Heparan Sulfate Proteoglycans in Drosophila melanogaster

2014 ◽  
pp. 1-6
Author(s):  
Keisuke Kamimura ◽  
Nobuaki Maeda
Keyword(s):  
Drosophila Melanogaster ◽  
Heparan Sulfate ◽  
Heparan Sulfate Proteoglycans

scholarly journals Perlecan regulates bidirectional Wnt signaling at the Drosophila neuromuscular junction

2013 ◽  
Vol 200 (2) ◽  
pp. 219-233 ◽  
Author(s):  
Keisuke Kamimura ◽  
Kohei Ueno ◽  
Jun Nakagawa ◽  
Rie Hamada ◽  
Minoru Saitoe ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Neuromuscular Junction ◽  
Heparan Sulfate ◽  
Wnt Signaling ◽  
Nuclear Import ◽  
Heparan Sulfate Proteoglycans ◽  
Down Regulation ◽  
Bidirectional Signaling ◽  
Synaptic Boutons ◽  
Signaling Activity

Heparan sulfate proteoglycans (HSPGs) play pivotal roles in the regulation of Wnt signaling activity in several tissues. At the Drosophila melanogaster neuromuscular junction (NMJ), Wnt/Wingless (Wg) regulates the formation of both pre- and postsynaptic structures; however, the mechanism balancing such bidirectional signaling remains elusive. In this paper, we demonstrate that mutations in the gene of a secreted HSPG, perlecan/trol, resulted in diverse postsynaptic defects and overproduction of synaptic boutons at NMJ. The postsynaptic defects, such as reduction in subsynaptic reticulum (SSR), were rescued by the postsynaptic activation of the Frizzled nuclear import Wg pathway. In contrast, overproduction of synaptic boutons was suppressed by the presynaptic down-regulation of the canonical Wg pathway. We also show that Trol was localized in the SSR and promoted postsynaptic accumulation of extracellular Wg proteins. These results suggest that Trol bidirectionally regulates both pre- and postsynaptic activities of Wg by precisely distributing Wg at the NMJ.

scholarly journals Host Glycosaminoglycan Confers Susceptibility to Bacterial Infection in Drosophila melanogaster

2008 ◽  
Vol 77 (2) ◽  
pp. 860-866 ◽  
Author(s):  
Miriam J. Baron ◽  
Sandra L. Wong ◽  
Kent Nybakken ◽  
Vincent J. Carey ◽  
Lawrence C. Madoff
Keyword(s):  
Drosophila Melanogaster ◽  
Heparan Sulfate ◽  
Group B Streptococcus ◽  
Heparan Sulfate Proteoglycans ◽  
Bacterial Killing ◽  
C Protein ◽  
Susceptibility To Infection ◽  
Anchoring Proteins ◽  
Group B ◽  
Streptococcus A

ABSTRACT Many pathogens engage host cell surface glycosaminoglycans, but redundancy in pathogen adhesins and host glycosaminoglycan-anchoring proteins (heparan sulfate proteoglycans) has limited the understanding of the importance of glycosaminoglycan binding during infection. The alpha C protein of group B streptococcus, a virulence determinant for this neonatal human pathogen, binds to host glycosaminoglycan and mediates the entry of bacteria into human cells. We studied alpha C protein-glycosaminoglycan binding in Drosophila melanogaster, whose glycosaminoglycan repertoire resembles that of humans but whose genome includes only three characterized membrane heparan sulfate proteoglycan genes. The knockdown of glycosaminoglycan polymerases or of heparan sulfate proteoglycans reduced the cellular binding of alpha C protein. The interruption of alpha C protein-glycosaminoglycan binding was associated with longer host survival and a lower bacterial burden. These data indicate that the glycosaminoglycan-alpha C protein interaction involves multiple heparan sulfate proteoglycans and impairs bacterial killing. Host glycosaminoglycans, anchored by multiple proteoglycans, thereby determine susceptibility to infection. Because there is homology between Drosophila and human glycosaminoglycan/proteoglycan structures and many pathogens express glycosaminoglycan-binding structures, our data suggest that interfering with glycosaminoglycan binding may protect against infections in humans.

Localization of cell-surface and basement-membrane heparan-sulfate proteoglycans using the malaria circumsporozoite protein

1994 ◽  
Vol 52 ◽  
pp. 294-295
Author(s):  
U. Frevert ◽  
S. Sinnis ◽  
C. Cerami ◽  
V. Nussenzweig
Keyword(s):  
Heparan Sulfate ◽  
Protein A ◽  
Kidney Tissue ◽  
Plasmodium Species ◽  
Its Region ◽  
Basement Membranes ◽  
Heparan Sulfate Proteoglycans ◽  
Infected Mosquito ◽  
Complement Components ◽  
Region Ii

Malaria sporozoites, which invade hepatocytes within minutes after transmission by an infected mosquito, are covered with the circumsporozoite (CS) protein, which in all Plasmodium species contains the conserved region II-plus. This region is also found as a cell-adhesive motif in a variety of host proteins like thrombospondin, properdin and the terminal complement components.The CS protein with its region II-plus specifically binds to heparan sulfate proteoglycans (HSPG) on the basolateral surface of hepatocytes in the space of Disse (FIG. 1), to certain basolateral cell membranes and basement membranes of the kidney (FIG. 2) as well as to heparin in the granules of connective tissue mast cells. The distribution of the HSPG receptors for the CS protein was examined by incubation of Lowicryl K4M or LR White sections of liver and kidney tissue with the recombinant CS ligand, whose binding sites were detected with a monoclonal anti-CS antibody and protein A gold.

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