Abstract
This review is a limited update of a previous review of enzymes that degrade heparan sulphate (HS) and heparin (Hopwood, 1989). Newly-synthesised HS proteoglycan (HSPG) is internalised from the cell surface and catabolised with a half-time of 4 to 6 h in rat ovarian granulosa cells (Yanagishita and Hascall, 1984), and by more than 28 h in human colon carcinoma cells (Iozzo, 1987). Studies of both cell types have shown the existence of preliminary protease and an initial endoglycosidase activity in non-lysosomal (chloroquine-insensitive compartments) to generate HS intermediates of Mr 10 kDa, and further chloroquine-sensitive endoglycosidic activity to produce HS fragments of Mr 5 kDa which are rapidly degraded in the lysosome by a series of exohydrolases to monosaccharides and sulphate without the generation of intermediates. A number of distinct lysosomal membrane transporters are involved in the efflux of the monomeric products GlcNAc, GlcA and IdoA and sulphate ions from the lysosome (Jonas et al., 1989; Jonas and Jobe, 1990a, 1990b; Mancini et al., 1989) which can be reutilised in biosynthetic pathways (Rome and Hill, 1986).
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Barzu, T., van Rijn, J. L. M. L., Petitou, M., Tobelem, G. and Caen, J. P., 1987, Heparin degradation in the endothelial cells, Thromb. Res., 47:601.
Bielicki, J., Freeman, C., Clements, P. R., and Hopwood, J. J., 1990, Human liver iduronate-2-sulphatase: purification, characterisation and catalytic properties, Biochem. J., 271:75.
Buckmaster, M. J., Ferris, A. L., and Storrie, B., 1988, Effects of pH, detergent and salt on aggregation of Chinese-hamster-ovary-cell lysosomal enzymes, Biochem. J., 249:921.
Clements, P. R., Brooks, D. A., McCourt, P. A. G., and Hopwood, J. J., 1989, Immunopurification and characterisation of human a-L-iduronidase using monoclonal antibodies, Biochem. J., 259:199.
Clements, P. R., Brooks. D. A., Saccone, G. T. P., and Hopwood, J. J., 1985a, Human α-L-iduronidase. Purification, monoclonal antibody production, native and subunit molecular mass, Eur. J. Biochem., 152:21.
Clements, P. R., Muller, V., and Hopwood, J. J., 1985b, Human α-L-iduronidase. 2. Catalytic properties, Eur. J. Biochem., 152:29.
Freeman, C., and Hopwood, J. J., 1986, Human liver sulphamate sulphohydrolase: determination of native protein and subunit Mr values and influence of substrate aglycone structure on catalytic properties, Biochem. J., 234: 83.
Freeman, C., and Hopwood, J. J., 1987, Human liver N-acetylglucosamine 6-sulphate sulphatase: catalytic properties, Biochem. J., 246:355.
Freeman, C., and Hopwood, J. J., 1989, Human liver glucuronic acid-2-sulphatase: purification, characterization and catalytic properties, Biochem. J., 259:209.
Freeman, C., and Hopwood, J. J., 1991a, The estimation of glucuronate-2-sulphatase activity in skin fibroblast homogenates, Biochem. J., 278: In press.
Freeman, C., and Hopwood, J. J., 1991b, Human glucosamine-6-sulphatase deficiency: diagnostic enzymology towards heparin-derived trisaccharide substrates, Biochem. J., In press.
Freeman, C., and Hopwood, J. J., 1991c, Human liver a-L-iduronidase: catalytic activity toward heparin-derived oligosaccharide substrates, Biochem. J., In press.
Freeman, C., Clements, P. R., and Hopwood, J. J., 1987, Human liver N-acetylglucosamine 6-sulphate sulphatase: purification and characterization, Biochem. J., 246:347.
Gahl, W. A., Tietze, F., Bashan, N., Steinherz, J. D., and Schulman, J. D., 1982, Defective cysteine exodus from isolated lysosomal rich fractions of cystinoic leucocytes, Science. 257:9570.
