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Heparin‐binding growth factor isolated from human prostatic extracts
Author(s) -
Mydlo Jack H.,
Bulbul Muhammad A.,
Richon Victoria M.,
Heston Warren D. W.,
Fair William R.
Publication year - 1988
Publication title -
the prostate
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.295
H-Index - 123
eISSN - 1097-0045
pISSN - 0270-4137
DOI - 10.1002/pros.2990120408
Subject(s) - thymidine , fibroblast growth factor , cell culture , umbilical vein , basic fibroblast growth factor , growth factor , human umbilical vein endothelial cell , fibroblast , heparin , chorioallantoic membrane , biology , microbiology and biotechnology , endocrinology , biochemistry , dna , in vitro , genetics , receptor
Prostatic tissue extracts from patients with benign prostatic hyperplasia (BPH) and prostatic carcinoma were fractionated using heparin‐Sepharose chromatography. The mitogenic activity of eluted fractions on quiescent subconfluent Swiss Albino 3T3 fibroblasts was tested employing a tritiated‐thymidine‐incorporation assay. Two peaks of activity were consistently noted—one in the void volume and a second fraction which eluted with 1.3–1.6 M NaCl and contained the majority of the mitogenic activity. Both non‐heparin‐ and heparin‐binding fractions increased tritiated thymidine incorporation into a mouse osteoblast cell line (MC3T3), while only the heparin‐binding fractions stimulated a human umbilical vein endothelial cell line (HUV). No increased uptake of thymidine was seen using a human prostatic carcinoma cell line (PC‐3). Sodium dodecyl sulfate/polyacrylamide gel electrophoresis (SDS/PAGE) of lyophilized active fractions showed a persistent band at 17,500 daltons. The purified protein demonstrated angiogenic properties using the chick embryo chorioallantoic membrane (CAM) assay. Western blot analysis using antibodies specific to basic fibroblast growth factor (bFGF) or acidic FGF (aFGF) demonstrated that the former, but not the latter, bound to prostatic growth factor (PrGF), and inhibited its mitogenic activity as well. It appears that PrGF shares homology with basic fibroblast growth factors.