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TP508 inhibits cell attachment to extra cellular matrix proteins
Author(s) -
Morin Kimberly M,
Sheller Michael
Publication year - 2006
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.20.5.lb57-a
Subject(s) - fibrinogen , integrin , chemistry , cell adhesion , fibroblast , dermal fibroblast , umbilical vein , peptide , rgd motif , adhesion , microbiology and biotechnology , cell , thrombin , biophysics , biochemistry , in vitro , platelet , immunology , biology , organic chemistry
TP508, a portion of human thrombin, is a 23 amino acid peptide chain containing an internal RGD sequence. Peptides containing an RGD motif can inhibit cell attachment to fibrinogen and collagen by blocking the integrin recognition site. A cellular impedance measuring system (ECIS system, Applied Biophysics) was used to determine the effect of TP508 on cell adhesion to fibrinogen and collagen. Normal human dermal fibroblasts (NHDF), Chinese hamster lung fibroblast V79‐4 and Human umbilical vein endothelial cells (HUVEC) were mixed with TP508 at dosages of 1, 10, 100, and 230 ug/ml and inoculated on protein coated wells containing an array of gold electrodes. The resistance was measured over 24 hrs and the percent binding analyzed. A significant decrease in cell adhesion was measured in NHDF binding to fibrinogen at doses of 100 and 230 ug/ml of TP508 compared to a 0 ug/ml TP508 control. Hence, the RGD sequence in TP508 may interact with integrins to inhibit the attachment of NHDF to fibrinogen.