scholarly journals Interaction between the Carboxyl-terminal Heparin-binding Domain of Fibronectin and (−)-Epigallocatechin Gallate

1998 ◽  
Vol 62 (5) ◽  
pp. 1031-1032 ◽  
Author(s):  
Masaki SAZUKA ◽  
Mamoru ISEMURA ◽  
Satoko ISEMURA
Keyword(s):  
Epigallocatechin Gallate ◽  
Binding Domain ◽  
Heparin Binding ◽  
Heparin Binding Domain ◽  
Carboxyl Terminal

scholarly journals Platelet thrombospondin mediates attachment and spreading of human melanoma cells.

1987 ◽  
Vol 104 (1) ◽  
pp. 131-139 ◽  
Author(s):  
D D Roberts ◽  
J A Sherwood ◽  
V Ginsburg
Keyword(s):  
Monoclonal Antibodies ◽  
Cell Attachment ◽  
Melanoma Cells ◽  
Binding Domain ◽  
Heparin Binding ◽  
Amino Terminal ◽  
Sulfated Fucan ◽  
Heparin Binding Domain ◽  
Carboxyl Terminal ◽  
Inhibition Studies

Human platelet thrombospondin adsorbed on plastic promotes attachment and spreading of human G361 melanoma cells. Attachment is rapid, and spreading is maximal by 90 min with 60-90% of the attached cells spread. In contrast, thrombospondin promotes attachment but not spreading of human C32 melanoma cells, which attach and spread only on laminin substrates. The specificity of these interactions and the regions of the thrombospondin molecule involved in attachment and spreading were examined using proteolytic fragments of thrombospondin and by inhibition studies. The sulfated fucan, fucoidan, and monoclonal antibody A2.5, which is directed against the heparin-binding domain of thrombospondin, selectively inhibit spreading but only weakly inhibit attachment. Monoclonal antibodies against some other domains of thrombospondin, however, are potent inhibitors of attachment. The amino-terminal heparin-binding domain of thrombospondin does not promote attachment. Large fragments lacking the heparin-binding domain support attachment but not spreading of G361 cells. Attachment activity is lost following removal of the 18-kD carboxyl-terminal domain. These results suggest that at least two melanoma ligands are involved in cell attachment and spreading on thrombospondin. The carboxyl-terminal region and perhaps other regions of the molecule bind to receptor(s) on the melanoma surface that promote initial attachment but not cell spreading. Interaction of the heparin-binding domain with sulfated glycoconjugates on melanoma surface proteoglycans and/or sulfated glycolipids mediates spreading. Monoclonal antibodies A2.5 and C6.7 also reverse spreading of G361 cells growing on glass culture substrates, suggesting that binding to thrombospondin mediates attachment of these melanoma cells in culture.

Evidence that binding to the carboxyl-terminal heparin-binding domain (Hep II) dominates the interaction between plasma fibronectin and heparin

Biochemistry ◽  
1988 ◽  
Vol 27 (19) ◽  
pp. 7565-7571 ◽  
Author(s):  
Michael J. Benecky ◽  
Carl G. Kolvenbach ◽  
David L. Amrani ◽  
Michael W. Mosesson
Keyword(s):  
Binding Domain ◽  
Heparin Binding ◽  
Plasma Fibronectin ◽  
Heparin Binding Domain ◽  
Carboxyl Terminal

Bacillus Calmette-Guérin Interacts with the Carboxyl-Terminal Heparin Binding Domain of Fibronectin: Implications for BCG-Mediated Antitumor Activity

1994 ◽  
Vol 152 (4) ◽  
pp. 1275-1280 ◽  
Author(s):  
David Li-Wei Cheng ◽  
Wei-Ping Shu ◽  
Jimmy C.S. Choi ◽  
Eric J. Margolis ◽  
Michael J. Droller ◽  
...  
Keyword(s):  
Antitumor Activity ◽  
Binding Domain ◽  
Heparin Binding ◽  
Bacillus Calmette Guerin ◽  
Heparin Binding Domain ◽  
Carboxyl Terminal

Overlap of IGF- and heparin-binding sites in rat IGF-binding protein-5

2000 ◽  
Vol 24 (1) ◽  
pp. 43-51 ◽  
Author(s):  
H Song ◽  
J Beattie ◽  
IW Campbell ◽  
GJ Allan
Keyword(s):  
Binding Site ◽  
Conformational Changes ◽  
Binding Protein ◽  
Binding Activity ◽  
Binding Domain ◽  
Site Directed Mutagenesis ◽  
Heparin Binding ◽  
Igf I ◽  
Heparin Binding Domain ◽  
Igf Binding

Using site-directed mutagenesis, we have undertaken a study of a potential IGF-binding site in the C-terminal domain of rat IGFBP-5, lying close to or within a previously described heparin-binding domain (residues 201-218) in this protein. After analysis of binding activity using three different methods - ligand blotting, solution phase equilibrium binding and biosensor measurement of real-time on- and off-rates - we report that the mutation of two highly conserved residues within this region (glycine 203 and glutamine 209) reduces the affinity of the binding protein for both IGF-I and IGF-II, while having no effect on heparin binding. In addition, we confirm that mutation of basic residues within the heparin-binding domain (R201L, K202E, K206Q and R214A) results in a protein that has attenuated heparin binding but shows only a small reduction in affinity for IGF-I and -II. Previous findings have described the reduction in affinity of IGFBP-5 for IGFs that occurs after complexation of the binding protein with heparin or other components of the extracellular matrix (ECM) and have postulated that such an interaction may result in conformational changes in protein structure, affecting subsequent IGF interaction. Our data suggesting potential overlap of heparin- and IGF-binding domains argue for a more direct effect of ECM modulation of the affinity of IGFBP-5 for ligand by partial occlusion of the IGF-binding site after interaction with ECM.

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