scholarly journals Cancer Metastasis: The Role of the Extracellular Matrix and the Heparan Sulfate Proteoglycan Perlecan

2020 ◽  
Vol 9 ◽  
Author(s):  
Zehra Elgundi ◽  
Michael Papanicolaou ◽  
Gretel Major ◽  
Thomas R. Cox ◽  
James Melrose ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Heparan Sulfate ◽  
Cancer Metastasis ◽  
Heparan Sulfate Proteoglycan ◽  
Sulfate Proteoglycan

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.

The binding of heparin to the extracellular matrix of endothelial cells up-regulates the synthesis of an antithrombotic heparan sulfate proteoglycan

2008 ◽  
Vol 217 (2) ◽  
pp. 328-337 ◽  
Author(s):  
Edvaldo S. Trindade ◽  
Constance Oliver ◽  
Maria C. Jamur ◽  
Hugo A.O. Rocha ◽  
Célia R.C. Franco ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Endothelial Cells ◽  
Heparan Sulfate ◽  
Heparan Sulfate Proteoglycan ◽  
Sulfate Proteoglycan

scholarly journals Role of the Heparan Sulfate Proteoglycan Syndecan-1 (CD138) in Delayed-Type Hypersensitivity

2009 ◽  
Vol 182 (8) ◽  
pp. 4985-4993 ◽  
Author(s):  
Behzad Kharabi Masouleh ◽  
Gerdy B. Ten Dam ◽  
Martin K. Wild ◽  
Ruth Seelige ◽  
Johan van der Vlag ◽  
...  
Keyword(s):  
Heparan Sulfate ◽  
Heparan Sulfate Proteoglycan ◽  
Delayed Type Hypersensitivity ◽  
Sulfate Proteoglycan

scholarly journals Characterization of a novel heparan sulfate proteoglycan found in the extracellular matrix of liver sinusoids and basement membranes.

1991 ◽  
Vol 113 (5) ◽  
pp. 1231-1241 ◽  
Author(s):  
C J Soroka ◽  
M G Farquhar
Keyword(s):  
Extracellular Matrix ◽  
Basement Membrane ◽  
Heparan Sulfate ◽  
Rat Liver ◽  
Core Protein ◽  
Heparan Sulfate Proteoglycan ◽  
Basement Membranes ◽  
Sulfate Proteoglycan ◽  
Sinusoidal Cell ◽  
Space Of Disse

A novel heparan sulfate proteoglycan (HSPG) present in the extracellular matrix of rat liver has been partially characterized. Proteoglycans were purified from a high salt extract of total microsomes from rat liver and found to consist predominantly (approximately 90%) of HSPG. A polyclonal antiserum raised against this fraction specifically recognized HSPG by immunoprecipitation and immunoblotting. The intact, fully glycosylated HSPG migrated as a broad smear (150-300 kD) by SDS-PAGE, but after deglycosylation with trifluoromethanesulfonic acid only a single approximately 40-kD band was seen. By immunocytochemistry this HSPG was localized in the perisinusoidal space of Disse associated with irregular clumps of basement membrane-like extracellular matrix material, some of which was closely associated with the hepatocyte sinusoidal cell surface. It was also localized in biosynthetic compartments (rough ER and Golgi cisternae) of hepatocytes, suggesting that this HSPG is synthesized and deposited in the space of Disse by the hepatocyte. The anti-liver HSPG IgG also stained basement membranes of hepatic blood vessels and bile ducts as well as those of kidney and several other organs (heart, pancreas, and intestine). An antibody that recognizes the basement membrane HSPG found in the rat glomerular basement membrane did not precipitate the 150-300-kD rat liver HSPG. We conclude that the liver sinusoidal space of Disse contains a novel population of HSPG that differs in its overall size, its distribution and in the size of its core protein from other HSPG (i.e., membrane-intercalated HSPG) previously described in rat liver. It also differs in its core protein size from HSPG purified from other extracellular matrix sources. This population of HSPG appears to be a member of the basement membrane HSPG family.

An important role of heparan sulfate proteoglycan (perlecan) in a model system for the deposition and persistence of fibrillar aβ-amyloid in rat brain

Neuron ◽  
1994 ◽  
Vol 12 (1) ◽  
pp. 219-234 ◽  
Author(s):  
Alan D. Snow ◽  
Raymond Sekiguchi ◽  
David Nochlin ◽  
Paul Fraser ◽  
Koji Kimata ◽  
...  
Keyword(s):  
Heparan Sulfate ◽  
Rat Brain ◽  
Model System ◽  
Heparan Sulfate Proteoglycan ◽  
Sulfate Proteoglycan ◽  
Aβ Amyloid
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