Drosophila heparan sulfate, a novel design.

The Journal of Biological Chemistry
Marion Kusche-GullbergU Lindahl

Abstract

Heparan sulfate (HS) proteoglycans play critical roles in a wide variety of biological processes such as growth factor signaling, cell adhesion, wound healing, and tumor metastasis. Functionally important interactions between HS and a variety of proteins depend on specific structural features within the HS chains. The fruit fly (Drosophila melanogaster) is frequently applied as a model organism to study HS function in development. Previous structural studies of Drosophila HS have been restricted to disaccharide composition, without regard to the arrangement of saccharide domains typically found in vertebrate HS. Here, we biochemically characterized Drosophila HS by selective depolymerization with nitrous acid. Analysis of the generated saccharide products revealed a novel HS design, involving a peripheral, extended, presumably single, N-sulfated domain linked to an N-acetylated sequence contiguous with the linkage to core protein. The N-sulfated domain may be envisaged as a heparin structure of unusually low O-sulfate content.

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Citations

Jul 16, 2015·International Journal of Experimental Pathology·John Gallagher
Apr 26, 2019·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Dominique ManikowskiKay Grobe
Nov 28, 2019·Glycoconjugate Journal·Shoko Nishihara
Jan 30, 2021·Frontiers in Cell and Developmental Biology·Dominique ManikowskiKay Grobe
May 15, 2015·Journal of Cell Science·Corinna OrtmannKay Grobe

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