Potentiation of the growth-promoting activity of porcine growth hormone (pGH) with an antibody generated in rabbits to the peptide sequence pGH110–118

1990 ◽  
Vol 127 (3) ◽  
pp. 481-485 ◽  
Author(s):  
B. S. Wang ◽  
E. Szewczyk ◽  
H.-M. Shieh ◽  
I. C. Hart

ABSTRACT An effort was made to identify the antigenic epitope(s) of porcine GH (pGH) capable of inducing antibodies which would enhance the growth-promoting activity of the hormone. Several peptide sequences of the pGH molecule were synthesized and the antibodies to these peptides were generated in rabbits. The majority of these antibodies were found to be immunoreactive with both intact pGH and their respective peptide antigens. The biological activity of the antibodies was tested in growth-retarded hypophysectomized rats. Daily injections with pGH alone significantly increased their growth rate and treatment with a combination of pGH and antibody specific to the peptide sequence 110–118 further heightened the somatogenic effect. Administration of this antibody alone did not enhance the growth rate of hypophysectomized rats, neither did antibodies raised to intact pGH or the other peptide sequences. The present findings suggest that antibody with a particular pGH epitope specificity is able to increase the somatogenic activity of pGH and that the peptide corresponding to pGH amino acids 110–118 may prove useful in the development of growth promoting vaccines. Journal of Endocrinology (1990) 127, 481–485

1954 ◽  
Vol 32 (1) ◽  
pp. 400-406 ◽  
Author(s):  
M. O. Burton ◽  
F. J. Sowden ◽  
A. G. Lochhead

A procedure is described for the production and concentration of the 'terregens factor' (TF), a bacterial growth promoting substance synthesized by Arthrobacter pascens and essential for the growth of Arthrobacter terregens. From culture filtrates of A. pascens cultivated in a medium of inorganic salts and sucrose, concentrates of TF may be obtained that are active at 0.001 μgm. Per ml., heat stable and contain about 12.7% nitrogen. Acid hydrolysis yielded a number of amino acids, including glutamic acid, glycine, α–alanine, valine, leucine, proline, lysine, and arginine, as well as some unidentified compounds; however, TF does not appear to be a low molecular weight straight chain peptide.Although TF contains no iron, it combines readily with ferrous or ferric iron to form reddish-brown complexes with this metal. Activity for A. terregens is shown by certain iron containing complexes as hemin, coprogen, and ferrichrome. On the other hand none is shown by cytochrome or pulcherrimin; however, aspergillic acid, structurally related to the latter, possesses some growth promoting activity for the test organism.


1968 ◽  
Vol 109 (1) ◽  
pp. 19-24 ◽  
Author(s):  
Louise Oliver ◽  
Anne Stockell Hartree

The cystine-containing peptides of horse growth hormone were isolated and their amino acid sequences determined. Four unique half-cystine residues occur in two peptides, one containing 11 and the other, at the C-terminus of the protein, 15 amino acids. These sequences are compared with published data on growth hormones from other species.


1970 ◽  
Vol 119 (4) ◽  
pp. 629-634 ◽  
Author(s):  
M. J. Clemens ◽  
A. Korner

1. Incorporation of [14C]leucine into protein in rat liver slices, incubated in vitro, increased as the concentration of unlabelled amino acids in the incubation medium was raised. A plateau of incorporation was reached when the amino acid concentration was 6 times that present in rat plasma. Labelling of RNA by [3H]orotic acid was not stimulated by increased amino acid concentration in the incubation medium. 2. When amino acids were absent from the medium, or present at the normal plasma concentrations, no effect of added growth hormone on labelling of protein or RNA by precursor was observed. 3. When amino acids were present in the medium at 6 times the normal plasma concentrations addition of growth hormone stimulated incorporation of the appropriate labelled precursor into protein of liver slices from normal rats by 31%, and into RNA by 22%. A significant effect was seen at a hormone concentration as low as 10ng/ml. 4. Under the same conditions addition of growth hormone also stimulated protein labelling in liver slices from hypophysectomized rats. Tissue from hypophysectomized rats previously treated with growth hormone did not respond to growth hormone in vitro. 5. No effect of the hormone on the rate or extent of uptake of radioactive precursors into acid-soluble pools was found. 6. Cycloheximide completely abolished the hormone-induced increment in labelling of both RNA and protein. 7. It was concluded that, in the presence of an abundant amino acid supply, growth hormone can stimulate the synthesis of protein in rat liver slices by a mechanism that is more sensitive to cycloheximide than is the basal protein synthesis. The stimulation of RNA labelling observed in the presence of growth hormone may be a secondary consequence of the hormonal effect on protein synthesis. 8. The mechanism of action of growth hormone on liver protein synthesis in vitro was concluded to be similar to its mechanism of action in vivo.


