Advertisement

Endocrine Pituitary Cell Cultures: Cellular Morphology, Protein Secretion, and Susceptibility to Weak Bases and Ionophores

  • Athanassios Sambanis
Conference paper
Part of the NATO ASI Series book series (volume 64)

Abstract

Animal cells are of significant use in bioprocessing technology, tissue engineering, and gene therapy applications. In bioprocess technology, cells cultured in bioreactors produce specific recombinant or, occasionally, endogenous proteins. Compared to bacteria and yeast, animal cells have the disadvantages of slow growth to relatively low densities, and of complex and expensive culture media requirements. On the other hand, they offer the distinct advantage of possessing the enzymatic machinery necessary for performing post-translational modifications on recombinant proteins. Such modifications are essential for biological activity of a protein product and may not be feasible in yeast or, even more so, in bacteria. Animal cells are thus indispensable for production of pharmaceuticals such as tissue plasminogen activator (tPA), factor VIII, or other complex proteins.

Keywords

Secretory Granule Endocrine Cell Secretory Vesicle Signal Recognition Particle Complete Growth Medium 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Basu SK, Goldstein JL, Anderson RGW, Brow MS (1981) Monensin interrupts the recycling of low density lipoprotein receptors in human fibroblasts. Cell 24:493–502PubMedCrossRefGoogle Scholar
  2. Bell E, Ehrlich H, Buttle D, Nakatsuji T (1981) Living tissue formed in vitro and accepted as skin-equivalent tissue of full thickness. Science 211:1052–1054PubMedCrossRefGoogle Scholar
  3. Berg T, Blomhoff R, Naess L, Tolleshaug H, Drevon CA (1983) Monensin inhibits receptor-mediated endocytosis in rat hepatocytes. Exp Cell Res 148:319–330PubMedCrossRefGoogle Scholar
  4. Burgess TL, Craik CS, Kelly RB (1985) The exocrine protein trypsinogen is targeted into the secretory granules of an endocrine cell line: studies by gene transfer. J Cell Biol 101:639–645PubMedCrossRefGoogle Scholar
  5. Burgess TL, Kelly RB (1987) Constitutive and regulated secretion of proteins. Ann Rev Cell Biol 3:243–293PubMedCrossRefGoogle Scholar
  6. Chung K-N, Walter P, Aponte GW, Moore H-PH (1989) Molecular sorting in the secretory pathway. Science 243:192–197PubMedCrossRefGoogle Scholar
  7. Colton CK, Dionne KE, Yarmush ML (1988) Oxygen effects on pancreatic islet insulin secretion in hybrid artificial pancreas. In: Skalak R, Fox CF (eds) Tissue Engineering, Alan R. Liss, New York, p 217Google Scholar
  8. Docherty K, Carroll RJ, Steiner DF (1982) Conversion of proinsulin to insulin: involvement of a 31,500 molecular weight thiol-protease. Proc Natl Acad Sci USA 79:4613–4617PubMedCrossRefGoogle Scholar
  9. Darnell J, Lodish H, Baltimore D (1990) Molecular Cell Biology, 2nd edn. American Scientific Books, WH Freeman and Company, New YorkGoogle Scholar
  10. Dyken JJ, Sambanis A (1991a) Protein secretion from endocrine animal cells: effects of chemical and physical stresses. In: Proceedings of 1991 Graduate Student Symposium, Georgia Institute of Technology, Atlanta, p 41Google Scholar
  11. Dyken JJ, Vachtsevanos J, Sambanis A (1991b) Protein secretion from endocrine animal cells: effects of chemical and physical stresses. Presented at ACS National Meeting, Atlanta, Georgia, April 1991Google Scholar
  12. Galletti PM, Aebischer P (1988) Bioartificial organs. In: Skalak R, Fox CF (eds) Tissue Engineering, Alan R. Liss, New York, p 211Google Scholar
  13. Grampp GE, Stephanopoulos G (1991) Controlled protein secretion in a pancreatic islet-derived cell line. Presented at ACS National Meeting, Atlanta, Georgia, USA, April 1991Google Scholar
  14. Gumbiner B, Kelly RB (1982) Two distinct intracellular pathways transport secretory and membrane glycoproteins to the surface of pituitary tumor cells. Cell 28:51–59PubMedCrossRefGoogle Scholar
  15. Helenius A, Kartenbeck J, Simons K, Fries E (1980) On the entry of Semliki Forest virus into BHK-21 cells. J Cell Biol 84:404–420PubMedCrossRefGoogle Scholar
  16. Huttner WB, Gerdes H-H, Rosa P, Tooze SA (1990) Biogenesis of secretory granules in vivo and in vitro. J Cell Biol Suppl 14C:9Google Scholar
  17. Kelly RB (1985) Pathways of protein secretion in eucaryotes. Science 230:25–32PubMedCrossRefGoogle Scholar
  18. Mains RE, Cullen EI, May V, Eipper BA (1987) The role of secretory granules in peptide biosynthesis. Ann NY Acad Sci 493:278–291PubMedCrossRefGoogle Scholar
  19. Marsh M, Wellstead J, Kern H, Harms E, Helenius A (1982) Monensin inhibits Semliki Forest virus penetration into culture cells. Proc Natl Acad Sci USA 79:5297–5301PubMedCrossRefGoogle Scholar
  20. Maxfield FR (1982) Weak bases and ionophores rapidly and reversibly raise the pH of endocytic vesicles in cultured mouse fibroblasts. J Cell Biol 95:676–681PubMedCrossRefGoogle Scholar
