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Transport and Processing of Lysosomal Enzymes

  • Kurt von Figura
  • Andrej Hasilik
  • Peter Lemansky
  • Thomas Braulke
Part of the NATO ASI Series book series (NSSA, volume 116)

Abstract

At present more than 50 different lysosomal enzymes are known. They have in common their location in lysosomes and their function to degrade endogenous and exogenous macromolecules mostly by hydrolytic cleavage. With a few exceptions lysosomal enzymes fall into the class of low abundant proteins with a frequency ranging from 0.05 to 0.005% of total protein. Their low frequency severely impairs studies on the in-vitro synthesis of lysosomal enzymes. The best characterized example for in-vitro synthesis of lysosomal enzymes is that of cathepsin D programmed by porcine spleen mRNA (1–3). Cathepsin D is synthesized with an aminoterminal extension of 20 amino acid. This aminoterminal “signal sequence” directs translocation of the nascent cathepsin D precursors across the membrane of the rough endoplasmic reticulum. Translocation involves recognition of the signal sequence when protruding from the ribosomes by a cytosolic ribonucleotide particle (SRP) and transfer of this complex to a receptor protein (SRP-receptor or docking protein) at the cytosolic face of the rough endoplasmic reticulum. After crossing the membrane the signal sequence is cleaved by a proteinase at the luminal side of the rough endoplasmic reticulum. It is therefore not found on cathepsin D, isolated from translation system supplemented with dog pancreas microsomal vesicles. The existence of a similar transient aminoterminal presequence has been postulated for ß-glucuronidase and cathepsin D in rat hepatocytes and the α- and ß-chain of ß-hexosaminidase in human fibroblasts by comparison of the size of the in-vitro synthesized products with that of tunicamycin treated cells (4,5).

Keywords

Lysosomal Enzyme Rough Endoplasmic Reticulum Golgi Complex Coated Vesicle Mannose Residue 
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.

