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J. Biol. Chem., Vol. 276, Issue 6, 3772-3777, February 9, 2001

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Altered Processing of Fibronectin in Mice Lacking Heparin
A ROLE FOR HEPARIN-DEPENDENT MAST CELL CHYMASE IN FIBRONECTIN DEGRADATION^*

Elena Tchougounova, Erik Forsberg^§, Gustaf Angelborg, Lena Kjellén, and Gunnar Pejler^¶

From the  Swedish University of Agricultural Sciences, Department of Veterinary Medical Chemistry, The Biomedical Center, 751 23 Uppsala, Sweden and the ^§ Uppsala University, Department of Medical Biochemistry and Microbiology, The Biomedical Center, 751 24 Uppsala, Sweden

We have previously generated a mouse strain with a defect in its heparin biosynthesis by targeting the gene for N-deacetylase/N-sulfotransferase-2 (NDST-2). The NDST-2^/ mice show reduced levels of various mast cell mediators such as histamine and various heparin-binding mast cell proteases, including chymases, tryptases, and carboxypeptidase A. In this work we have addressed the possible functional consequences of the lack of sulfated heparin. Peritoneal cells were harvested from normal and NDST-2^/ mice. After culturing the cells, conditioned media were collected and were subjected to SDS-polyacrylamide gel electrophoresis under reducing conditions. Several differences in the protein patterns were observed, including the presence of large amounts of a ~250-kDa protein in medium from NDST-2^/ mice that was absent in normal controls. Peptide microsequencing revealed identity of this protein with fibronectin. Western blot analysis showed the presence of fibronectin degradation products in cell cultures from normal mice, which were absent in cultures from NDST-2^/ animals. Further experiments showed that the degradation of fibronectin observed in cell cultures from NDST-2^+/+ mice was catalyzed by mast cell chymase in a strongly heparin-dependent manner. This report thus indicates a biological function for chymase/heparin proteoglycan complexes in fibronectin turnover.

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