  21. Mellman I, Fuchs R, Helenius A (1986) Acidification of the endocytic and exocytic pathways. Annu Rev Biochem 55:663–700PubMedCrossRefGoogle Scholar
  22. Merion MW, Sly S (1983) The role of intermediate vesicles in the adsorptive endocytosis and transport of ligand to lysosomes by human fibroblasts. J Cell Biol 96:644–650PubMedCrossRefGoogle Scholar
  23. Moore HP (1986) Factors controlling packaging of peptide hormones into secretory granules. Ann NY Acad Sci 493:50–61CrossRefGoogle Scholar
  24. Moore HP, Gumbiner B, Kelly RB (1983) Chloroquine diverts ACTH from a regulated to a constitutive secretory pathway in AtT-20 cells. Nature 302:434–436PubMedCrossRefGoogle Scholar
  25. Moore HP, Kelly RB (1985) Secretory protein targeting in a pituitary cell line: differential transport of foreign secretory proteins to distinct secretory pathways. J Cell Biol 101:1773–1781PubMedCrossRefGoogle Scholar
  26. Moore HP, Walker MD, Lee F, Kelly RB (1983) Expressing a human proinsulin cDNA in a mouse ACIH-secreting cell. Intracellular storage, proteolytic processing, and secretion on stimulation. Cell 35:531–538PubMedCrossRefGoogle Scholar
  27. Nerem RM (1991) Cellular Engineering. Ann Biomed Engng, in pressGoogle Scholar
  28. Ohkuma S, Poole B (1981) Cytoplasmic vacuolation of mouse peritoneal macrophages and the uptake into lysosomes of weakly basic substances. J Cell Biol 90:656–664Google Scholar
  29. Orci L, Halban P, Amherdt M, Ravazzola M, Vassalli J-D, Perrelet A (1984) A clathrin- coated, Golgi-related compartment of the insulin secreting cell accumulates proinsulin in the presence of monensin. Cell 39:39–47PubMedCrossRefGoogle Scholar
  30. Orci L, Ravazzola M, Amherdt M, Madsen O, Vassalli J-D, Perrelet A (1985) Direct identification of prohormone conversion site in insulin-secreting cells. Cell 42:671–681PubMedCrossRefGoogle Scholar
  31. Orci L, Ravazzola M, Storch M-J, Anderson RGW, Vassalli J-D, Perrelet A (1987) Proteolytic maturation of insulin is a post-Golgi event which occurs in acidifying clathrin- coated secretory vesicles. Cell 49:865–868PubMedCrossRefGoogle Scholar
  32. Sambanis A, Lodish HF, Stephanopoulos G (1991) A model of secretory protein trafficking in recombinant AtT-20 cells. Biotechnol Bioeng 38:280–295PubMedCrossRefGoogle Scholar
  33. Sambanis A, Stephanopoulos G, Lodish HF (1990) Multiple episodes of induced secretion of human growth hormone from recombinant AtT-20 cells. Cytotechnology 4:111–119PubMedCrossRefGoogle Scholar
  34. Sambanis A, Stephanopoulos G, Sinskey AJ, Lodish HF (1990) Use of regulated secretion in protein production from animal cells: an evaluation with the AtT-20 model cell line. Biotechnol Bioeng 35:771–780PubMedCrossRefGoogle Scholar
  35. Stenseth K, Thyberg J (1989) Monensin and chloroquine inhibit transfer to lysosomes of endocytosed macromolecules in cultured mouse peritoneal macrophages. Eur J Cell Biol 49:326–333PubMedGoogle Scholar
  36. Stoscheck CM, Carpenter G (1984) Down regulation of epidermal growth factor receptors: direct demonstration of receptor degradation in human fibroblasts. J Cell Biol 98:1048–1053PubMedCrossRefGoogle Scholar
  37. Tietze C, Schlesinger P, Stahl P (1980) Chloroquine and ammonium ion inhibit receptor- mediated endocytosis of mannose-glycoconjugates by macrophages: apparent inhibition of receptor recycling. Biochem Biophys Res Comm 93:1–8PubMedCrossRefGoogle Scholar
  38. Tolleshaug H, Berg T (1979) Chloroquine reduces the number of asialoglycoprotein receptors in the hepatocyte plasma membrane. Biochem Pharmacol 28:2919–2922PubMedCrossRefGoogle Scholar
  39. Tooze J, Tooze SA (1986) Clathrin-coated vesicular transport of secretory proteins during the formation of ACTH-containing secretory granules in AtT-20 cells. J Cell Biol 103:839–850PubMedCrossRefGoogle Scholar
  40. Weinberg CB, Bell E (1986) A blood vessel model constructed from collagen and cultured vascular cells. Science 231:397–399PubMedCrossRefGoogle Scholar
  41. Wibo M, Poole B (1974) Protein degradation in cultured cells. II. The uptake of chloroquine by rat fibroblasts and the inhibition of cellular protein degradation and cathepsin B1 J Cell Biol 63:430–440PubMedCrossRefGoogle Scholar
  42. Wickner WT, Lodish HF (1985) Multiple mechanisms of protein insertion into and across membranes. Science 230: 400–407.PubMedCrossRefGoogle Scholar
  43. Wileman T, Boshans RL, Schlesinger P, Stahl P (1984) Monensin inhibits recycling of macrophage mannose-glycoprotein receptors and ligand delivery to lysosomes. Biochem J 220:665–67PubMedGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 1992

Authors and Affiliations

  • Athanassios Sambanis
    • 1
  1. 1.School of Chemical EngineeringGeorgia Institute of TechnologyAtlantaUSA

Personalised recommendations