Abstract
Myofibroblasts (Mfs) from rat fat tissues produced a potent endothelial cell growth factor (Mf-ECGF). The growth factor activity found in the conditioned media from primary cultures of Mfs, was labile to heat (80°C for 10 min) and proteinase (trypsin), and did not bind to heparin in the presence of 0.2 M NaCl. Mf-ECGF was partially purified 4760-fold with a recovery of 25% from serum-free conditioned media by sequential carboxymethyl (CM) ion-exchange column chromatography and gel filtration. This Mf-ECGF activity was recovered from the 40 kD region of a non-reducing SDS-PAGE, and from the pH region between 6.5 and 7 of isoelectric focusing, with recoveries of 20% and 65%, respectively. These results indicated that a major portion of ECGF activity in the conditioned media was clearly distinct from other well-known endothelial cell growth factors including fibroblast growth factors (FGFs).
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© 1992 Birkhäuser Verlag Basel/Switzerland
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Sato, N., Tsuruoka, N., Yamamoto, M., Nishihara, T., Goto, T. (1992). Identification of non heparin-binding endothelial cell growth factor from rat myofibroblasts. In: Steiner, R., Weisz, P.B., Langer, R. (eds) Angiogenesis. Experientia Supplementum, vol 61. Birkhäuser, Basel. https://doi.org/10.1007/978-3-0348-7001-6_27
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DOI: https://doi.org/10.1007/978-3-0348-7001-6_27
Publisher Name: Birkhäuser, Basel
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