Gallagher, J. T., Walker, A., Lyon, M., and Evans, W. M., 1988, Heparan sulphate-degrading endoglycosidase in liver plasma membranes, Biochem. J., 250:719.
Hopwood, J. J., 1989, Enzymes that degrade heparin and heparan sulphate, In: ‘Heparin: Chemical and Biological Properties, Clinical Applications’, (Lane D. W., and Lindahl, U., eds), Edward Arnold, London, pp 191.
Hopwood, J. J., and Morris, C. P., 1990, The mucopolysaccharidoses: diagnosis, molecular genetics and treatment, Mol. Biol. Med., 7:381.
Iozzo, R. V., 1987, Turnover of heparan sulfate proteoglycan in human colon carcinoma cells, J. Biol. Chem., 262:1888.
Ishihara, M., Fedarko, N. S., and Conrad, H. E., 1986, Transport of heparan sulphate into nuclei of hepatocytes, J. Biol. Chem., 261:13575.
Jin, L., Nakajima, M., and Nicolson, G. L., 1990, Immunochemical localization of heparanase in mouse and human melanomas. Int. J. Cancer. 45:1088.
Jonas, A. J., and Jobe, H., 1990a, Sulfate transport by rat liver lysosomes, J. Biol. Chem., 265:17545.
Jonas, A. J., and Jobe, H., 1990b, N-Acetyl-D-glucosamine countertransport in lysosomal membrane vesicles. Biochem. J., 268:41.
Jonas, A. J., Speller, R. J., Conrad, P. B., and Dubinsky, W. P., 1989, Transport of N-acetyl-D-glucosamine and N-acetyl-D-galactosamine by rat liver lysosomes, J. Biol. Chem., 264:15247.
Krüger, U., and Kresse, H., 1986, Endocytosis of proteoheparan sulfate by cultured skin fibroblasts, Biol. Chem. Hoppe-Seyler, 367:465.
Lindahl, U., 1989, Biosynthesis of heparin and related polysaccharides, In: ‘Heparin: Clinical and Biological Properties, Clinical Applications’, (Lane, D., and Lindahl, U., eds), Edward Arnold, London, pp 159.
Mancini, G. M. S., De Jong, H. R., Galjaard, H. and Verheijen, F. W., 1989, Characterisation of a proton-driven carrier for sialic acid in the lysosomal membrane, J. Biol. Chem., 264:15247.
Myerowitz, R., and Neufeld, E. F., 1981, Maturation of α-L-iduronidase in cultured human fibroblasts, J. Biol. Chem., 256:3044.
Nakajima, M., Irimura, T., and Nicolson, G. I., 1988 Heparanase and tumor metastasis, J. Cell Biochem., 36:157.
Nakajima, M., Irimura, T., Di Ferrante, N., and Nicolson, G. L., 1984, Metastatic melanoma cell heparanase: characterization of heparan sulfate degradation fragments produced by B16 melanoma endoglucuronidase, J. Biol. Chem., 259:2283.
Neufeld, E. F., and Muenzer, J., 1989, The mucopolysaccharidoses, In: ‘Metabolic Basis of Inherited Disease’, (Scriver, C. R., Beaudet, A. L., Sly, W. S., and Valle, D., eds), McGraw-Hill, New York, 6th Ed., pp 1565.
Oldberg, A., Heldin, C-H., Wasteson, Å., Busch, C., And Höök, M., 1980, Characterization of a platelet endoglycosidase degrading heparin-like polysaccharides, Biochem., 19:5755.
Oosta, G. M., Favreau, L. V., Beller, D. L., and Rosenberg, R. D., 1982, Purification and properties of human platelet heparitinase, J. Biol. Chem., 257:11249.
Renlund, M., Tietze, F., Gahl, W. A., 1986, Defective sialic acid egress from isolated fibroblast lysosomes of patients with Salla disease, Science, 232:759.
Roberts, S. H., Upadhyaya, M., Sarfarazi, M., and Harper, P. S., 1989, Further evidence localising the gene for Hunter’s syndrome to the distal region of the X chromosome, J. Med. Genet., 26:309.
