GROWTH RETARDATION: USE OF SULFATION FACTOR AS A BIOASSAY FOR GROWTH HORMONE

PEDIATRICS ◽  
1963 ◽  
Vol 31 (4) ◽  
pp. 538-551
Author(s):  
Maurice D. Kogut ◽  
S. A. Kaplan ◽  
C. S. N. Shimizu

A bioassay for measurement of human growth hormone based upon the observation that normal human serum, in vitro, will favor the incorporation of S-35 into immature rat cartilage is described. The factor in serum is called "sulfation factor." Sulfation factor determinations were performed on 27 normal children, 15 with hypopituitarism, 26 dwarfs without demonstrable endocrine or other diseases, 11 children with a variety of non-pituitary diseases causing dwarfism, and 1 adult with acromegaly. The mean activity (± S. E.) of sulfation factor was 0.84 ± 0.057 S. F. units in the normal children, 0.45 ± 0.024 S. F. units in idiopathic hypopituitary patients (p < 0.01), 0.95 ± 0.054 S. F. units in dwarfs without evidence of endocrine or other recognizable diseases, 0.82 ± 0.057 S. F. units in dwarfs with well recognized nonpituitary disease, and 2.2 S. F. units in one adult with acromegaly. There was an excellent correlation between sulfation factor and other laboratory determinations of pituitary function. Hypophysectomized rats receiving bovine growth hormone showed substantial increase of sulfation factor as compared to control hypophysectomized rats. Sulfation factor activity appears to be a valid and useful indicator of growth hormone activity in serum.

1984 ◽  
Vol 247 (5) ◽  
pp. E639-E644
Author(s):  
C. M. Cameron ◽  
J. L. Kostyo ◽  
J. A. Rillema ◽  
S. E. Gennick

The biological activity profile of reduced and S-carboxymethylated human growth hormone (RCM-hGH) was determined to establish its suitability for study of the diabetogenic property of hGH. RCM-hGH was found to have greatly attenuated in vivo growth-promoting activity in the 9-day weight-gain test in hypophysectomized rats (approximately 1%) and to have a similar low order of in vitro activity in stimulating amino acid incorporation into the protein of the isolated rat diaphragm. RCM-hGH also only had approximately 1% of the in vitro insulin-like activity of the native hormone on isolated adipose tissue from hypophysectomized rats. In contrast, RCM-hGH retained substantial in vivo diabetogenic activity in the ob/ob mouse, appearing to have approximately 50% of the activity of the native hormone. RCM-hGH was also found to retain significant, although attenuated (25%), in vitro lactogenic activity when tested for the ability to stimulate amino acid incorporation into a casein-rich protein fraction in mouse mammary gland explants. Because RCM-hGH exhibits a high degree of diabetogenic activity, although lacking significant anabolic or insulin-like activities, it will be useful as a "monovalent" probe for the study of the molecular mechanism of the diabetogenic action of GH.


1981 ◽  
Vol 98 (1) ◽  
pp. 24-28 ◽  
Author(s):  
R. M. Schimpff ◽  
M. Donnadieu ◽  
M. Gautier ◽  
G. Polini ◽  
A. M. Repellin

Abstract. Normal human explants from liver and from connective tissues (aponeurosis or skin) incubated in vitro released sulphation activity measurable in chick embryo cartilage. Addition of human Growth Hormone (hGH) at physiological levels (10 ng/ml) increased the sulphation activity after 6 hours incubation time. Higher doses failed to increase the sulphation activity produced by connective tissues and decreased the sulphation activity produced by the liver.


1960 ◽  
Vol 38 (1) ◽  
pp. 1069-1075
Author(s):  
O. J. Lucis ◽  
E. H. Venning

Porcine, monkey, and human growth hormone have no effect on the in vitro secretion of aldosterone by the rat adrenal gland. When monkey growth hormone is injected into hypophysectomized rats, the adrenals of these animals secrete, under in vitro conditions, increased amounts of aldosterone with no change in the secretion rate of corticosterone. The plasma of these rats contains a substance which appears to stimulate the secretion of aldosterone in the adrenals of normal rats.


1989 ◽  
Vol 120 (6) ◽  
pp. 745-752 ◽  
Author(s):  
R. M. Schimpff ◽  
A. M. Repellin

Abstract. Cultures of human blood peripheral lymphocytes were performed in the presence or absence of human growth hormone, and also of phytohemagglutinin and normal human serum 10%. After incubation for 48 h, the supernatants were tested for their ability to promote the uptake of [3H]thymidine into lectin-activated lymphocytes. Supernatants from lymphocyte-free control samples, treated in the same manner, were assayed under the same experimental conditions. Variance analysis of the different dose-response relationships was performed. The results of these in vitro experiments confirm that physiological levels of GH inhibit the lectin-induced lymphoproliferation and that lymphocytes secrete an 'activity' able to stimulate the incorporation of [3H]thymidine into lectin activated lymphocytes. Furthermore we show that: 1) Secretion of this lymphocyte-stimulating activity is increased by physiological levels of GH; 2) This lymphocytic secretion is not radioimmunoassayable IGF-I; 3) Using fast protein liquid chromatography (FPLC), this activity appears in fractions with various molecular weights.


1960 ◽  
Vol 38 (10) ◽  
pp. 1069-1075 ◽  
Author(s):  
O. J. Lucis ◽  
E. H. Venning

Porcine, monkey, and human growth hormone have no effect on the in vitro secretion of aldosterone by the rat adrenal gland. When monkey growth hormone is injected into hypophysectomized rats, the adrenals of these animals secrete, under in vitro conditions, increased amounts of aldosterone with no change in the secretion rate of corticosterone. The plasma of these rats contains a substance which appears to stimulate the secretion of aldosterone in the adrenals of normal rats.


