsulin I gene is a functional retroposon. Molecular and Cellular Biology 5, 2090–2103.Google ScholarPubMed
Walker, M. D., Edlund, T., Boulet, A. M. & Rutter, W. J. (1983). Cell-specific expression controlled by the 5@; flanking region of insulin and chymotrypsin genes. Nature 306, 557–561.CrossRefGoogle ScholarPubMed
Walker, M. D., Park, C. W., Rosen, A. & Aronheim, A. (1990). A cDNA from a mouse pancreatic β cell encoding a putative transcription factor of the insulin gene. Nucleic Acids Research 18, 1159–1166.CrossRefGoogle ScholarPubMed
Welsh, M., Hammer, R. E., Brinster, R. L. & Steiner, D. F. (1986a). Stimulation of growth hormone synthesis by glucose in islets of Langerhans isolated from transgenic mice. Journal of Biological Chemistr 261, 12915–12917.CrossRefGoogle Scholar
Welsh, M., Nielsen, D. A., MacKreil, A. J. & Steiner, D. F. (1985). Control of insulin gene expression in pancreatic β cells and in an insulin producing cell line. Rin-5F cell. Journal of Biological Chemistry 260, 13590–13594.CrossRefGoogle Scholar
Welsh, M., Scherberg, N., Gilmore, R. & Steiner, D. F. (1986 b). Translational control of insulin biosynthesis: evidence for regulation of elongation, initiation, and signal recognition particle-mediated translational arrest by glucose. Biochemical Journa 235, 459–467.CrossRefGoogle ScholarPubMed
Welsh, N., Welsh, M., Steiner, D. F. & Hellerstrom, C. (1987). Mechanisms of leucine- and theophylline-stimulated insulin biosynthesis in isolated rat pancreatic islets. Biochemical Journal 246, 245–248.CrossRefGoogle ScholarPubMed
Wolin, S. L. & Walter, P. (1988). Ribosome pausing and stacking during translation of a eukaryotic mRNA. EMBO Journal 7, 3559–3569.CrossRefGoogle ScholarPubMed