Robertson, D. A., Callen, D. F., Baker, E. G., Morris, C. P., and Hopwood, J. J., 1988b, Chromosomal location of the gene for human glucosamine-6-sulphatase to 12q14, Hum. Genet., 79:175.
Robertson, D. A., Freeman, C, Nelson, P. V., Morris, C. P., and Hopwood, J. J., 1988a, Human glucosamine 6-sulphatase cDNA reveals homology with steroid sulphatase, Biochem. Biophys. Res. Commun., 157:218.
Rome, L. H., and Hill, D. F., 1986, Lysosomal degradation of glycoproteins and glycosaminoglycans: efflux and recycling of sulphate and N-acetylhexosamines, Biochem. J., 235:707.
Scott, H. S., Anson, D. S., Orsborn, A. M., Nelson, P. V., Clements, P. R., Morris, C. P., and Hopwood, J. J., 1991, Human α-L-iduronidase: cDNA isolation and expression. Proc. Natl. Acad. Sci. USA, In press.
Scott, H. S., Ashton, L. J., Eyre, H. J., Baker, E., Brooks, D. A., Callen, D. F., Morris, C. P., and Hopwood, J. J., 1990, α-L-Iduronidase is isolated to chromosome 4p16.3, Am. J. Hum. Genet., 47:802.
Sewell, R. F., Brenchley, P. E. C, and Mallick, N. P., 1989, Human mononuclear cells contain an endoglycosidase specific for heparan sulphate glycosaminoglycan demonstrable with the use of a specific solid-phase metabolically radiolabelled substrate. Biochem. J., 264:777.
Siciliano, L., Fiumara, L. P., Pavone, L., Freeman, C., Robertson, D., Morris, C. P., Hopwood, J. J., DiNatale, P., Musumeci, S., and Horwitz, A. L., 1990, Sanfilippo syndrome type D in two adolescent sisters, J. Med. Genet., 28:402.
Taylor, J. A., Gibson, G. J., Brooks, D. A., and Hopwood, J. J., 1991, α-L-Iduronidase in normal and mucopolysaccharidosis type I human skin fibroblasts, Biochem. J., 274:263.
Thunberg, L., Bäckström, G., Wasteson, Å., Robinson, H. C., Ögren, S., and Lindahl, U., 1982, Enzymatic depolymerization of heparin-related polysaccharides: substrate specificities of mouse mastocytoma and human platelet endo-β-D-glucuronidase, J. Biol. Chem., 257:10278.
Wilson, P. J., Bielicki, J., Clements, P. R., Occhiodoro, T., Anson, D., Morris, C. P., and Hopwood, J. J., 1990, Hunter syndrome: isolation of a cDNA clone encoding human iduronate-2-sulphatase and analysis of patient DNA, Proc. Natl. Acad. Sci. USA. 87:8531.
Wilson, P. J., Suthers, G. K., Callen, D. F., Baker, E., Nelson, P., Cooper, A., Wraith, E. J., Sutherland, G. R., Morris, C. P., and Hopwood, J. J., 1991, Frequent deletions at Xq28 indicate genetic heterogeneity in Hunter syndrome, Hum. Genet., 86:505.
Yanagishita, M., and Hascall, V. C., 1984, Metabolism of proteoglycans in rat ovarian granulosa cell culture: multiple intracellular degradative pathways and the effect of chloroquine, J. Biol. Chem., 259:10270.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1992 Springer Science+Business Media New York
About this chapter
Cite this chapter
Freeman, C., Hopwood, J. (1992). Lysosomal Degradation of Heparin and Heparan Sulphate. In: Lane, D.A., Björk, I., Lindahl, U. (eds) Heparin and Related Polysaccharides. Advances in Experimental Medicine and Biology, vol 313. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-2444-5_13
Download citation
DOI: https://doi.org/10.1007/978-1-4899-2444-5_13
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4899-2446-9
Online ISBN: 978-1-4899-2444-5
eBook Packages: Springer Book Archive