Skip to main content
SpringerLink
Log in

Recent studies on the maturation of lysosomal enzymes

  • Chapter
Book cover Inborn Errors of Metabolism in Humans

  • 80 Accesses

Abstract

The class of enzymes called ‘lysosomal’ refers in general to hydrolases with an acid pH optimum, which reside in lysosomes but which may also be found in body fluids and sometimes in microsomes. Recent work has shown that the fine structure of these hydrolases determines their location, and conversely, that the location and history of the hydrolases affects their structure. Because acid hydrolases are glycoproteins, the structural variations may be in the polypeptide or the carbohydrate portions of the molecule.

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 39.99
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 54.99
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

  1. Hasilik, A. and Neufeld, E. F. (1980). Biosynthesis of lysosomal enzymes in fibroblasts; synthesis as precursors of higher molecular weight. J. Biol. Chem., 255, 4937

    PubMed  CAS  Google Scholar 

  2. Puchalski, C. and Neufeld, E. F. (1981). Polypeptides of processed β-hexosaminidase remain associated under non-reducing conditions. Fed. Proc., 40, 1551

    Google Scholar 

  3. Robbins, A. R. and Myerowitz, R. (1981). The mannose 6-phosphate receptor of Chinese hamster ovary cells. J. Biol. Chem., 256, 10623

    PubMed  CAS  Google Scholar 

  4. Myerowitz. R and Neufeld, E. F. (1981). Maturation of a-L-iduronidase in cultured human fibroblasts. J. Biol. Chem., 256, 3044

    PubMed  CAS  Google Scholar 

  5. Erickson, A. H and Blobel, G. (1979). Early events in the biosynthesis of the lysosomal enzyme cathepsin D. J. Biol. Chem., 254, 11771

    PubMed  CAS  Google Scholar 

  6. Skudlarek, M D. and Swank, B. T. (1979). Biosynthesis of two lysosomal enzymes in macrophages. J. Biol. Chem., 254, 9939

    PubMed  CAS  Google Scholar 

  7. Frisch, A and Neufeld, E. F. (1980). Limited proleolysis of β-hexosaminidase in a cell-free system. Fed. Proc., 39, 1866

    Google Scholar 

  8. Frisch, A and Neufeld, E. F. (1981). Limited proteolysis of the β-hexosamimdase precursor in a cell-free system. J. Biol. Chem., 256, 8242

    PubMed  CAS  Google Scholar 

  9. Hickman. S., Shapiro, L. J. and Neufeld, E. F. (1974). A recognition marker required for uptake of a lysosomal enzyme by cultured fibroblasts. Biochem. Biophys. Res. Commun., 57, 55

    Article  PubMed  CAS  Google Scholar 

  10. Neufeld, E. F., Sando, G. N., Garvin, A. J. and Rome, L. H. (1977). The transport of lysosomal enzymes. J. Supramol. Struct., 6, 95

    Article  PubMed  CAS  Google Scholar 

  11. Kaplan, A., Achord, D. T. and Sly, W. S. (1977). Phosphohexosyl components of a lysosomal enzyme are recognized by pinocytosis receptors on human fibroblasts Proc. Natl. Acad. Sci. USA, 74, 2026

    Article  PubMed  CAS  Google Scholar 

  12. Sando, G N, and Neufeld, E. F. (1977). Recognition and receptor-mediated uptake of a lysosomal enzyme, a-L-iduronidase, by cultured human fibroblasts. Cell 12, 619

    Article  PubMed  CAS  Google Scholar 

  13. Kaplan, A., Fischer, D., Achord, D. and Sly, W. (1977). Phosphohexosyl recognition is a general characteristic of pinocytosis of lysosomal glycosidases by human fibroblasts. J. Clin. Invest., 60, 1088.

