scholarly journals Metabolic effects of the major component of bovine growth hormone

1971 ◽  
Vol 122 (5) ◽  
pp. 633-640 ◽  
Author(s):  
N. I. Swislocki ◽  
M. Sonenberg ◽  
M. Kikutani
Keyword(s):  
Growth Hormone ◽  
Deae Cellulose ◽  
Heterogeneous Material ◽  
Parent Material ◽  
Metabolic Effects ◽  
Sedimentation Equilibrium ◽  
Bovine Growth Hormone ◽  
Hormone Effects

Bovine growth hormone, subjected to DEAE-cellulose chromatography, yielded one major and several minor components. The various chromatographic fractions of bovine growth hormone were compared with the parent material for their ability to promote hormone effects in vivo and in vitro. The major component of bovine growth hormone was homogeneous by acrylamide-gel electrophoresis, rechromatography and sedimentation equilibrium. Its amino acid composition was similar to that of the parent hormone. The major component possessed all the qualitative activities present in the original heterogeneous material, including promotion of acute hypoglycaemia and hypolipaemia. In studies in vitro in adipose-tissue segments the major component of the hormone increased entry of glucose and its oxidation to CO2, conversion of glucose into glyceride glycerol, release of glycerol and incorporation of histidine into adiposetissue protein. Other chromatographic fractions of bovine growth hormone were not homogeneous and possessed some but not all of the metabolic activities attributed to the hormone preparations or its major component. Thus, the metabolic effects obtained with bovine growth-hormone preparations in vivo and in vitro can be obtained with the major homogeneous component of the hormone. This observation precludes the possibility that the metabolic effects obtained with bovine growth-hormone preparations are due to the combined actions of a number of components found therein.

scholarly journals Sulfate Uptake and Somatomedin Levels in the 'Little' (lit/lit) Mouse

1981 ◽  
Vol 34 (2) ◽  
pp. 221 ◽  
Author(s):  
NeiI M McKern ◽  
Donald B Cheek ◽  
WGordon Crewther
Keyword(s):  
Growth Hormone ◽  
Costal Cartilage ◽  
Fresh Medium ◽  
Bovine Growth Hormone ◽  
Consistent Difference ◽  
Sulfate Uptake ◽  
Low Levels ◽  
In Vivo Uptake

The mutant 'little' (lit/lit) mouse is deficient in growth hormone and has correspondingly low levels of serum somatomedin. Injection of these mice with human or bovine growth hormone significantly r(l.ises serum somatomedin levels within 6 h. In vivo uptake of radioactive sulfate by costal cartilage in lit/lit mice is similar to that of normal mice, which is unexpected in view of the low levels of circulating somatomedin. If costal cartilages from normal and lit/lit mice are preincubated in medium 199 in vitro before transfer to fresh medium containing radioactive sulfate and serum, there is no consistent difference in uptake of sulfate, demonstrating similar endogenous cartilage activity. In contrast, omission of the preincubation step reveals a lower uptake of sulfate in vitro by cartilage from lit/lit mice as compared with normal mice. Cartilage removed from lit/lit mice 24 h after injection with growth hormone, however, takes up greater amounts of sulfate than cartilage from untreated normal mice.

Active transport of calcium by intestine: effects of hypophysectomy and growth hormone

1962 ◽  
Vol 203 (5) ◽  
pp. 873-880 ◽  
Author(s):  
James D. Finkelstein ◽  
David Schachter
Keyword(s):  
Growth Hormone ◽  
Active Transport ◽  
Electrical Potential ◽  
Potential Gradient ◽  
Initial Increase ◽  
Bovine Growth Hormone ◽  
Hypophysectomized Rats ◽  
Rat Duodenum

