Bovine growth hormone fragment (1–133) has in-vitro somatomedin-like activity

1983 ◽  
Vol 96 (2) ◽  
pp. 195-199 ◽  
Author(s):  
J. P. Liberti ◽  
L. A. Durham
Keyword(s):  
Growth Hormone ◽  
Amino Acid ◽  
Costal Cartilage ◽  
Peptide Bond ◽  
Biologically Active ◽  
The Other ◽  
Bovine Growth Hormone ◽  
Amino Acid Residues ◽  
In Vitro Uptake

Thrombin digestion of bovine growth hormone (1–191) resulted in cleavage of the peptide bond between amino acid residues 133 and 134. Native growth hormone and purified peptides (1–133) and (134–191) were assayed for somatomedin-like activity. Peptide (1–133), ranging in concentration from 0·15–15 nmol/l, stimulated in-vitro uptake of [3H]thymidine by rat costal cartilage. None of the other peptides was biologically active.

Oxytocin analogues with non-coded amino acid residues in position 8: [8-Neopentylglycine]oxytocin and [8-cycloleucine]oxytocin

1987 ◽  
Vol 52 (9) ◽  
pp. 2317-2325 ◽  
Author(s):  
Jan Hlaváček ◽  
Jan Pospíšek ◽  
Jiřina Slaninová ◽  
Walter Y. Chan ◽  
Victor J. Hruby
Keyword(s):  
Amino Acid ◽  
Solid Phase Synthesis ◽  
Solid Phase ◽  
The Other ◽  
Amino Acid Residues ◽  
Phase Synthesis ◽  
Other Hand ◽  
Fragment Condensation

[8-Neopentylglycine]oxytocin (II) and [8-cycloleucine]oxytocin (III) were prepared by a combination of solid-phase synthesis and fragment condensation. Both analogues exhibited decreased uterotonic potency in vitro, each being about 15-30% that of oxytocin. Analogue II also displayed similarly decreased uterotonic potency in vivo and galactogogic potency. On the other hand, analogue III exhibited almost the same potency as oxytocin in the uterotonic assay in vivo and in the galactogogic assay.

scholarly journals Amino Acid Sequence of a Biologically Active Fragment of Bovine Growth Hormone

1972 ◽  
Vol 247 (12) ◽  
pp. 3874-3880
Author(s):  
Nobuyuki Yamasaki ◽  
Kenji Kangawa ◽  
Shigeru Kobayashi ◽  
Motosuke Kikutani ◽  
Martin Sonenberg
Keyword(s):  
Growth Hormone ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Biologically Active ◽  
Bovine Growth Hormone ◽  
Active Fragment

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.

scholarly journals Effects of Modifications on the Immunosuppressive Properties of Cyclolinopeptide A and its Analogs in Animal Experimental Models

2021 ◽  
Author(s):  
Michał Zimecki ◽  
Krzysztof Kaczmarek
Keyword(s):  
Amino Acid ◽  
Biological Activities ◽  
Peptide Bond ◽  
Mechanisms Of Action ◽  
Experimental Models ◽  
Amino Acid Residues ◽  
Modified Peptides ◽  
Immunosuppressive Potency

The consequences of manipulations in structure and amino acid composition of native cyclolinopeptide A (CLA) from linen seeds and its linear precursor on their biological activities and mechanisms of action are reviewed. The modifications included truncation of the peptide chain, replacement of amino acid residues with proteinogenic or non-proteinogenic ones, modifications of peptide bond, and others. The studies revealed changes in the immunosuppressive potency of these analogs investigated in a number of in vitro and in vivo experimental models, predominantly in rodents, as well as differences in their postulated mechanism of action. The modified peptides were compared with cyclosporine A and parent CLA. Some of the synthesized and investigated peptides show potential therapeutic usefulness.

scholarly journals Purification of a high-molecular-weight somatoliberin (growth-hormone-releasing factor) from pig hypothalami

1983 ◽  
Vol 209 (3) ◽  
pp. 643-651 ◽  
Author(s):  
J E C Sykes ◽  
P J Lowry
Keyword(s):  
Molecular Weight ◽  
Growth Hormone ◽  
Amino Acid ◽  
Response Curve ◽  
Gel Filtration ◽  
Apparent Molecular Weight ◽  
Amino Acid Residues ◽  
Growth Hormone Releasing Factor

Preliminary observations [Sykes & Lowry (1980) J. Endocrinol. 85, 42P-43P] had suggested that the major hypothalamic somatoliberin (growth-hormone-releasing factor) was a larger peptide than the other characterized hypothalamic factors, with an elution position on Sephadex G-50 between those of neurophysin and corticotropin. The present paper reports the isolation and preliminary characterization of pig hypothalamic somatoliberin. Acid extracts of pig stalk median eminence were purified by gel filtration and preparative and analytical high-pressure liquid chromatography to yield a preparation that was specific in the release of somatotropin (growth hormone) in vitro, giving a steep dose-response curve at doses in the range 0.20-3.0 ng. Amino acid analysis revealed a non-cysteine-containing peptide with a high number of glutamate (or glutamine) and aspartate (or asparagine) residues. The peptide had about 56-57 amino acid residues and an apparent molecular weight of 6400, in keeping with its elution position on a column of Sephadex G-50.

scholarly journals Tryptic digestion of peptides corresponding to modified fragments of human growth hormone-releasing hormone.

