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Gene Review

PF4  -  platelet factor 4 (chemokine (C-X-C motif)...

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Disease relevance of PF4

  • GAGs which can neutralize PF4 and which can also have specific anti-factor Xa activity could represent a great advantage in thrombosis prophylaxis [1].

High impact information on PF4

  • The effects of PF-4 were antagonized by heparin [2].
  • PF-4 inhibited DNA synthesis, as well as proliferation of endothelial cells derived from large and small blood vessels [2].
  • Inhibition of cell growth by PF-4 was reversible [2].
  • In cells synchronized in S phase by hydroxyurea and then released, addition of PF-4 promptly blocked further progression of DNA synthesis [2].
  • The addition of c7E3 Fab also significantly prolonged the ACTs of blood anticoagulated with the direct thrombin inhibitors hirudin and D-phenylalanyl-L-prolyl-L-arginyl chloromethyl ketone, indicating that the effect of c7E3 Fab was not exclusively related to decreased release of PF4, a heparin-neutralizing factor, from platelets [3].

Biological context of PF4


Anatomical context of PF4

  • When PF4 was added to the medium of cells, attachment on either substratum was unaffected as was neurite outgrowth on pFN, revealing differences in PF4's inhibition as the substratum-bound or medium-borne component [6].
  • We utilized platelet factor 4 (PF4) conjugated to fluorescein to stain the proteoglycans of permeabilized fixed bovine aorta endothelial cells in monolayer culture [7].
  • CONCLUSIONS: This study confirms the high frequency of heparin-PF4 antibodies after coronary artery bypass grafting and demonstrates a significantly higher incidence after bovine heparin [4].
  • From activated human leukocyte culture supernatants, we have isolated a form of PF-4 that acts as a potent inhibitor of endothelial cell proliferation [8].
  • Involvement of hepatocyte nuclear factor-4 in the expression of the growth hormone receptor 1A messenger ribonucleic acid in bovine liver [9].

Associations of PF4 with chemical compounds

  • These differences should significantly affect the secondary structure and heparin-binding properties of the protein based on considerations of the bovine PF4 crystal structure [10].
  • Aggregation and release of 14C-serotonin and PF4 were inhibited by the metabolic inhibitors 2-deoxyglucose (16.7 mM) and antimycin-A (8.3 micrograms/ml), by the membrane-active drugs mepacrine (10 microM) and chlorpromazine (0.025 mM), by PGI2 (5.34 nM), which elevates intracellular c-AMP, by indomethacin (10 microM) or aspirin (100 microM) [11].
  • In vitro, PF4 is comparable to protamine sulfate in the neutralization of heparin, but the complexes formed with heparin are different [12].
  • The content of PF4 determined by radioimmunoassay was 22.6 (+/- 1.6 S.D.) micrograms per 10(9) platelets and 46.8 (+/- 19.6 S.D.) ng per ml platelet poor plasma collected in acid citrate dextrose in the presence of prostaglandin E1 [5].
  • The relative degree of both kallikrein activation and PF4 release was greater in the non-fixed tissue but a greater number of fibrin(ogen) molecules per cm2 was found on GA-treated tissue [13].

Other interactions of PF4

  • Immunohistochemically, staining for the octamer-binding transcription factor 4 (OCT4, also known as POU5F1), revealed a specific and exclusive staining of nuclei of the complete epiblast [14].


  1. Effects on platelets and on the clotting system of four glycosaminoglycans extracted from hog mucosa and one extracted from aortic intima of the calf. Cella, G., Scattolo, N., Luzzatto, G., Stevanato, F., Vio, C., Girolami, A. Journal of medicine. (1986) [Pubmed]
  2. Inhibition of endothelial cell proliferation by platelet factor-4 involves a unique action on S phase progression. Gupta, S.K., Singh, J.P. J. Cell Biol. (1994) [Pubmed]
  3. In vitro effects of the platelet glycoprotein IIb/IIIa receptor antagonist c7E3 Fab on the activated clotting time. Ammar, T., Scudder, L.E., Coller, B.S. Circulation (1997) [Pubmed]
  4. Comparison of bovine and porcine heparin in heparin antibody formation after cardiac surgery. Francis, J.L., Palmer, G.J., Moroose, R., Drexler, A. Ann. Thorac. Surg. (2003) [Pubmed]
  5. Ovine platelet factor 4: purification, amino acid sequence, radioimmunoassay and comparison with platelet factor 4 of other species. Shigeta, O., Lu, W.Q., Holt, J.C., Edmunds, L.H., Niewiarowski, S. Thromb. Res. (1991) [Pubmed]
  6. Ganglioside-dependent adhesion events of human neuroblastoma cells regulated by the RGDS-dependent fibronectin receptor and proteoglycans. Mugnai, G., Lewandowska, K., Choi, H.U., Rosenberg, L.C., Culp, L.A. Exp. Cell Res. (1988) [Pubmed]
  7. Glycosaminoglycans of bovine aorta endothelial cells: identification and localization by use of a platelet factor 4-fluorescein probe. Silbert, D.I., Gill, P.J., Humphries, D.E., Silbert, J.E., Culp, L.A., Silbert, C.K. J. Histochem. Cytochem. (1990) [Pubmed]
  8. A potent inhibitor of endothelial cell proliferation is generated by proteolytic cleavage of the chemokine platelet factor 4. Gupta, S.K., Hassel, T., Singh, J.P. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  9. Involvement of hepatocyte nuclear factor-4 in the expression of the growth hormone receptor 1A messenger ribonucleic acid in bovine liver. Jiang, H., Lucy, M.C. Mol. Endocrinol. (2001) [Pubmed]
  10. Identification and characterization of PF4varl, a human gene variant of platelet factor 4. Green, C.J., Charles, R.S., Edwards, B.F., Johnson, P.H. Mol. Cell. Biol. (1989) [Pubmed]
  11. Effect of platelet-activating factor (PAF) on human platelets. Chesney, C.M., Pifer, D.D., Byers, L.W., Muirhead, E.E. Blood (1982) [Pubmed]
  12. Influence of platelet factor 4 on the neutralization of heparin by protamine. Shanberge, J.N., Quattrociocchi-Longe, T.M. Ann. N. Y. Acad. Sci. (1989) [Pubmed]
  13. An in vitro bovine pericardial hemocompatibility testing system. Amrani, D.L., Lee, C., Earles, K., DiOrio, J., Murphy, M., Yang, J., Rubalcaba, S., LiVecchi, A. J. Heart Valve Dis. (1998) [Pubmed]
  14. Ultrastructural and immunohistochemical characterization of the bovine epiblast. Vejlsted, M., Avery, B., Schmidt, M., Greve, T., Alexopoulos, N., Maddox-Hyttel, P. Biol. Reprod. (2005) [Pubmed]
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