Skip to main content
SpringerLink
Log in

Intracellular Pathways; Exocytic and Endocytic Routes Relying upon Selective Vesicular Transport

  • Chapter
Pharmaceutical Applications of Cell and Tissue Culture to Drug Transport

Part of the book series: NATO ASI Series ((NSSA,volume 218))

  • 245 Accesses

Abstract

For hydrophilic macromolecules to be transported into cells and across tissue barriers the major permeability barriers are the lipid bilayers of the continuous membrane boundaries which surround and compartmentalise all eukaryotic cells. Specialised mechanisms within these boundaries can translocate relatively large molecular species such as polypeptides across the hydrophobic internum of the bilayer but these mechanisms provide major routes of access only into biosynthetic compartments such as the rough endoplasmic reticulum (RER).

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Log in via an institution
Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 84.99
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 109.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  • Breitfeld, P.P., J.M. Harris, and K.E. Mostov. (1989). Postendocytotic sorting of the ligand for the polymeric immunoglobulin receptor in Madin-Darby Canine Kidney cells. J. Cell Biol. 109: 475–486.

    Article  PubMed  CAS  Google Scholar 

  • Caplan, M.J., H.C. Anderson, G.E. Palade, and J.D. Jamieson. (1986). Intracellular sorting and polarized cell surface delivery of (Na+-K+) — ATPase, an endogenous component of MDCK cell basolateral plasma membranes. Cell. 24: 24–32.

    Google Scholar 

  • Carpenter, G. (1987). Receptors for epidermal growth factor and other polypeptide mitogens. Ann. Rev. Biochem. 56: 881–914.

    Article  PubMed  CAS  Google Scholar 

  • Cereijido, M., E.S. Robbins, W.J. Dolan, C.A. Rotuno, and D.D. Sabatini. (1978). Polarized monolayers formed by epithelial cells on a permeable and translucent support. J. Cell Biol. 77: 853–880.

    Article  PubMed  CAS  Google Scholar 

  • Ciechanover, A., A.L. Schwartz, and H.F. Lodish. (1983). The asialoglycoprotein receptor internalizes and recycles independently of the transferrin and insulin receptors. Cell. 32: 267–275.

    Article  PubMed  CAS  Google Scholar 

  • Cutler, D.F. (1988). The role of transport signals and retention signals in constitutive export from animal cells. J. Cell Science. 91: 1–4.

    PubMed  Google Scholar 

  • Davis, C.G., I.R. van Driel, D.W. Russell, M.S. Brown and J.L. Goldstein. (1987). The low density lipoprotein receptor. Identification of amino acids in cytoplasmic domain required for rapid endocytosis. J. Biol. Chem. 262: 4075–4082.

    PubMed  CAS  Google Scholar 

  • Diamond, J.M. (1977). The epithelial junction: bridge, gate, and fence. Physiologist. 20: 10–18.

    PubMed  CAS  Google Scholar 

  • De Brabander, M., R. Nuydens, H. Geerts, and C.R. Hopkins. (1988). Dynamic behaviour of the transferrin receptor followed in living epidermoid carcinoma (A431) cells with nanovid microscopy. Cell Motil. Cytoskeleton. 9: 30–47.

    Article  PubMed  Google Scholar 

  • Dudouet, B., S. Robine, C. Huet, C. Sahuquillo-Merino, L. Blair, E. Coudrier, and D. Louvard. (1987). Changes in villin synthesis and subcellular distribution during intestinal differentiation of HT29-18 clones. J. Cell Biol. 105: 359–370.

    Article  PubMed  CAS  Google Scholar 

  • Dunn, W.A., A.L. Hubbard, and N.V. Aronson. (1980). Low temperature selectively inhibits fusion between pinocytic vesicles and lysosomes during heterophagy of 125 asialofetuin by the perfused rat liver. J. Biol. Chem. 255: 5971–5978.

    PubMed  CAS  Google Scholar 

  • Eilers, U., J. Klumperman, and H.-P. Hauri. (1989). Nocodazole, a microtubule-active drug, interferes with apical protein delivery in cultured intestinal epithelial cells (Caco-2). J. Cell Biol. 108: 13–22.

    Article  PubMed  CAS  Google Scholar 

  • Escobedo, J.A., and L.T. Williams. (1988). A PDGF receptor domain essential for mitogenesis but not for many other responses to PDGF. Nature. 335: 85–87.

