Urogastrone–epidermal growth factor concentrations in prostatic fluid of normal individuals and patients with benign prostatic hypertrophy

1986 ◽  
Vol 70 (4) ◽  
pp. 359-363 ◽  
Author(s):  
H. Gregory ◽  
I. R. Willshire ◽  
J. P. Kavanagh ◽  
N. J. Blacklock ◽  
S. Chowdury ◽  
...  

1. High concentrations (272 ± 33 ng/ml) of urogastrone-epidermal growth factor were measured in prostatic fluid from normal males by a specific radioimmunoassay. 2. Significantly lower concentrations (155 ± 24 ng/ml) were observed in the prostatic fluid of patients with benign prostatic hypertrophy than in the age-matched normal controls (2P < 0.01). 3. The growth factor content of seminal fluid was accounted for by the contribution of prostatic fluid. 4. Immunochemical studies failed to show evidence of synthesis within the gland nor could high affinity receptors for the protein be demonstrated in membrane preparations of the gland.

1987 ◽  
Vol 112 (1) ◽  
pp. 87-96 ◽  
Author(s):  
J. M. M. Harper ◽  
J. B. Soar ◽  
P. J. Buttery

ABSTRACT Methods for the primary culture of muscle cells from fetal sheep were developed which gave high yields of cells. Myoblasts were grown in vitro, and allowed to fuse to form contractile multinucleate myotubes; these could be maintained in a good condition for at least 2 weeks. Protein turnover in these differentiated cultures was examined for sensitivity to each of four potentially anabolic peptide hormones and growth factors: insulin, insulin-like growth factor I (somatomedin C), epidermal growth factor and growth hormone. Insulin was found to have no effect except at high concentrations (1 μmol/l), compatible with its role as a somatomedin analogue. Insulin-like growth factor I was active at lower levels (1 nmol/l) but the cultures were not as responsive to it as were primary rat muscle cultures or differentiated L6 cells, which were tested in similar experiments. The maximum stimulation of protein synthesis observed with the ruminant system was only 16%. Epidermal growth factor was highly anabolic for primary cultures from sheep muscle, and the cells were very sensitive to it, half-maximal stimulation of protein synthesis being seen with concentrations as low as 20 pmol/l. No effects of bovine growth hormone were seen in the ovine system. However, an inhibition of protein breakdown was found with high concentrations (0·1 μmol/l) in the L6 rat myoblast cell line. It was found that the culture conditions used could affect the observed responses of protein synthesis and degradation, despite withdrawal of serum from the incubation media 22 h before testing. J. Endocr. (1987) 112, 87–96


The Prostate ◽  
1997 ◽  
Vol 32 (4) ◽  
pp. 234-240 ◽  
Author(s):  
Peter H. Gann ◽  
Robert Chatterton ◽  
Kirsten Vogelsong ◽  
John T. Grayhack ◽  
Chung Lee

1983 ◽  
Vol 96 (3) ◽  
pp. 489-497 ◽  
Author(s):  
D. J. Hill ◽  
A. T. Holder ◽  
J. Seid ◽  
M. A. Preece ◽  
S. Tomlinson ◽  
...  

The incorporation of [3H]thymidine by rat costal cartilage in vitro was studied at different fetal and postnatal ages and the effect of partially purified human somatomedin, mouse epidermal growth factor, platelet secretion products, insulin and growth hormone on thymidine uptake by fetal cartilage was examined. Thymidine uptake in plasma-free medium was many times greater in late fetal life than after birth. The incorporation of [3H]thymidine into costal cartilage from 21-day fetuses was significantly (P <0·05) increased above control values in the presence of 10 μg somatomedin/l, and when cartilage was incubated in medium containing somatomedin and diluted human plasma there was a synergistic action. Epidermal growth factor at a concentration of 1 ng/l was a potent stimulator of thymidine uptake. Secretion products from human platelets after their aggregation by thrombin stimulated [3H]thymidine uptake at a concentration of 2% (v/v), but were inhibitory at high concentrations. High concentrations of platelet secretion products stimulated the incorporation of [35S]sulphate by cartilage. A pharmacological concentration of 10 mu. insulin/ml stimulated [3H]thymidine uptake, but not concentrations of 1 or 100 mu./ml. Growth hormone had no effect. The results showed that fetal cartilage had a greater endogenous mitogenic activity than postnatal cartilage. While somatomedins may be important in the regulation of fetal body growth, other protein growth factors also stimulate fetal skeletal tissues.


1983 ◽  
Vol 96 (2) ◽  
pp. 287-292 ◽  
Author(s):  
J. M. Beardmore ◽  
R. C. Richards

A radioimmunoassay was used to measure the concentration of epidermal growth factor (EGF) in mouse milk throughout lactation. The EGF content of mouse milk increased steadily from birth to a concentration of 427 μg/l at day 8 of lactation. These high levels were maintained until the approach of weaning, when values decreased from day 17 to 130 μg/l at day 22. Milk samples chromatographed on a Biogel P10 column gave a major peak of immunoreactivity at the point at which pure standard EGF was eluted. The origin of milk EGF is unknown, but the high concentrations of this peptide identified in mouse milk suggest that it must play a role in the neonate.


2001 ◽  
Vol 120 (5) ◽  
pp. A11-A12 ◽  
Author(s):  
A SINHA ◽  
J NIGHTINGALE ◽  
K WEST ◽  
R PLAYFORD

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