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Last Updated: 2 years ago

Possible Interaction: Tyrosine and Sphingosine 1-Phosphate

supplement:

Tyrosine

Research Papers that Mention the Interaction

The study also indicated that these changes … mediated through leptin signal transduction as S1P injection resulted in a …-dependent increase in tyrosine phosphorylation of both Janus kinase 2 (Jak2) and signal transducer and activator of transcription 3 (STAT3), signalling of which controls anorexigenic and thermogenic signalling in the hypothalamus.
Aging  •  2017  |  View Paper
S1P induced the recruitment of over 20 cell … raft proteins exhibiting increasing levels of tyrosine phosphorylation including known barrier-regulatory proteins such as focal adhesion kinase (FAK), cortactin, p85alpha phosphatidylinositol 3-kinase (p85alphaPI3K), myosin light chain kinase (nmMLCK), filamin A/C, and the non-receptor tyrosine kinase, c-Abl.
These results suggest that S1P induces both the tyrosine phosphorylation and recruitment of key actin cytoskeletal proteins to membrane rafts, resulting in enhanced human EC barrier function.
Cellular signalling  •  2009  |  View Paper
S1P also induces a rapid increase in cortactin tyrosine phosphorylation (within 30 s) critical to subsequent barrier enhancement, since EC transfected with a tyrosine-deficient mutant cortactin exhibit a blunted TER response.
Journal of Biological Chemistry  •  2004  |  View Paper
Sph-1-P stimulated tyrosine phosphorylation of Cas, which was inhibited by the G(i) inactivator pertussis toxin but not by the Rho inactivator C3 exoenzyme or the Rho kinase inhibitor Y-27632.
The Journal of biological chemistry  •  2001  |  View Paper
Sph-1-P induced FAK tyrosine phosphorylation, myosin light chain phosphorylation, and the formation of stress fibers in HUVECs.
Journal of biochemistry  •  2000  |  View Paper
S1P induces a rapid increase in tyrosine phosphorylation of p125(FAK).
Biochemical and biophysical research communications  •  2000  |  View Paper
SPP rapidly increased tyrosine phosphorylation of FAK and paxillin and of the paxillin-associated protein Crk.
Experimental cell research  •  1999  |  View Paper
We now report that S1P treatment of bovine aortic endothelial cells acutely increases the tyrosine phosphorylation of Flk-1/KDR, similar to VEGF treatment.
The Journal of Biological Chemistry  •  2002  |  View Paper
SPP was found to strongly induce tyrosine phosphorylation of Crk, but not Shc, in NIH-3T3 parental, insulin-like growth factor-I receptor-overexpressing and Crk-overexpressing (3T3-Crk) fibroblasts.
The Journal of Biological Chemistry  •  1997  |  View Paper