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References

  1. 1.
    Erickson, A. H., Blobel, G., 1979, J. Biol. Chem, 254: 11771–74.PubMedGoogle Scholar
  2. 2.
    Erickson, A. H., V. Conner, G. E., Blobel, G., 1981, J. Biol. Chem, 256: 11224–31.PubMedGoogle Scholar
  3. 3.
    Erickson, A. H., Walter, P., Blobel, G., 1983, Biochem. Biophys. Res. Commun, 115: 275–80.PubMedCrossRefGoogle Scholar
  4. 4.
    Rosenfeld, M. G., Kreibich, D., Popov, D., Kato, K., Sabatini, D. D., 1982, J. Cell Biol, 93: 135–43PubMedCrossRefGoogle Scholar
  5. 5.
    Proia, R., Neufeld, E. F., 1982, Proc. Natl. Acad. Sci. USA, 79: 6360–64.PubMedCrossRefGoogle Scholar
  6. 6.
    Kornfeld, R., Kornfeld, S., 1985, Ann. Rev. Biochem, 54: 631–64PubMedCrossRefGoogle Scholar
  7. 7.
    Lemansky, P., Gieselmann, V., Hasilik, A., von Figura, K., 1984, J. Biol. Chem, 259: 10129–35.PubMedGoogle Scholar
  8. 8.
    Creek, K. E., Sly, W. S., 1984, in: Lysosomes in Biology and Pathology, ed. J. T. Dingle, R. T. Dean, W. Sly, pp. 63–82, Amsterdam: Elsevier.Google Scholar
  9. 9.
    von Figura, K., Hasilik, A., Ann. Rev. Biochem., 1986, in press.Google Scholar
  10. 10.
    Hasilik, A., Waheed, A., von Figura, K., 1981, Biochem. Biophys. Res. Commun, 98: 761–67.PubMedCrossRefGoogle Scholar
  11. 11.
    Reitman, M. L., Kornfeld, S., 1981, J. Biol. Chem, 256: 4275–81.PubMedGoogle Scholar
  12. 12.
    Reitman, M. L., Kornfeld, S., 1981, J. Biol. Chem, 256: 11977–80.PubMedGoogle Scholar
  13. 13.
    Waheed, A., Hasilik, A., von Figura, K., 1982, J. Biol. Chem.,257:12322–31.PubMedGoogle Scholar
  14. 14.
    Varki, A., Kornfeld, S., 1980, J. Biol. Chem, 255: 10847–58.PubMedGoogle Scholar
  15. 15.
    Goldberg, D. E., Kornfeld, S., 1981, J. Biol. Chem, 256: 13060–67PubMedGoogle Scholar
  16. 16.
    Hasilik, A., von Figura, K., 1981, Eur. J. Biochem, 121: 125–29.PubMedCrossRefGoogle Scholar
  17. 17.
    Lang, L., Reitman, M., Tang, J., Roberts, R. M., Kornfeld, S., 1984, J. Biol. Chem, 259: 14663–71.PubMedGoogle Scholar
  18. 18.
    Pohlmann, R., Waheed, A., Hasilik, A., von Figura, K., 1982, J. Biol. Chem, 257: 5723–25.Google Scholar
  19. 19.
    Goldberg, D., Kornfeld, S., 1983, J. Biol. Chem, 258: 3159–65.PubMedGoogle Scholar
  20. 20.
    Deutscher, S. L., Creek, K. E., Merion, M., Hirschberg, C. B., 1983, Proc. Natl. Acad. Sci. USA, 80: 3938–42.PubMedCrossRefGoogle Scholar
  21. 21.
    Morré, D. J., Minnifield, N., Creek, K. E., Navas, P., 1985, Special FEBS Meeting, p. 144 (abstract), Algarve, Portugal, printed in Dept. Zool. Univ. of Coimbra.Google Scholar
  22. 22.
    Varki, A., Kornfeld, S., 1980, J. Biol. Chem, 255: 8398–401.PubMedGoogle Scholar
  23. 23.
    Varki, A., Kornfeld, S., 1981, J. Biol. Chem, 256: 9937–43.PubMedGoogle Scholar
  24. 24.
    Waheed, A., Hasilik, A., von Figura, K., 1981, J. Biol. Chem.,256:5717–21.PubMedGoogle Scholar
  25. 25.
    Varki, A., Kornfeld, S., 1983, J. Biol. Chem, 258: 2808–18.PubMedGoogle Scholar
  26. 26.
    Yamamoto, K., Tsuji, T., Tarutani, O., Osawa, T., 1985, Biochim. Biophys. Acta, 838: 84–91.PubMedCrossRefGoogle Scholar
  27. 27.
    Kress, B., Freeze, H., Herd, K. J., Alhadeff, J. A., Miller, A., 1980, J. Biol. Chem, 255: 955–61.PubMedGoogle Scholar
  28. 28.
    Miller, A. L., Kress, B. C., Stein, R., Kinnon, C., Kern, H., Schneider, J. A., Harms, E., 1981, J. Biol. Chem, 256: 9352–62.PubMedGoogle Scholar
  29. 29.
    Kress, B. C., Hirani, S., Freeze, H., Little, L. and Miller, A. L., 1982, Biochem. J, 207: 421–428.PubMedGoogle Scholar
  30. 30.
    Hasilik, A., Klein, U., Waheed, A., Strecker, G., von Figura, K., 1980, Proc. Natl. Acad. Sci. USA, 77: 7074–78.PubMedCrossRefGoogle Scholar
  31. 31.
    Gieselmann, V., Pohlmann, R., Hasilik, A., von Figura, K., 1983, J. Cell Biol, 97: 1–5.PubMedCrossRefGoogle Scholar