1977 ◽  
Vol 74 (2) ◽  
pp. 205-212 ◽  
Author(s):  
I. K. ASHTON ◽  
M. J. O. FRANCIS

The incorporation of [3H]thymidine by rabbit chondrocytes in vitro has been developed as a sensitive assay for plasma somatomedin. A concentration of normal plasma of 2·5% enhanced [3H]thymidine incorporation by 5- to 20-fold compared with basal levels in the absence of plasma. The mean potency of plasma from normal adult men was 0·96 ± 0·1 u./ml (mean ± s.d.) and from acromegalic patients 1·9 ± 0·4 u./ml. The apparent potency of hypopituitary plasma alone increased on heating which suggested the presence of heatlabile inhibitors of somatomedin activity. The potency of heated hypopituitary plasma (0·6 ± 0·09 u./ml) remained significantly lower (P < 0·01) than normal plasma. Human growth hormone (0·1–20 μu./ml), bovine growth hormone (0·5–20 μu./ml), insulin (0·5–5 μu./ml) and glucose (0·3–2 mmol/l) had no direct effect on the incorporation of [3H]thymidine. Chondrocytes which had been previously stored frozen also showed a response to plasma somatomedin.


1978 ◽  
Vol 87 (3) ◽  
pp. 485-494 ◽  
Author(s):  
Kazue Takano ◽  
Naomi Hizuka ◽  
Koichi Kawai ◽  
Kazuo Shizume

ABSTRACT Somatomedin A was determined by radioreceptor assay of serum from rats with various conditions. The mean value of somatomedin A in 28 day old male rats was 6.2 ± 0.44 U/ml. Following hypophysectomy, serum somatomedin A decreased with a half-life of approximately 6 h. After a single ip injection of human growth hormone into hypophysectomized rats, the levels of somatomedin A increased within 4 h and reached the maximal level between 8 and 24 h. There was a dose-dependent increase of somatomedin A at 24 h after injection of hGH when the injected dose was between 3.2 and 80 μg. Serum somatomedin A was significantly decreased after 24 h of fasting to the same levels as after hypophysectomy. However the changes in serum rGH between fasting rats and fed rats did not show any significant differences. After different intakes of diets with different composition for 32 days, the mean levels of serum somatomedin A were 14.5 ± 2.2, 6.22 ± 0.4, 2.5 ± 0.3 and 13.0 ± 1.1 U/ml when control-, high protein-, high carbohydrate-low protein- and high fat diets were given respectively. There was a positive correlation between the per cent increase in weight and the serum level of somatomedin A. These results indicate that not only growth hormone but also adequate food intake is required for the generation of somatomedin.


1961 ◽  
Vol 37 (2) ◽  
pp. 176-182 ◽  
Author(s):  
Elliott J. Collins ◽  
Vernon F. Baker

ABSTRACT The characteristics and nature of the effect of growth hormone on the incorporation of radio-sulfate into the costal cartilage of hypophysectomized rats has been studied. The time-response studies indicate that a reliable estimation of growth hormone activity can be ascertained within a 24 hour period, and a reproducible dose-related response can be obtained at dosage levels ranging from 12-48 μg. Growth hormone stimulates the synthesis of organic sulfates and accumulation of inorganic sulfates within 48 hours.


1967 ◽  
Vol 54 (4) ◽  
pp. 645-662 ◽  
Author(s):  
Å. Hjalmarson ◽  
K. Ahrén

ABSTRACT The effect of growth hormone (GH) in vitro on the rate of intracellular accumulation of the non-utilizable amino acid α-aminoisobutyric acid (AIB) was studied in the intact rat diaphragm preparation. Bovine or ovine GH (25 μg/ml incubation medium) markedly stimulated the accumulation of AIB-14C by diaphragms from hypophysectomized rats, while there was no or only a very slight effect on diaphragms from normal rats. In diaphragms from rats with the pituitary gland autotransplanted to the kidney capsule GH in vitro stimulated the accumulation of AIB-14C significantly more than in diaphragms from normal rats but significantly less than in diaphragms from hypophysectomized rats. Injections of GH intramuscularly for 4 days to hypophysectomized rats made the diaphragms from these rats less sensitive or completely insensitive to GH in vitro. These results indicate strongly that the relative insensitivity to GH in vitro of diaphragms from normal rats is due to the fact that the muscle tissues from these rats has been exposed to the endogenously secreted GH. The results show that GH can influence the accumulation of AIB-14C in the isolated rat diaphragm in two different ways giving an acute or »stimulatory« effect and a late or »inhibitory« effect, and that it seems to be a time-relationship between these two effects of the hormone.


1965 ◽  
Vol 49 (1) ◽  
pp. 1-16 ◽  
Author(s):  
M. Apostolakis

ABSTRACT A method for the extraction of prolactin from human pituitary glands is described. It is based on acetone drying, distilled water extraction, acetone and isoelectric precipitation. Two main products are obtained: Fraction R8 with a mean prolactin activity of 12.2 IU/mg and fraction U8 with a mean prolactin activity of 8.6 IU/mg. The former fraction does not contain any significant gonadotrophin activity and the latter contains on an average 50 HMG U/mg. In both cases contamination with ACTH and MSH is minimal. The growth hormone activity of both these fractions is low. It is postulated that in man too, prolactin and growth hormone are two distinct hormones. A total of 1250 human pituitary glands have been processed by this method. The mean prolactin content per pituitary gland has been found to be 73 IU.


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