scholarly journals Insights into the role of 3-O-sulfotransferase in heparan sulfate biosynthesis

2017 ◽  
Vol 15 (32) ◽  
pp. 6792-6799 ◽  
Author(s):  
Maria Cecília Zorél Meneghetti ◽  
Tarsis Gesteira Ferreira ◽  
Alexandre Keiji Tashima ◽  
Suely F. Chavante ◽  
Edwin Alexander Yates ◽  
...  
Keyword(s):  
Heparan Sulfate ◽  
Tree Structure

Tree structure for the biosynthesis of 3-O-sulfated glucosamine.

scholarly journals Role of heparan sulfate proteoglycans in the binding and uptake of apolipoprotein E-enriched remnant lipoproteins by cultured cells

1993 ◽  
Vol 268 (14) ◽  
pp. 10160-10167
Author(s):  
Z.S. Ji ◽  
W.J. Brecht ◽  
R.D. Miranda ◽  
M.M. Hussain ◽  
T.L. Innerarity ◽  
...  
Keyword(s):  
Apolipoprotein E ◽  
Heparan Sulfate ◽  
Cultured Cells ◽  
Heparan Sulfate Proteoglycans ◽  
Remnant Lipoproteins

Biological role of heparan sulfate in osteogenesis: A review

2021 ◽  
pp. 118490
Author(s):  
Zhujie Xu ◽  
Shayang Chen ◽  
Dehong Feng ◽  
Yi Liu ◽  
Qiqi Wang ◽  
...  
Keyword(s):  
Heparan Sulfate ◽  
Biological Role

scholarly journals Heparan sulfate and heparin interactions with proteins

2015 ◽  
Vol 12 (110) ◽  
pp. 20150589 ◽  
Author(s):  
Maria C. Z. Meneghetti ◽  
Ashley J. Hughes ◽  
Timothy R. Rudd ◽  
Helena B. Nader ◽  
Andrew K. Powell ◽  
...  
Keyword(s):  
Heparan Sulfate ◽  
Ex Vivo ◽  
Sequence Specificity ◽  
Structure Activity ◽  
Multiple Binding Sites ◽  
Multiple Binding ◽  
Heparin Activity

Heparan sulfate (HS) polysaccharides are ubiquitous components of the cell surface and extracellular matrix of all multicellular animals, whereas heparin is present within mast cells and can be viewed as a more sulfated, tissue-specific, HS variant. HS and heparin regulate biological processes through interactions with a large repertoire of proteins. Owing to these interactions and diverse effects observed during in vitro , ex vivo and in vivo experiments, manifold biological/pharmacological activities have been attributed to them. The properties that have been thought to bestow protein binding and biological activity upon HS and heparin vary from high levels of sequence specificity to a dependence on charge. In contrast to these opposing opinions, we will argue that the evidence supports both a level of redundancy and a degree of selectivity in the structure–activity relationship. The relationship between this apparent redundancy, the multi-dentate nature of heparin and HS polysaccharide chains, their involvement in protein networks and the multiple binding sites on proteins, each possessing different properties, will also be considered. Finally, the role of cations in modulating HS/heparin activity will be reviewed and some of the implications for structure–activity relationships and regulation will be discussed.

scholarly journals Role of heparan sulfate in intestinal normal and cancer stem cells (607.10)

2014 ◽  
Vol 28 (S1) ◽  
Author(s):  
Motohiro Nonaka ◽  
Jun Nakayama ◽  
Minoru Fukuda
Keyword(s):  
Stem Cells ◽  
Cancer Stem Cells ◽  
Heparan Sulfate

scholarly journals Glypican-1 drives unconventional secretion of Fibroblast Growth Factor 2

2021 ◽  
Author(s):  
Carola Sparn ◽  
Eleni Dimou ◽  
Annalena Meyer ◽  
Roberto Saleppico ◽  
Sabine Wegehingel ◽  
...  
Keyword(s):  
Growth Factor ◽  
Heparan Sulfate ◽  
Fibroblast Growth Factor ◽  
Fibroblast Growth Factor 2 ◽  
Structural Basis ◽  
Limiting Factor ◽  
Fibroblast Growth ◽  
Unconventional Secretion ◽  
Rate Limiting

Fibroblast Growth Factor 2 (FGF2) is a tumor cell survival factor that is transported into the extracellular space by an unconventional secretory mechanism. Cell surface heparan sulfate proteoglycans are known to play an essential role in this process. Unexpectedly, we found that among the diverse sub-classes consisting of syndecans, perlecans, glypicans and others, Glypican-1 (GPC1) is both the principle and rate-limiting factor that drives unconventional secretion of FGF2. By contrast, we demonstrate GPC1 to be dispensable for FGF2 signaling into cells. We provide first insights into the structural basis for GPC1-dependent FGF2 secretion, identifying disaccharides with N-linked sulfate groups to be enriched in the heparan sulfate chains of GPC1 to which FGF2 binds with high affinity. Our findings have broad implications for the role of GPC1 as a key molecule in tumor progression.