The effects of hypophysectomy on active transport of calcium in vitro by everted gut sacs of rat duodenum are 1) an initial increase 4–5 days postoperatively and 2) a marked decrease 2–3 weeks postoperatively. The defect in transport results from reduction in the unidirectional transfers of Ca toward the serosa, and both steps in the transport (mucosal uptake and transfer to serosal surface) are impaired. Hypophysectomy also decreases iron transport (duodenal gut sacs), decreases l-proline transfer less strikingly (ileal gut sacs), increases d-galactose transport (jejunal gut sacs), and does not appear to influence either the electrical potential gradient from mucosa to serosa or the net flux of sodium. Treatment of hypophysectomized rats with a preparation of bovine growth hormone restores transfer mechanisms for calcium and iron. Ovine prolactin is also active in restoring the Ca mechanism, whereas other pituitary and nonpituitary hormones are not. Cortisone, l-thyroxin, and estradiol decrease Ca transport further in hypophysectomized rats. Absorption of Ca from loops of rat duodenum in vivo is also decreased 2 weeks after hypophysectomy and can be increased by prior treatment with bovine growth hormone.

The interrelationships of thyroid and growth hormones: effect of growth hormone releasing hormone in hypo- and hyperthyroid male rats

1986 ◽  
Vol 113 (4_Suppl) ◽  
pp. S367-S375 ◽  
Author(s):  
Allen W. ROOT ◽  
Dorothy SHULMAN ◽  
Jennifer ROOT ◽  
Frank DIAMOND
Keyword(s):  
Growth Hormone ◽  
Thyroid Hormones ◽  
Secretory Response ◽  
Metabolic Effects ◽  
Male Rats ◽  
Male Rat ◽  
Peripheral Tissues ◽  
Releasing Hormone

ABSTRACT Growth hormone (GH) and the thyroid hormones interact in the hypothalamus, pituitary and peripheral tissues. Thyroid hormone exerts a permissive effect upon the anabolic and metabolic effects of GH, and increases pituitary synthesis of this protein hormone. GH depresses the secretion of thyrotropin and the thyroid hormones and increases the peripheral conversion of thyroxine to triiodothyronine. In the adult male rat experimental hypothyroidism produced by ingestion of propylthiouracil depresses the GH secretory response to GH-releasing hormone in vivo and in vitro, reflecting the lowered pituitary stores of GH in the hypothyroid state. Short term administration of large amounts of thyroxine with induction of the hyperthyroid state does not affect the in vivo GH secretory response to GH-releasing hormone in this animal.

ANALYSIS OF THE BIPHASIC ACTION OF GROWTH HORMONE IN VITRO ON THE RAT DIAPHRAGM

1968 ◽  
Vol 57 (3_Suppl) ◽  
pp. S19-S35 ◽  
Author(s):  
Å. Hjalmarson
Keyword(s):  
Growth Hormone ◽  
Actinomycin D ◽  
Accumulation Rate ◽  
Inhibitory Effect ◽  
Bovine Growth Hormone ◽  
Rat Diaphragm ◽  
Dual Nature ◽  
Hypophysectomized Rats ◽  
D 20

ABSTRACT In vitro addition of bovine growth hormone (GH) to intact hemidiaphragms from hypophysectomized rats has previously been found to produce both an early stimulatory effect lasting for 2—3 hours and a subsequent late inhibitory effect during which the muscle is insensitive to further addition of GH (Hjalmarson 1968). These effects on the accumulation rate of α-aminoisobutyric acid (AIB) and D-xylose have been further studied. In presence of actinomycin D (20 μg/ml) or puromycin (100 μg/ml) the duration of the stimulatory effect of GH (25 μg/ml) was prolonged to last for at least 4—5 hours and the late inhibitory effect was prevented. Similar results were obtained when glucose-free incubation medium was used. Preincubation of the diaphragm at different glucose concentrations (0—5 mg/ml) for 3 hours did not change the GH sensitivity. Addition of insulin at start of incubation could not prevent GH from inducing its late inhibitory effect, while dexamethasone seemed to potentiate this effect of GH. Furthermore, adrenaline was found to decrease the uptake of AIB-14C and D-xylose-14C in the diaphragm, but not to change the sensitivity of the muscle to GH. Preincubation of the diaphragm for 3 hours with puromycin in a concentration of 200 μg/ml markedly decreased the subsequent basal uptake of both AIB-14C and D-xylose-14C, in the presence of puromycin, and abolished the stimulatory effect of GH on the accumulation of AIB-14C. However, the effect of GH on the accumulation of D-xylose-14C was unchanged. The present observations are discussed and evaluated in relation to various mechanisms of GH action proposed to explain the dual nature of the hormone.