1959 ◽  
Vol 196 (4) ◽  
pp. 859-865 ◽  
Author(s):  
Robert O. Scow

Rats were thyroidectomized-hypophysectomized at weaning and 5 weeks later treated for 36 days with either growth hormone (0.1 or 0.5 mg/day), thyroxine (2.5 µg/day), or both. Growth hormone stimulated growth of all tissues whereas thyroxine accelerated growth of only muscle and certain viscera. The growth response of some tissues to thyroxine was as pronounced as that to growth hormone. Administration of thyroxine increased the response to growth hormone of only the tissues that grew when thyroxine was given alone. Although thyroxine had no effect on the amount of bone protein in growth hormone treated and untreated rats, it had a pronounced effect on the morphology (length and maturation) of bone. The amount of collagen in muscle increased with dosage of growth hormone; thyroxine had no effect on this response. Myosin, on the other hand, increased with growth hormone dosage only in those animals also given thyroxine. Thyroxine given alone increased myosin deposition in muscle but had no effect on collagen in muscle, bone or skin.


1956 ◽  
Vol 145 (919) ◽  
pp. 259-270 ◽  

Protamine zinc insulin has no growth-promoting effect in rats whose growth has been inhibited by diethylstilboestrol. Hypophyseal growth hormone stimulates growth in diethylstilboestrol-treated rats, and treatment with growth hormone and protamine zinc insulin results in an enhanced rate of growth. Protamine zinc insulin has growth-promoting properties in hypophysectomized rats, and cortisone acetate inhibits growth in insulin-treated hypophysectomized rats. 2-4-Dinitrophenol prevents growth and increases nitrogen excretion in young rats. Combined treatm ent with insulin, growth hormone and glucose induces growth and brings about positive nitrogen balance in dinitrophenol-poisoned rats. Adrenal, testis, liver and pancreas weights are normal in dinitrophenol-poisoned rats. The amount of extractable pancreatic insulin is also within normal limits. It is suggested that the functions of the hypophysis and pancreas are not seriously impaired, and that treatment with growth hormone and insulin promotes esterification of inorganic phosphate to high-energy phosphate compounds in the dinitrophenol-poisoned rats.


1962 ◽  
Vol 203 (5) ◽  
pp. 933-938 ◽  
Author(s):  
C. A. Snipes ◽  
J. L. Kostyo

Hypophysectomy decreased the concentrations of alanine and histidine in the cell water of the rat diaphragm, but had no influence on the levels of these amino acids in plasma. The concentrations of alanine and histidine in the cell water did not vary appreciably from in vivo values, when "intact" diaphragms of either normal or hypophysectomized rats were incubated in Krebs bicarbonate buffer. Addition of l-alanine or l-histidine to the incubation medium resulted in the accumulation of these amino acids in the cell water of both normal and hypophysectomized rat diaphragms. However, muscles or hypophysectomized rats accumulated these amino acids to a lesser extent. When added to the incubation medium, bovine growth hormone stimulated the accumulation of l-alanine and l-histidine by diaphragms of hypophysectomized rats. Thus, these experiments suggest that growth hormone participates in the regulation of utilizable amino acid transport into muscle.


