Abstract
A peptide fraction of low molecular weight (Vueffe) prepared from porcine Factor VIII by enzymatic hydrolysis with trypsin, reduces bleeding time in laboratory animals without interfering either with platelets or blood coagulation1. For its molecular weight and pharmacological properties this fraction is completely different from other larger peptide fractions also derived from Factor VIII2. Remarkable properties of Vueffe are the low doses at which it is active, the long duration of action and the resistance to oral administration. The effect of Vueffe appears to be promising for controlling blood effusions in important areas such as the eye3,4.
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Gervasi, G.B., Bartoli, C., Carpita, G., Baldacci, M. Decrease of bleeding time by a peptide fraction from bovine factor VIII in laboratory animals. Arzneim-Forsch/Drug Res. 1988; 38: 1268–1270.
Weiss, H.J., Phillips, L.L., Rosner, W. Separation of sub-units of antihemophilic factor (AHF) by agarose gel chromatography. Thromb Diath Haemorrh. 1972; 27: 212–219.
Valli, A., Bellone, A., Protti, R., Bolla, N. Colour Doppler imaging to evaluate the action of a drug in ocular pathology. Ophthalmologica. 1995; 209: 117–122.
Cardillo Piccolino, F., Ghiglione, D., Ceppa, P. Villaggio, B., Carli, F., Allegri, P., Bertagno, R., Zingirian, M. Fundus angiography with fluorescein-labelled peptide fraction from bovine factor VIII: correlation with histologic findings. Eur J Ophthalmol. 1992; 2: 135–143.
Inoue, M., Kishimoto, A., Takai, Y., Nishizumka, Y. Studies on a cyclic nucleotide-independent protein kinase and its proenzyme in mammalian tissues. II. Proenzyme and its activation by calcium dependent protease from rat brain. J Biol Chem. 1977; 252: 7610–7616.
Newton, A.C. Protein kinase C: structure, function and regulation. J Biol Chem. 1995; 270: 28495–28498.
Jaken, S. Protein kinase C isoenzymes and substrates. Curr Opinion Cell Biol. 1996; 8: 168–173.
Hachiya, H.L., Takayama, S., White, M.F., King, G.L. Regulation of insulin receptor internalization in vascular endothelial cells by insulin and phorbol ester. J Biol Chem. 1987; 262: 6417–6424.
Jiang, M.J., Morgan, K.G. Intracellular calcium levels in phorbol ester-induced contractions of vascular muscle. Am J Physiol. 1987; 253: H1365–H1371.
Limas, C.J., Limas, C. Phorbol ester-and diacylglycerol-mediated desensitization of cardiac ß-adrenergic receptors. Cire Res. 1985; 57: 443–449.
Lynch, J.J., Ferro, T.J., Blumenstock, F.A., Brockenauer, A.M., Malik, A.B. Increased endothelial albumin permeability mediated by protein kinase C activation. J Clin Invest. 1990; 85: 1991–1998.
Lee, T.S., MacGregor, L.C., Fluharty, S.J., King, G.L. Differential regulation of protein kinase C and (Na,K)-adenosine triphosphatase activities by elevated glucose levels in retinal capillary endothelial cells. J. Clin. Invest. 1989; 83: 90–94.
Witte, S. Surface phenomena of coagulation factors “in vivo”, observed by fluorescence intravital microscopy. Ann NY Acad Sci. 1983; 416: 426–440.
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© 1998 Springer Science+Business Media Dordrecht
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Pazzagli, L., Cecchi, C., Bertini, M., Gervasi, G.B. (1998). Decrease of PKC activity by a peptide fraction from porcine factor VIII in endothelial cells CPA-47. In: Coscas, G., Piccolino, F.C. (eds) Retinal Pigment Epithelium and Macular Diseases. Documenta Ophthalmologica Proceedings Series, vol 62. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-5137-5_74
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DOI: https://doi.org/10.1007/978-94-011-5137-5_74
Publisher Name: Springer, Dordrecht
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