Heparan sulfate proteoglycans (HSPGs) are molecules that are comprised of a core protein modified with heparan sulfate (HS), a negatively charged linear polysaccharide, consisting of uronic acid and N-acetyl-glucosamine (GlcNAc) disaccharide repeats. Generally, these molecules are located on the cell surface and the extracellular matrix. HSPGs have been known to be associated with various biological processes such as growth factor signaling, neuronal
development, and cell adhesion. HS chains possess heterogeneous structures, and their diverse patterns of sulfation can determine the binding specificity for certain proteins. 6-O-sulfation of GlcNAc (or GlcNSO3) is the key modification of HS, since it can be dynamically regulated; heparan sulfate 6-sulfotransferase (Hs6st) catalyzes the transfer of sulfate groups of GlcNAc (or GlcNSO3), while heparan sulfate 6-O endosulfatase (Sulf1) removes it. However, how 6-O-sulfation is regulated during animal development remains largely unknown. In this poster, we will present expression analysis of these enzymes in the fruit fly Drosophila melanogaster. We generated a transgenic reporter fly for Sulf1 gene, and its expression pattern was compared with that of Hs6st gene using Hs6st-lacZ enhancer trapline. Our study will provide regulatory mechanisms of HS during the development of Drosophila as well as other multi-cellular organisms.
Mentor: Dr. Hiroshi Nakato
Acknowledgements: Katsufumi Dejima and Adam Kleinschmit
Uk, Samantha; Dang, An.
Comparative Analysis of Hs6st and Sulf1-mcherry Expression Patterns in Drosophila.
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