  32. 32.
    Hickman, S., Neufeld, E. F., 1972, Biochem. Biophys. Res. Commun, 49: 992–99.PubMedCrossRefGoogle Scholar
  33. 33.
    Waheed, A., Pohlmann, R., Hasilik, A., von Figura, K., van Elsen, A., Leroy, J. G., 1982, Biochem. Biophys. Res. Commun, 105: 1052–58.PubMedCrossRefGoogle Scholar
  34. 34.
    Owada, M., Neufeld, E. F., 1982, Biochem. Biophys. Res. Commun, 105: 814–20.PubMedCrossRefGoogle Scholar
  35. 35.
    Sahagian, G. G., 1985, in: Recent Research on Vertebrate Lectins, ed. J. T. Dingle, R. T. Dean, W. Sly, pp. 63–82, Amsterdam: Elsevier.Google Scholar
  36. 36.
    Hoflack, B., Kornfeld, S., 1985, Proc. Natl. Acad. Sci. USA,82:4428–32.PubMedCrossRefGoogle Scholar
  37. 37.
    Hoflack, B., Kornfeld, S., 1985, in: Glycoconjugates, Proceedings of the Vllith International Symposium, vol. 1, pp. 144–145, Praeger, New York.Google Scholar
  38. 38.
    Brown, W. J., Farquhar, M. G., 1984, Cell, 36: 295–307.PubMedCrossRefGoogle Scholar
  39. 39.
    Geuze, H. J., Slot, J. W., Strous, G. J. A. M., Hasilik, A., von Figura, K., 1984, J. Cell Biol, 98: 2047–54.PubMedCrossRefGoogle Scholar
  40. 40.
    Geuze, H. J., Slot, J. W., Strous, G. J. A. M., Hasilik, A., von Figura, K., 1985, J. Cell Biol., in the press.Google Scholar
  41. 41.
    Vladutiu, G. D., 1983, Biochim. Biophys. Acta, 760: 363–70.PubMedCrossRefGoogle Scholar
  42. 42.
    Gabel, C. A., Goldberg, D. E., Kornfeld, S., 1982, J. Cell Biol., 95: 536–42.PubMedCrossRefGoogle Scholar
  43. 43.
    Roth, J., Berger, E., 1982, J. Cell Biol., 92: 223–29.CrossRefGoogle Scholar
  44. 44.
    Berger, E., Hesford, F. J., 1985, Proc. Natl. Acad. Sci. USA, 82: 4736–4739.PubMedCrossRefGoogle Scholar
  45. 45.
    Willingham, M. C., Pastan, I. H., Sahagian, G. G., Jourdian, G. W., Neufeld, E. F., 1981, Proc. Natl. Acad. Sci. USA, 78: 6967–71.PubMedCrossRefGoogle Scholar
  46. 46.
    Campbell, C. H., Rome, L. H., 1983, J. Biol. Chem, 258: 13347–52.PubMedGoogle Scholar
  47. 47.
    Willingham, M. C., Pastan, I. H., Sahagian, G. G., 1983, J. Histochem. Cytochem, 31: 1–11.PubMedCrossRefGoogle Scholar
  48. 48.
    Schulze-Lohoff, E., Hasilik, A., von Figura, K., 1985, J. Cell Biol., in the press.Google Scholar
  49. 49.
    Rome, L. H., Weissmann, B., Neufeld, E. F., 1979, Proc. Natl. Acad. Sci. USA, 76: 2331–34.PubMedCrossRefGoogle Scholar
  50. 50.
    Gonzalez-Noriega, A., Grubb, J. H., Talked, V., Sly, W. S., 1980, J. Cell Biol, 85: 839–52.PubMedCrossRefGoogle Scholar
  51. 51.
    Geuze, H. J., Slot, J. W., Strous, G. J. A. M., Peppard, J., von Figura, K., Hasilik, A., Schwartz, A. L., 1984, Cell, 37: 195–204.PubMedCrossRefGoogle Scholar
  52. 52.
    Dude Elferink, R. P. J., Doorn-van Wakeren, J., Strijland, A., Reuser, A. J. J., Tager, J. M., 1985, Eur. J. Biochem in the press.Google Scholar
  53. 53.
    Hasilik, A., von Figura, K., 1984, in: Lysosomes in Biology and Pathology, ed. J. T. Dingle, R. T. Dean, W. Sly, pp. 3–16, Amsterdam: Elsevier.Google Scholar
  54. 54.
    Skudlarek, M. D., Novak, E., Swank, R. T., 1984, in: Lysosomes in Biology and Pathology, ed. J. T. Dingle, R. T. Dean, W. Sly, pp. 17–34, Amsterdam: Elsevier.Google Scholar
  55. 55.
    D’Azzo, A., Hoogeveen, A., Reuser, A. J. J., Robinson, D., Galjaard, A., 1982, Proc. Natl. Acad. Sci. USA, 79: 4535–39.PubMedCrossRefGoogle Scholar
  56. 56.
    von Figura, K., Steckel, F., Hasilik, A., 1983, Proc. Natl. Acad. Sci. USA, 80: 6066–70.CrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1986

Authors and Affiliations

  • Kurt von Figura
    • 1
  • Andrej Hasilik
    • 1
  • Peter Lemansky
    • 1
  • Thomas Braulke
    • 1
  1. 1.Physiologisch-Chemisches InstitutUniversität MünsterMünsterGermany

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