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Secretion of unphosphorylated and phosphorylated xyloside-induced glycosaminoglycan chains

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Abstract

Secretion ofp-nitrophenyl-β-xyloside-induced glycosaminoglycan chains in cultured fibroblasts is considered to involve transport through the endoplasmic reticulum and the Golgi apparatus. Purified glycosaminoglycans from fibroblast secretions contain small amounts of covalently bound [32P]phosphate. However, exhaustive digestion with chondroitin AC and ABC lyases yields an unphosphorylated linkage region tetrasaccharide in the majority of all polysaccharide chains. The phosphate label is associated predominantly with material of the expected behavior of linkage region hexasaccharides. Thus, phosphorylation is not a prerequisite to secretion of xyloside-induced glycosaminoglycan chains.

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Authors and Affiliations

  1. Institute of Physiological Chemistry and Pathobiochemistry, University of Münster, Waldeyerstr. 15, D-4400, Münster, Federal Republic of Germany

    Hermann Greve & Hans Kresse

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  1. Hermann Greve
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  2. Hans Kresse
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Greve, H., Kresse, H. Secretion of unphosphorylated and phosphorylated xyloside-induced glycosaminoglycan chains. Glycoconjugate J 5, 175–183 (1988). https://doi.org/10.1007/BF01061206

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  • DOI: https://doi.org/10.1007/BF01061206

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