Synergistic actions of a thrombin-derived synthetic peptide and a thrombin receptor-activating peptide in stimulating fibroblast mitogenesis

Journal of Cellular Physiology
M D HollenbergJ DiMaio

Abstract

We measured the ability of the thrombin receptor activating peptide, SFLLR-NH2 (P5A) to stimulate 3H-thymidine incorporation in hamster CCL-39 fibroblasts either alone or in combination with the thrombin-derived polypeptides, YPPWNKNFTENDLL (TDP-1) and AGYKPDEGKRGDACEGDSGGPFV (TDP-2). In the presence (but not absence) of the amino peptidase inhibitor amastatin (10 microM), P5A alone (7.5 to 100 microM) caused a 1.5- to 2-fold stimulation of thymidine incorporation above basal, even though this inhibitor did not abrogate the degradation of P5A by other peptidases present in the assay medium. Neither TDP-1 nor TDP-2 alone had any effect on thymidine incorporation. However, TDP-1 (30 to 90 microM) considerably augmented P5A-mediated thymidine incorporation at low P5A concentrations (7.5 to 30 microM), shifting the P5A concentration-effect curve to the left. TDP-2 was inactive in this regard. The EC50 for this potentiating action of TDP-1 was approximately 40 microM. Further, thrombin, rendered proteolytically inactive by a low-molecular-weight bifunctional inhibitor, hirutonin-6, also acted synergistically with P5A to stimulate CCL-39 cell thymidine incorporation. We hypothesize that thrombin can cause its cellular effects, such a...Continue Reading

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Citations

Sep 24, 2002·Pharmacology & Therapeutics·Rommel S LanPeter J Henry
Jun 5, 2007·Neurobiology of Learning and Memory·Antoine G AlmonteStephen F Traynelis
Sep 13, 2005·American Journal of Physiology. Lung Cellular and Molecular Physiology·James K BrownCary A Jones
Dec 31, 2002·American Journal of Physiology. Cell Physiology·Michelle L SeymourWallace K MacNaughton
Jul 11, 2006·Blood·Maureane HoffmanDougald M Monroe

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