    Article  PubMed  CAS  Google Scholar 

  14. Ullrich, K., Mersmann, G., Weber, E. and von Figura, K. (1978). Evidence for lysosomal enzyme recognition by human fibroblasts via a phosphorylated carbohydrate moiety. Biochem. J., 170, 643

    PubMed  CAS  Google Scholar 

  15. Natowicz, M. R., Chi, M. M-Y., Lowry, O. H. and Sly, W. S. (1979). Enzymatic identification of mannose 6-phosphate on the recognition marker for receptor-mediated pinocytosis of β-glucuronidase by human fibroblasts. Proc. Natl. Acad. Sci. USA, 76, 4322

    Article  PubMed  CAS  Google Scholar 

  16. Distier, J., Hieber, V., Sahagian, G., Schmickel, R. and Jourdian, G. W. (1979). Identification of mannose 6-phosphate in glycoproteins that inhibit the assimilation of β-galactosidase by fibroblasts. Proc. Natl. Acad. Sci. USA, 76, 4235

    Article  Google Scholar 

  17. von Figura, K. and Klein, U. (1979). Isolation and characterization of phosphorylated oligosaccharides from a-N-acetyl-glucosaminidase that are recognized by cell surface receptors. Eur. J. Biochem., 94, 347

    Article  Google Scholar 

  18. Sahagian, G., Distier, J., Hieber, V., Schmickel, R., and Jourdian, G. W. (1979). Role of mannose-6-phosphate in β-galactosidase assimilation. Fed. Proc., 38, 467

    Google Scholar 

  19. Hasilik, A. and Neufeld, E. F. (1980). Biosynthesis of lysosomal enzymes in fibroblasts; phosphorylation of mannose residues. J. Biol. Chem., 255, 4946

    PubMed  CAS  Google Scholar 

  20. Tabas, I. and Kornfeld, S. (1980). Biosynthetic intermediates of β-glucuronidase contain high mannose oligosaccharides with blocked phosphate residues. J. Biol. Chem., 255, 6633

    PubMed  CAS  Google Scholar 

  21. Hasilik, A., Klein, U., Waheed, A., Strecker, G. and von Figura, K. (1980). Phosphorylated oligosaccharides in lysosomal enzymes: identification of a-N-acetylglucosamine(1)phospho(6)mannose diester groups. Proc. Natl. Acad. Sci. USA, 77, 7074

    Article  PubMed  CAS  Google Scholar 

  22. McKusick, V. A., Neufeld, E. F. and Kelly, T. E. (1978). The mucopolysaccharide storage diseases. In Stanbury, J. B., Wyngaarden, J. B. and Fredrickson, D. S. (eds.) The Metabolic Basis of Inherited Disease, pp. 1282-1307. (New York: McGraw-Hill).

    Google Scholar 

  23. Hickman, S. and Neufeld, E. F. (1972). A hypothesis for I-Cell disease: defective hydrolases that do not enter lysosomes. Biochem. Biophys. Res. Commun., 49, 992

    Article  PubMed  CAS  Google Scholar 

  24. Bach, G., Bargal, R. and Cantz, M. (1979). I-Cell disease: deficiency of extracellular hydrolase phosphorylation. Biochem. Biophys. Res. Commun., 91, 976

    Article  PubMed  CAS  Google Scholar 

  25. Vladutiu, G. D. and Rattazzi, M. C. (1975). Abnormal lysosomal hydrolases excreted by cultured fibroblasts in I-Cell disease (mucolipidosis II). Biochem. Biophys. Res. Commun., 67, 956

    Article  PubMed  CAS  Google Scholar 

  26. Miller, A. L., Freeze, H. S. and Kress, B. C. (1981). I-Cell disease. In Callahan, J. W. and Lowden, J. A. (eds.) Lysosomes and Lysosomal Storage Diseases, p. 271. (New York: Raven Press)

    Google Scholar 

  27. Struck, D. K. and Lennarz, W. J. (1980). The functions of saccharide lipids in synthesis of glycoproteins. In Lennarz, W. J. (ed.) The Biochemistry of Glycoproteins and Proteoglycans, pp. 35-83 (New York: Plenum Press)

    Google Scholar 

  28. Schachter, H. and Roseman, S. (1980). Mammalian glycosyltransferases: their role in the synthesis and function of complex carbohydrates and glycolipids. In Lennarz, W. J. (ed.) The Biochemistry of Glycoproteins and Proteoglycans, pp. 85-160 (New York: Plenum Press)

    Google Scholar 

  29. Robey, P. G. and Neufeld, E. F. (1982). Defective phosphorylation and processing of β-hexosaminidase by intact cultured fibroblasts from patients with mucolipidosis III. Arch. Biochem. Biophys., 213, 251

