Abnormal mast cells in mice deficient in a heparin-synthesizing enzyme

Erik Forsberg, Gunnar Pejler, Maria Ringvall, Carolina Lunderius, Bianca Tomasini-Johansson, Marion Kusche-Gullberg, Inger Eriksson, Johan Ledin, Lars Hellman and Lena Kjellén ()
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Erik Forsberg: Department of Cell and Molecular Biology
Gunnar Pejler: Swedish University of Agricultural Sciences
Maria Ringvall: Department of Cell and Molecular Biology
Carolina Lunderius: Department of Cell and Molecular Biology
Bianca Tomasini-Johansson: Swedish University of Agricultural Sciences
Marion Kusche-Gullberg: Department of Medical Biochemistry and Microbiology
Inger Eriksson: Swedish University of Agricultural Sciences
Johan Ledin: Swedish University of Agricultural Sciences
Lars Hellman: Department of Cell and Molecular Biology
Lena Kjellén: Swedish University of Agricultural Sciences

Nature, 1999, vol. 400, issue 6746, 773-776

Abstract: Abstract Heparin is a sulphated polysaccharide, synthesized exclusively by connective-tissue-type mast cells1 and stored in the secretory granules in complex with histamine and various mast-cell proteases2. Although heparin has long been used as an antithrombotic drug, endogenous heparin is not present in the blood, so it cannot have a physiological role in regulating blood coagulation. The biosynthesis of heparin involves a series of enzymatic reactions, including sulphation at various positions1,3. The initial modification step, catalysed by the enzyme glucosaminyl N -deacetylase/N -sulphotransferase-2, NDST-2 (4–7), is essential for the subsequent reactions. Here we report that mice carrying a targeted disruption of the gene encoding NDST-2 are unable to synthesize sulphated heparin. These NDST-2-deficient mice are viable and fertile but have fewer connective-tissue-type mast cells; these cells have an altered morphology and contain severely reduced amounts of histamine and mast-cell proteases. Our results indicate that one site of physiological action for heparin could be inside connective-tissue-type mast cells, where its absence results in severe defects in the secretory granules.

Date: 1999
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DOI: 10.1038/23488

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