    Article  PubMed  CAS  Google Scholar 

  • Farquhar, M.G. (1978). Recovery of surface membrane in anterior pituitary cell. Variations in traffic detected with anionic and cationic ferritin. J. Cell Biol. 77: R35–R42.

    Article  PubMed  CAS  Google Scholar 

  • von Figura, K., and A. Hasilik. (1986). Lysosomal enzymes and their receptors. Annu. Rev. Biochem. 55: 167–193.

    Article  Google Scholar 

  • Fujiki, Y., A.L. Hubbard, S. Fowler, and P.B. Lazarow. (1982). Isolation of intracellular membranes by means of sodium carbonate treatment: application to endoplasmic reticulum. J. Cell Biol. 93: 97–102.

    Article  PubMed  CAS  Google Scholar 

  • Fujita, M., F. Reinhart, and M. Neutra. (1988). Convergence of apical and basolateral endocytic pathways at the late endosome; double tracer studies in ileal absorptive cells of suckling rats. J. Cell Biol. 107: Abtr. 616.

    Google Scholar 

  • Glenney, J.R. Jr., W.S. Chen, C.S. Lazar, G.M. Walton, L.M. Zokas, M.G. Rosenfield, and G.N. Gill. (1988). Ligand induced endocytosis of the EGF receptor is blocked by mutational inactivation and by microinjection of anti-phosphoprotein antibodies. Cell. 52: 675–684.

    Article  PubMed  CAS  Google Scholar 

  • Gould, S.J., G.-A. Keller, N. Hosken, J. Wilkinson, and S. Subramani. (1989). A conserved tripeptide sorts proteins to peroxisomes. J. Cell Biol. 108: 1657–1664.

    Article  PubMed  CAS  Google Scholar 

  • Griffiths, G., and K. Simons. (1986). The trans Golgi network: sorting at the exit site of the Golgi complex. Science. 234: 438–443.

    Article  PubMed  CAS  Google Scholar 

  • Griffiths, G., B. Hoflack, K. Simons, and S. Kornfeld. (1988). The mannose 6-phosphate receptor and the biogenesis of lysosomes. Cell. 52: 329–341.

    Article  PubMed  CAS  Google Scholar 

  • Heuser, J. (1989). Changes in lysosome shape and distribution correlated with changes in cytoplasmic pH. J. Cell Biol. 108: 855–864.

    Article  PubMed  CAS  Google Scholar 

  • Honeggar, A., M. Dull, T.J. Felder, S. Van Obberghen, E. Bellot, F. Szapary, D. Schmidt, A. Ulrich, and J. Schlessinger. (1987). Point mutation at the ATP binding site of EGF receptor abolishes protein-tyrosine kinase activity and alters cellular routing. Cell. 51: 199–209.

    Article  Google Scholar 

  • Hopkins, C.R. and I.S. Trowbridge. (1983). Internalization and processing of transferrin and the transferrin receptor in human carcinoma A431 cells. J. Cell Biol. 97: 508–521.

    Article  PubMed  CAS  Google Scholar 

  • Hopkins, C.R. (1986). Membrane boundaries involved in the uptake and intracellular processing of cell surface receptors. TIBS. 11: 473–477.

    CAS  Google Scholar 

  • Huet, C., C. Sahuquillo-Merino, E. Coudrier, and D. Louvard. (1987). Absorptive and mucus-secreting subclones isolated from a multipotent intestinal cell line (HT-29) provide new models for cell polarity and terminal differentiation. J. Cell Biol. 105: 345–358.

    Article  PubMed  CAS  Google Scholar 

  • Kelly, R.B. (1985). Pathways of protein secretion in eukaryotes. Science. 230: 25–32.

    Article  PubMed  CAS  Google Scholar 

  • Kirchausen, T., K.L. Nathanson, W. Matsui, A. Vaisberg, E.P. Chow, C. Burne, J. Keen, J. Hand, and A.E. Davis. (1989). Structural and functional division into two domains of the large (100-to 115-kDa)) chains of the clathrin-associated protein complex AP-2. Proc. Natl. Acad. Sci. USA. 86: 2612–2616.

    Article  Google Scholar 

  • Koval, M., and R.E. Pagano. (1989). Lipid recycling between the plasma membrane and intracellular compartments: Transport and metabolism of fluorescent sphingomyelin analogues in cultured fibroblasts. J. Cell Biol. 108: 2169–2181.

    Article  PubMed  CAS  Google Scholar 

  • Lazarovits, J., and M. Roth. (1988). A single amino acid change in the cytoplasmic domain allows the influenza haemagglutinin to be endocytosed through coated pits. Cell 53: 743–752.

