Lysophosphatidic acid (LPA) and sphingosine 1-phosphate (S1P) are both low-molecular-weight lysophospholipid (LPL) ligands which are recognized by the Edg family of G protein-coupled receptors (GPCRs). In endothelial cells, these two ligands activate Edg receptors resulting in cell proliferation and
Interleukin-1 increases tumor cell adhesion to endothelial cells through an RGD dependent mechanism:in vitroandin vivostudies
โ Scribed by Davide Lauri; Maria-Cruz Bertomeu; F. William Orr; Eva Bastida; D. Sauder; Michael R. Buchanan
- Book ID
- 104646598
- Publisher
- Springer
- Year
- 1990
- Tongue
- English
- Weight
- 362 KB
- Volume
- 8
- Category
- Article
- ISSN
- 0262-0898
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โฆ Synopsis
The effects of human recombinant interleukin-1 ~t and fl (rIL-1 ~t; rIL-1 fl) on the adhesion of human A549 lung carcinoma cells and M6 melanoma cells (TC) to human endothelial cells (HECs) in vitro were studied, and on TC/lung entrapment in vivo. In vitro, there was a significant increase in TC/HEC adhesion to HECs pretreated for 4 h with rIL-1 ~t or rIL-1 ft. The effects of rI L-1 ~t and fl on TC/HEC adhesion were time dependent and reached a plateau within 4-6 h. TC/HEC adhesion was not blocked when measured in the presence of antibodies to either fibronectin, glycoprotein IIb/IIIa, anti-ICAM, or anti-LFA. However, enhanced TC/HEC adhesion was completely blocked in the presence of the peptide, GRGDS. In vivo, pretreatment of nude mice for 4 h with rIL-1 ~t (given i.p. before i.v. injection of TCs) enhanced TC retention in the lung 24 h later. Our data demonstrate that IL-1 enhances TC adhesion to the vascular surface both in vitro and in vivo, suggesting that IL-1 can facilitate the metastatic process.
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