A Sensitive Method for Assay of Mixed-Function Oxygenase (p-450 complex) in Cell Culture

1988 ◽  
Vol 15 (3) ◽  
pp. 219-223
Author(s):  
Jørgen Clausen ◽  
Søren Achim Nielsen
Keyword(s):  
Human Lymphocytes ◽  
Cellular Systems ◽  
Metabolic Effects ◽  
Assay Method ◽  
Related Family ◽  
Oxygenase Activity ◽  
Metabolic Transformation ◽  
Mixed Function Oxygenase

The mixed-function oxygenase system involved in the metabolism of drugs and xenobiotics has been extensively studied in various animal species and in various organs (1). It is now apparent that in humans the p-450 complex is one representative of a related family, expressed by 13 c-DNA genes showing approximately 36% similarity between the different subfamilies (2). In order to compare the in vivo and in vitro metabolic effects of drugs and xenobiotics, the induction capabilities of the mixed-function oxygenase must be known. The most sensitive non-isotopic assay system for determination of mixed-function oxygenase activity is the method of Nebert & Gelboin (3,4), which is based on the metabolic transformation of benzo-(a)-pyrene to its fluorescent hydroxyl derivatives (5). However, the levels of the mixed-function oxygenase enzymes in different cellular systems show great variations, with the highest activities in liver cells. Therefore, in order to use human lymphocytes and other cellular systems with low mixed-function oxygenase activities, the assay method for determining oxygenase activity must have the highest possible sensitivity. The present communication is devoted to a study aimed at increasing the sensitivity of Nebert & Gelboin's methods for assay of mixed-function oxygenase subfamilies using benzo-(a)-pyrene as a substrate.

scholarly journals Lysyl-tRNA synthetase from Escherichia coli K12. Chromatographic heterogeneity and the lysU-gene product

1987 ◽  
Vol 248 (1) ◽  
pp. 43-51 ◽  
Author(s):  
J Charlier ◽  
R Sanchez
Keyword(s):  
Escherichia Coli ◽  
Gene Product ◽  
Activity Ratio ◽  
Deae Cellulose ◽  
Trna Synthetase ◽  
Trna Synthetases ◽  
E Coli ◽  
Aminoacyl Trna Synthetases

In contrast with most aminoacyl-tRNA synthetases, the lysyl-tRNA synthetase of Escherichia coli is coded for by two genes, the normal lysS gene and the inducible lysU gene. During its purification from E. coli K12, lysyl-tRNA synthetase was monitored by its aminoacylation and adenosine(5′)tetraphospho(5′)adenosine (Ap4A) synthesis activities. Ap4A synthesis was measured by a new assay using DEAE-cellulose filters. The heterogeneity of lysyl-tRNA synthetase (LysRS) was revealed on hydroxyapatite; we focused on the first peak, LysRS1, because of its higher Ap4A/lysyl-tRNA activity ratio at that stage. Additional differences between LysRS1 and LysRS2 (major peak on hydroxyapatite) were collected. LysRS1 was eluted from phosphocellulose in the presence of the substrates, whereas LysRS2 was not. Phosphocellulose chromatography was used to show the increase of LysRS1 in cells submitted to heat shock. Also, the Mg2+ optimum in the Ap4A-synthesis reaction is much higher for LysRS1. LysRS1 showed a higher thermostability, which was specifically enhanced by Zn2+. These results in vivo and in vitro strongly suggest that LysRS1 is the heat-inducible lysU-gene product.

Reduced and S-carboxymethylated human growth hormone: a probe for diabetogenic action

1984 ◽  
Vol 247 (5) ◽  
pp. E639-E644
Author(s):  
C. M. Cameron ◽  
J. L. Kostyo ◽  
J. A. Rillema ◽  
S. E. Gennick
Keyword(s):  
Growth Hormone ◽  
Amino Acid ◽  
Human Growth Hormone ◽  
Human Growth ◽  
Mouse Mammary Gland ◽  
Amino Acid Incorporation ◽  
Acid Incorporation ◽  
Hypophysectomized Rats

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.

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