1954 ◽  
Vol 32 (4) ◽  
pp. 400-406 ◽  
Author(s):  
M. O. Burton ◽  
F. J. Sowden ◽  
A. G. Lochhead

A procedure is described for the production and concentration of the 'terregens factor' (TF), a bacterial growth promoting substance synthesized by Arthrobacter pascens and essential for the growth of Arthrobacter terregens. From culture filtrates of A. pascens cultivated in a medium of inorganic salts and sucrose, concentrates of TF may be obtained that are active at 0.001 μgm. Per ml., heat stable and contain about 12.7% nitrogen. Acid hydrolysis yielded a number of amino acids, including glutamic acid, glycine, α–alanine, valine, leucine, proline, lysine, and arginine, as well as some unidentified compounds; however, TF does not appear to be a low molecular weight straight chain peptide.Although TF contains no iron, it combines readily with ferrous or ferric iron to form reddish-brown complexes with this metal. Activity for A. terregens is shown by certain iron containing complexes as hemin, coprogen, and ferrichrome. On the other hand none is shown by cytochrome or pulcherrimin; however, aspergillic acid, structurally related to the latter, possesses some growth promoting activity for the test organism.


1988 ◽  
Vol 118 (3) ◽  
pp. 465-470
Author(s):  
M. Volosin ◽  
M. E. Celis

ABSTRACT In hypophysectomized rats on day 1 of dioestrus, as well as on day 4 of pseudopregnancy, α-MSH (continuous infusion of 1 μg/h) failed to maintain serum concentrations of progesterone. On the other hand, α-MSH did not modify the increase induced by ACTH (1 μg/μl as an infusion plus two additional daily injections of 30 μg/μl), prolactin (200 μg/0·2 ml at 12-h intervals) or GH (300 μg/0·2 ml twice daily) on serum concentrations of progesterone in such rats. However, in intact rats α-MSH caused a significant rise in serum concentrations of GH on day 1 and day 2 of dioestrus. Continuous infusion of α-MSH produced an increase in serum concentrations of GH at 12.00 and 14.00 h on day 1 of dioestrus and at 07.00 h on day 2. It is therefore suggested that α-MSH may exert its effect by facilitating the secretion of GH, which in turn may induce the release of progesterone. J. Endocr. (1988) 118, 465–470


1965 ◽  
Vol 49 (3) ◽  
pp. 366-369 ◽  
Author(s):  
M. Reiss ◽  
M. B. Sideman ◽  
E. S. Plichta

ABSTRACT Human chorionic gonadotrophin (HCG) and an anabolic steroid did not raise the weight of hypophysectomized rats: those substances, however, prevented the weight decrease seen in the first 3 weeks after operation of 200 g rats which were maintained both pre- and post-operatively on the same routine diet. HCG did not have this effect on hypophysectomized animals which had been also castrated. It is assumed that the growth promoting action seen after HCG or anabolic steroid is due in normal animals and patients to an endogenous stimulation of growth hormone production by the pituitary anterior lobe.


1963 ◽  
Vol 42 (3) ◽  
pp. 389-394 ◽  
Author(s):  
B. Eckstein ◽  
H. Shain

The response of ovarian and uterine glutamic-oxalacetic transaminase (GOT) activity to serum gonadotrophin (PMS) treatment at various ages of the developing rat was studied. The greatest response (62.2 per cent increase in the ovary and 74.5 per cent increase in the uterus) were found at the ages of 31–33 days. Growth hormone and oestrogen administration caused an increase in ovarian weight with no rise in GOT. It is therefore concluded that the action of gonadotrophin on GOT activity in the ovary is specific. All sex hormones examined, (oestrone, testosterone and progesterone) which had a stimulating activity on the immature rat uterus, induced an increase of GOT activity in this organ. Growth hormone also stimulated growth of the uterus, but reduced its GOT activity. This indicates a difference between the growth promoting action of growth hormone and of the sex hormones on the uterus. As the GOT stimulating effect of PMS was induced in hypophysectomized rats, it is concluded that this effect is not mediated by the hypophysis.


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