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Last Updated: 3 years ago

Possible Interaction: Heparin and Polypeptides

drug:

Heparin

supplement:

Polypeptides

Research Papers that Mention the Interaction

The polypeptide required interaction with heparin for activity, demonstrating the importance of heparin for FGFR activation even with designed ligands structurally unrelated to FGF.
Nature Biotechnology  •  1999  |  View Paper
It is concluded that the sulfatase activity in some types of breast cancer cell can be inhibited by heparin combined with the polypeptides Decapeptyl or TGF-alpha.
The Journal of steroid biochemistry and molecular biology  •  1995  |  View Paper
It has been shown that dextran sulfate, heparin , denatured DNA and poly I inhibited the binding of autoantibodies with some polypeptides.
Biulleten' eksperimental'noi biologii i meditsiny  •  1990  |  View Paper
Heparin interacts structurally with ECGF [Maciag, T., Mehlman, T., Friesel, R. & Schreiber, A. B. (1984) Science 225, 932-935], potentiates the mitogenic activity of the polypeptide , restores the biological activity to inactivate ECGF, enhances the affinity of the ligand to cell surface receptors, and modifies antibody recognition of ECGF.
Proceedings of the National Academy of Sciences of the United States of America  •  1985  |  View Paper
The phosphorylation of both the 55-kDa polypeptide and exogenously added casein was inhibited with GTP, heparin , and 2,3-bisphosphoglycerate in a dose-dependent manner, indicating the involvement of a CK2-like protein kinase.
Experimental parasitology  •  2002  |  View Paper
Heparin (10 U/ml) and dextran sulfate (100 mg/ml) inhibited the contractile effect of cationic polypeptides but did not affect contractions to phorbol 12,13-dibutyrate.
Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism  •  1997  |  View Paper
These results suggest that heparin , via its antiproliferative rather than anticoagulant effect, can inhibit mesangial cell proliferation, overexpression of polypeptide growth factors, and ECM protein overproduction in vivo.
Kidney international  •  1993  |  View Paper
Mutant NCAM polypeptides purified from transfected cell lines have substantially reduced binding to heparin and fail to promote chick retinal cell attachment.
Cell regulation  •  1990  |  View Paper
Heparan and keratan sulfates failed to activate tyrosine hydroxylase in place of heparin; several fractions of the bulk heparin (constituting 5 and 15%) had enriched tyrosine hydroxylase‐activating potency; and two lysine copolypeptides (polylysyltyrosine and polylysylphenylalanine) inhibited the activation of tyrosine hydroxylase by heparin.
Journal of neurochemistry  •  1980  |  View Paper
The basic L-lysine polypeptides prolonged whole blood clotting time, increased prothrombin time and neutralized the effect of heparin.
Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine  •  1953  |  View Paper
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