Developing Heparan Sulfate Proteoglycan Miniaturized Capillary Column to Study its Recognition Mechanism with its Molecular Target. Application to Human Telomerase, a Cell Penetrating Peptide and Mitoxantrone a Potential Covid-19 Inhibitor.

2021 ◽  
Author(s):  
Yves Claude Guillaume ◽  
CLAIRE ANDRE
Keyword(s):  
Heparan Sulfate ◽  
Capillary Column ◽  
Molecular Target ◽  
Heparan Sulfate Proteoglycans ◽  
Cell Penetrating Peptide ◽  
Sulfate Proteoglycan ◽  
Recognition Mechanism ◽  
A Cell ◽  
Human Telomerase ◽  
Viral Receptors

The interactions of Heparan Sulfate proteoglycans (HSPGs) present on cell surface with target proteins lead to cell signaling and is considered as viral receptors. The analysis of the recognition mechanism...

Transient expression of a cell surface heparan sulfate proteoglycan (syndecan) during limb development

1990 ◽  
Vol 140 (1) ◽  
pp. 83-92 ◽  
Author(s):  
Michael Solursh ◽  
Rebecca S. Reiter ◽  
Karen L. Jensen ◽  
Masato Kato ◽  
Merton Bernfield
Keyword(s):  
Cell Surface ◽  
Heparan Sulfate ◽  
Transient Expression ◽  
Limb Development ◽  
Heparan Sulfate Proteoglycan ◽  
Sulfate Proteoglycan ◽  
A Cell

Syndecan-3: a cell-surface heparan sulfate proteoglycan important for chondrocyte proliferation and function during limb skeletogenesis

2005 ◽  
Vol 23 (3) ◽  
pp. 191-199 ◽  
Author(s):  
Maurizio Pacifici ◽  
Tsuyoshi Shimo ◽  
Chiara Gentili ◽  
Thorsten Kirsch ◽  
Theresa A. Freeman ◽  
...  
Keyword(s):  
Cell Surface ◽  
Heparan Sulfate ◽  
Heparan Sulfate Proteoglycan ◽  
Sulfate Proteoglycan ◽  
Chondrocyte Proliferation ◽  
A Cell ◽  
And Function

Heparan sulfate proteoglycan and FGF receptor target basic FGF to different intracellular destinations

1993 ◽  
Vol 105 (4) ◽  
pp. 1085-1093 ◽  
Author(s):  
J. Reiland ◽  
A.C. Rapraeger
Keyword(s):  
Heparan Sulfate ◽  
Cellular Responses ◽  
Heparan Sulfate Proteoglycans ◽  
Sulfate Proteoglycan ◽  
Heparin Binding ◽  
Fgf Receptor ◽  
Basic Fgf ◽  
Intracellular Targeting ◽  
Heparin Binding Growth Factors ◽  
Intracellular Fate

Basic FGF is a prototype of a family of heparin binding growth factors that regulate a variety of cellular responses including cell growth, morphogenesis and differentiation. At least two families of receptors bind bFGF and could mediate its response: (1) tyrosine kinase-containing FGF receptors, designated FGFR-1 to FGFR-4, and (2) heparan sulfate proteoglycans that bind bFGF through their heparan sulfate chains. Both are known to undergo internalization and thus bFGF bound to the different receptors may be internalized via more than one pathway. It is not known whether the intracellular fate of bFGF differs depending upon which receptor binds it at the cell surface. To investigate the respective roles of these receptors in the intracellular targeting of bFGF, we utilized NMuMG cells that bind and internalize bFGF through their heparan sulfate proteoglycans, but do not express detectable levels of FGFRs nor respond to bFGF. Basic FGF conjugated to saporin (bFGF-saporin) was used as a probe to study targeting of bFGF by the different receptors. Saporin is a cytotoxin that has no effect on cells if added exogenously. However, it kills cells if it gains access to the cytoplasm. The NMuMG cells internalize bFGF-saporin but are not killed. Transfecting these cells with FGFR-1 results in bFGF-responsive cells, which bind and internalize bFGF through FGFR-1, and are killed. Removing the heparan sulfate from these cells eliminates killing by bFGF-saporin.(ABSTRACT TRUNCATED AT 250 WORDS)

scholarly journals Molecular Characterization of the Heparin-Dependent Transduction Domain on the Capsid of a Novel Adeno-Associated Virus Isolate, AAV(VR-942)

2008 ◽  
Vol 82 (17) ◽  
pp. 8911-8916 ◽  
Author(s):  
Michael Schmidt ◽  
Lakshmanan Govindasamy ◽  
Sandra Afione ◽  
Nick Kaludov ◽  
Mavis Agbandje-McKenna ◽  
...  
Keyword(s):  
Heparan Sulfate ◽  
Virus Isolate ◽  
Simian Virus ◽  
Complementation Group ◽  
Heparan Sulfate Proteoglycans ◽  
Sulfate Proteoglycan ◽  
Amino Acid Residues ◽  
Adeno Associated Virus ◽  
High Level

ABSTRACT A new adeno-associated virus (AAV), referred to as AAV(VR-942), has been isolated as a contaminant of adenovirus strain simian virus 17. The sequence of the rep gene places it in the AAV serotype 2 (AAV2) complementation group, while the capsid is only 88% identical to that of AAV2. High-level AAV(VR-942) transduction activity requires cell surface heparan sulfate proteoglycans, although AAV(VR-942) lacks residues equivalent to the AAV2 R585 and R588 amino acid residues essential for mediating the interaction of AAV2 with the heparan sulfate proteoglycan receptor. Instead, AAV(VR-942) uses a distinct transduction region. This finding shows that distinct domains on different AAV isolates can be responsible for the same activities.

scholarly journals Isolation of a cell-surface receptor for chick neural retina adherons.

1985 ◽  
Vol 100 (1) ◽  
pp. 56-63 ◽  
Author(s):  
D Schubert ◽  
M LaCorbiere
Keyword(s):  
Cell Surface ◽  
Heparan Sulfate ◽  
Cell Aggregation ◽  
Neural Retina ◽  
Heparan Sulfate Proteoglycan ◽  
Cell Surface Receptor ◽  
Sulfate Proteoglycan ◽  
Surface Receptor ◽  
A Cell ◽  
Cell Cell

Embryonic chick neural retina cells release glycoprotein complexes, termed adherons, into their culture medium. When absorbed onto the surface of petri dishes, neural retina adherons increase the initial rate of neural retina cell adhesion. In solution they increase the rate of cell-cell aggregation. Cell-cell and adheron-cell adhesions of cultured retina cells are selectively inhibited by heparan-sulfate glycosaminoglycan, but not by chondroitin sulfate or hyaluronic acid, suggesting that a heparan-sulfate proteoglycan may be involved in the adhesion process. We isolated a heparan-sulfate proteoglycan from the growth-conditioned medium of neural retina cells, and prepared an antiserum against it. Monovalent Fab' fragments of these antibodies completely inhibited cell-adheron adhesion, and partially blocked spontaneous cell-cell aggregation. An antigenically and structurally similar heparan-sulfate proteoglycan was isolated from the cell surface. This proteoglycan bound directly to adherons, and when absorbed to plastic, stimulated cell-substratum adhesion. These data suggest that a heparan-sulfate proteoglycan on the surface of chick neural retina cells acted as a receptor for adhesion-mediating glycoprotein complexes (adherons).

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