    Article  PubMed  CAS  Google Scholar 

  30. Neufeld, E. F. (1981). Recognition and processing of lysosomal enzymes in cultured fibroblasts. In Callahan, J. W. and Lowden, J. A. (eds.) Lysosomes and Lysosomal Storage Diseases, p. 115 (New York: Raven Press)

    Google Scholar 

  31. Karson, E. M., Neufeld, E. F. and Sando, G. N. (1980). p-Isothiocyanatophenyl 6-phospho-α-D-mannopyranoside coupled to albumin. A model compound recognized by the fibroblast lysosomal enzyme uptake system. Biochemistry, 19, 3856.

    Article  PubMed  CAS  Google Scholar 

  32. Rome, L. H. and Miller, J. (1980). Butanedione treatment reduces receptor binding of a lysosomal enzyme to cells and membranes. Biochem. Biophys. Res. Commun., 92, 986

    Article  PubMed  CAS  Google Scholar 

  33. Davis, B. D. and Tai, P. C. (1980). The mechanism of protein secretion across membranes. Nature (London), 283, 433

    Article  PubMed  CAS  Google Scholar 

  34. Hasilik, A., Waheed, A. and von Figura, K. (1981). Enzymatic phosphorylation of lysosomal enzymes in the presence of UDP-N-acetylglucosamine. Absence of the activity in I-cell fibroblasts. Biochem. Biophys. Res. Commun., 98, 761

    Article  PubMed  CAS  Google Scholar 

  35. Reitman, M. L. and Kornfeld, S. (1981). UDP-N-acetylglucosamine: glycoprotein N-acetylglucosamine-l-transferase. Proposed enzyme for the phosphorylation of the high mannose oligosaccharide units of lysosomal enzymes. J. Biol. Chem., 256, 4275

    PubMed  CAS  Google Scholar 

  36. Varki, A. and Kornfeld, S. (1980). Identification of a rat liver α-N-acetylglucosaminyl phosphodiesterase capable of removing “blocking” α-N-acetylglucosamine residues from phosphorylated high mannose oligosaccharides of lysosomal enzymes. J. Biol. Chem., 255, 8398

    PubMed  CAS  Google Scholar 

  37. Waheed, A., Hasilik, A. and von Figura, K. (1981). Processing of the phosphorylated recognition markers in lysosomal enzymes. Characterization and partial purification of a microsomal α-N-acetylglucosaminyl phosphodiesterase. J. Biol. Chem., 256, 5717

    PubMed  CAS  Google Scholar 

  38. Varki, A. and Kornfeld, S. (1980). Structural studies of phosphorylated high mannose-type oligosaccharides. J. Biol. Chem., 255, 10847

    PubMed  CAS  Google Scholar 

  39. Reitman, M. L., Varki, A. and Kornfeld, S. (1981). Fibroblasts from patients with I-cell disease and pseudo-Hurler polydystrophy are deficient in uridine 5’-diphosphate-N-acetylglucosamine: glycoprotein-N-acetylglucosaminyl phosphotransferase activity. J. Clin. Invest., 67, 1574

    Article  PubMed  CAS  Google Scholar 

Download references

Authors
  1. E. F. Neufeld
    View author publications

    You can also search for this author in PubMed Google Scholar

Editor information

Editors and Affiliations

  1. University Department of Child Health, Royal Hospital for Sick Children, Yorkhill, Glasgow, G3 8SJ, UK

    Forrester Cockburn

  2. Division of Metabolism, University Paediatric Department, Kinderspital, 8032, Zurich, Switzerland

    Richard Gitzelmann

Rights and permissions

Reprints and permissions

Copyright information

© 1982 The Society for the Study of Inborn Errors of Metabolism

About this chapter

Cite this chapter

Neufeld, E.F. (1982). Recent studies on the maturation of lysosomal enzymes. In: Cockburn, F., Gitzelmann, R. (eds) Inborn Errors of Metabolism in Humans. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-7325-1_7

Download citation

  • DOI: https://doi.org/10.1007/978-94-009-7325-1_7

  • Publisher Name: Springer, Dordrecht

  • Print ISBN: 978-94-009-7327-5

  • Online ISBN: 978-94-009-7325-1

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics

Search

Navigation