    Article  PubMed  CAS  Google Scholar 

  • Lobel, P., K. Fujimoto, R. Ye, G. Griffiths, and S. Kornfeld. (1989). Mutations in the cytoplasmic domain of the 275kd mannose-6-phosphate receptor differentially alter lysosomal enzyme sorting and endocytosis. Cell. 57: 787–796.

    Article  PubMed  CAS  Google Scholar 

  • Matteoni, R., and T.E. Kreis. (1988). Translocation and clustering of endosomes and lysosomes depends on microtubules. J. Cell Biol. 105: 1253–1265.

    Article  Google Scholar 

  • Miettinen, H.M., J.K. Rose, and I. Mellman. (1989). Fc receptor isoforms exhibit distinct abilities for coated pit localization as a result of cytoplasmic domain hetereogeneity. Cell. 58: 3017–3027.

    Article  Google Scholar 

  • Orci, L., M. Ravazzola, M. Amherdt, D. Brown, and A. Perrelet. (1986). Transport of horseradish peroxidase from the cell surface to the Golgi in insulin-secreting cells: preferential labeling of cisternae located in an intermediate position in the stack. EMBO J. 5: 2097–2101.

    PubMed  CAS  Google Scholar 

  • Nilsson, T., M. Jackson, and P.A. Peterson. (1989). Short cytoplasmic sequences serve as retention signals for transmembrane proteins in the endoplasmic reticulum. Cell. 58: 707–718.

    Article  PubMed  CAS  Google Scholar 

  • Pearse, B.M.F. (1975). Coated vesicles from pig brain: purification and biochemical characterization. J. Mol. Biol. 97: 93–98.

    Article  PubMed  CAS  Google Scholar 

  • Pearse, B.M.F. (1988). Receptors compete for adaptors in plasma membrane coated pits. EMBO J. 7: 3331–3336.

    PubMed  CAS  Google Scholar 

  • Pearse, B.M.F., and R.A. Crowther. (1987). Structure and assembly of coated vesicles. Ann. Rev. Biophys. Chem. 16: 49–68.

    Article  CAS  Google Scholar 

  • Rivas, R., J. Hsiao-Ping, and H. Moore. (1989). Spatial segregation of the regulated and constitutive secretory pathways. J Cell Biol. 109: 9521–9525.

    Article  Google Scholar 

  • Robinson, M.S. (1989). Cloning of cDNAs of two related 100kD coated vesicle proteins (alpha adaptins). J. Cell Biol. 108: 833–842.

    Article  PubMed  CAS  Google Scholar 

  • Schmid, S.L., R. Fuchs, P. Male, and I. Mellman. (1988). Two distinct subpopulations of endosomes involved in membrane recycling and transport to the lysosomes. Cell. 52: 73–83.

    Article  PubMed  CAS  Google Scholar 

  • Simons K., and S.D. Fuller. (1985). Surface polarity in epithelia. Ann. Rev. Cell Biol. 1: 243–288.

    Article  PubMed  CAS  Google Scholar 

  • Snider, M., and O.C. Rogers. (1986). Membrane traffic in animal cells: cellular glycoproteins return to the site of Golgi mannosidase 1. J. Cell. Physiol. 115: 199–207.

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Department of Biochemistry, Imperial College, South Kensington, London, SW7, 2AZ, UK

    Colin R. Hopkins

Authors
  1. Colin R. Hopkins
    View author publications

    You can also search for this author in PubMed Google Scholar

Editor information

Editors and Affiliations

  1. SmithKline Beecham Pharmaceuticals, King of Prussia, Pennsylvania, USA

    Glynn Wilson

  2. University of Nottingham, Nottingham, UK

    S. S. Davis  & L. Illum  & 

  3. INSERM, Paris, France

    Alain Zweibaum

Rights and permissions

Reprints and permissions

Copyright information

© 1991 Plenum Press, New York

About this chapter

Cite this chapter

Hopkins, C.R. (1991). Intracellular Pathways; Exocytic and Endocytic Routes Relying upon Selective Vesicular Transport. In: Wilson, G., Davis, S.S., Illum, L., Zweibaum, A. (eds) Pharmaceutical Applications of Cell and Tissue Culture to Drug Transport. NATO ASI Series, vol 218. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-0286-6_6

Download citation

  • DOI: https://doi.org/10.1007/978-1-4757-0286-6_6

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4757-0288-0

  • Online ISBN: 978-1-4757-0286-6

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics

Search

Navigation