scholarly journals Mapping the Interactome of the Nuclear Heparan Sulfate Proteoglycan Syndecan-1 in Mesothelioma Cells

Biomolecules ◽  
2020 ◽  
Vol 10 (7) ◽  
pp. 1034 ◽  
Author(s):  
Ashish Kumar-Singh ◽  
Jatin Shrinet ◽  
Malgorzata Maria Parniewska ◽  
Jonas Fuxe ◽  
Katalin Dobra ◽  
...  
Keyword(s):  
Heparan Sulfate ◽  
Cell Line ◽  
Rna Splicing ◽  
Heparan Sulfate Proteoglycan ◽  
Sulfate Proteoglycan ◽  
Mesothelioma Cell Line ◽  
Mesothelioma Cell ◽  
And Migration ◽  
Dependent Transport

Syndecan-1 (SDC1) is a cell surface heparan sulfate proteoglycan (HSPG), which regulates various signaling pathways controlling the proliferation and migration of malignant mesothelioma and other types of cancer. We have previously shown that SDC1 can translocate to the nucleus in mesothelioma cells through a tubulin-dependent transport mechanism. However, the role of nuclear SDC1 is largely unknown. Here, we performed co-immunoprecipitation (Co-IP) of SDC1 in a mesothelioma cell line to identify SDC1 interacting proteins. The precipitates contained a large number of proteins, indicating the recovery of protein networks. Proteomic analysis with a focus on nuclear proteins revealed an association with pathways related to cell proliferation and RNA synthesis, splicing and transport. In support of this, the top RNA splicing candidates were verified to interact with SDC1 by Co-IP and subsequent Western blot analysis. Further loss- and gain-of-function experiments showed that SDC1 influences RNA levels in mesothelioma cells. The results identify a proteomic map of SDC1 nuclear interactors in a mesothelioma cell line and suggest a previously unknown role for SDC1 in RNA biogenesis. The results should serve as a fundament for further studies to discover the role of nuclear SDC1 in normal and cancer cells of different origin.

scholarly journals Genogroup II Noroviruses Efficiently Bind to Heparan Sulfate Proteoglycan Associated with the Cellular Membrane

2004 ◽  
Vol 78 (8) ◽  
pp. 3817-3826 ◽  
Author(s):  
Masaru Tamura ◽  
Katsuro Natori ◽  
Masahiko Kobayashi ◽  
Tatsuo Miyamura ◽  
Naokazu Takeda
Keyword(s):  
Cell Surface ◽  
Heparan Sulfate ◽  
Cellular Membrane ◽  
Heparan Sulfate Proteoglycan ◽  
Sulfate Proteoglycan ◽  
Sulfated Glycosaminoglycan ◽  
The Family ◽  
Sulfated Derivative ◽  
Causative Agents

ABSTRACT Norovirus (NV), a member of the family Caliciviridae, is one of the important causative agents of acute gastroenteritis. In the present study, we found that virus-like particles (VLPs) derived from genogroup II (GII) NV were bound to cell surface heparan sulfate proteoglycan. Interestingly, the VLPs derived from GII were more than ten times likelier to bind to cells than were those derived from genogroup I (GI). Heparin, a sulfated glycosaminoglycan, and suramin, a highly sulfated derivative of urea, efficiently blocked VLP binding to mammalian cell surfaces. The reagents known to bind to cell surface heparan sulfate, as well as the enzymes that specifically digest heparan sulfate, markedly reduced VLP binding to the cells. Treatment of the cells with chlorate revealed that sulfation of heparan sulfate plays an important role in the NV-heparan sulfate interaction. The binding efficiency of NV to undifferentiated Caco-2 (U-Caco-2) cells differed largely between GI NV and GII NV, whereas the efficiency of binding to differentiated Caco-2 (D-Caco-2) cells did not differ significantly between the two genogroups, although slight differences between strains were observed. Digestion with heparinase I resulted in a reduction of up to 90% in U-Caco-2 cells and a reduction of up to only 50% in D-Caco-2 cells, indicating that heparan sulfate is the major binding molecule for U-Caco-2 cells, while it contributed to only half of the binding in the case of D-Caco-2 cells. The other half of those VLPs was likely to be associated with H-type blood antigen, suggesting that GII NV has two separate binding sites. The present study is the first to address the possible role of cell surface glycosaminoglycans in the binding of recombinant VLPs of NV.

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