2004 ◽  
Vol 51 (1) ◽  
pp. 51-56 ◽  
Author(s):  
Ewa Witkowska ◽  
Alicja Orłowska ◽  
Jan Izdebski
Keyword(s):  
Growth Hormone ◽  
Amino Acid ◽  
Human Growth Hormone ◽  
Proteolytic Enzymes ◽  
Human Growth ◽  
Peptide Bond ◽  
Growth Hormone Releasing Hormone ◽  
Amino Acid Residues ◽  
Releasing Hormone ◽  
Hydrolysis Process

The objective of this study was to examine the degradation of short peptides corresponding to modified fragments of human growth hormone-releasing hormone by trypsin. Six analogues of pentapeptide 9-13 of human growth hormone-releasing hormone containing homoarginine, ornithine, glutamic acid, glycine, leucine or phenylalanine residue in position 11, two analogues of hexapeptide 8-13 of human growth hormone-releasing hormone and two analogues of heptapeptide 7-13 of human growth hormone-releasing hormone containing homoarginine or glycine residue in position 11 were obtained. The peptides were subjected to digestion by trypsin and the course of reaction was monitored using HPLC. It was found that the rate of hydrolysis of the Lys(12)-Val(13) peptide bond depends on the amino-acid residue preceding Lys(12). The extension of the peptide chain towards the N-terminus by introduction of consecutive amino-acid residues corresponding to the human growth hormone-releasing hormone sequence accelerates the hydrolysis process. These results may be of assistance in designing new analogues of human growth hormone-releasing hormone, more resistant to the activity of proteolytic enzymes.

scholarly journals Identification of a cDNA encoding a novel amphibian growth hormone-releasing peptide and localization of its transcript

2002 ◽  
Vol 174 (3) ◽  
pp. 395-402 ◽  
Author(s):  
K Sawada ◽  
K Ukena ◽  
S Kikuyama ◽  
K Tsutsui
Keyword(s):  
Growth Hormone ◽  
Amino Acid ◽  
Cellular Localization ◽  
Hormone Secretion ◽  
Basic Amino Acid ◽  
Pituitary Hormone ◽  
Amino Acid Residues ◽  
Rapid Amplification

Recently, we identified in the bullfrog brain a novel neuropeptide with a C-terminal Leu-Pro-Leu-Arg-Phe-NH(2) sequence. This amphibian neuropeptide was shown to stimulate growth hormone (GH) release in vitro and in vivo and so was designated frog GH-releasing peptide (fGRP). In this study, we cloned a cDNA encoding fGRP from the bullfrog brain by a combination of 3' and 5' rapid amplification of cDNA ends (RACE). The deduced fGRP precursor consisted of 221 amino acid residues, encoding one fGRP and three putative fGRP-related peptides that included Leu-Pro-Xaa-Arg-Phe-NH(2) (Xaa=Leu or Gln) at their C-termini. All these peptide sequences were flanked by a glycine C-terminal amidation signal and a single basic amino acid on each end as an endoproteolytic site. Northern blot analysis detected a single band of approximately 1.0 kb, indicating that no alternatively spliced forms were present. Such an apparent migration was in agreement with the estimated length of the cDNA, 902 bp. In situ hybridization further revealed the cellular localization of fGRP mRNA in the suprachiasmatic nucleus in the hypothalamus. In addition to fGRP, its related peptides may be hypothalamic factors involved in pituitary hormone secretion.

scholarly journals Effects of Modifications on the Immunosuppressive Properties of Cyclolinopeptide A and Its Analogs in Animal Experimental Models

Molecules ◽  
2021 ◽  
Vol 26 (9) ◽  
pp. 2538
Author(s):  
Michał Zimecki ◽  
Krzysztof Kaczmarek
Keyword(s):  
Amino Acid ◽  
Biological Activities ◽  
Peptide Bond ◽  
Mechanisms Of Action ◽  
Experimental Models ◽  
Amino Acid Residues ◽  
Modified Peptides ◽  
Immunosuppressive Potency

The consequences of manipulations in structure and amino acid composition of native cyclolinopeptide A (CLA) from linen seeds, and its linear precursor on their biological activities and mechanisms of action, are reviewed. The modifications included truncation of the peptide chain, replacement of amino acid residues with proteinogenic or non-proteinogenic ones, modifications of peptide bond, and others. The studies revealed changes in the immunosuppressive potency of these analogs investigated in a number of in vitro and in vivo experimental models, predominantly in rodents, as well as differences in their postulated mechanism of action. The modified peptides were compared with cyclosporine A and parent CLA. Some of the synthesized and investigated peptides show potential therapeutic usefulness.

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.

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