Growth hormone-releasing factor analogs with hydrophobic residues at position 19. Effects on growth hormone releasing activity in vitro and in vivo, stability in blood plasma in vitro, and secondary structure

1992 ◽  
Vol 35 (21) ◽  
pp. 3928-3933 ◽  
Author(s):  
Alan R. Friedman ◽  
Avneet K. Ichhpurani ◽  
William M. Moseley ◽  
Glenn R. Alaniz ◽  
William H. Claflin ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Secondary Structure ◽  
Blood Plasma ◽  
Growth Hormone Releasing Factor ◽  
Hydrophobic Residues ◽  
In Blood Plasma

scholarly journals Screening of lung cancer biomarker-proteins with a multiplex electrochemical sensor system based on aptamers

2018 ◽  
Vol 17 (3) ◽  
pp. 13-21
Author(s):  
Yu. E. Glazyrin ◽  
A. V. Shabalina ◽  
K. A. Ryginskaya ◽  
S. S. Zamay ◽  
V. A. Kolovski ◽  
...  
Keyword(s):  
Lung Cancer ◽  
Blood Plasma ◽  
Simultaneous Detection ◽  
Selection Procedure ◽  
Cancer Tissue ◽  
Dna Aptamers ◽  
Affinity Enrichment ◽  
In Blood Plasma

The aimof this work is the development and demonstration of the method of simultaneous detection of several biomarkers of lung cancer in the blood plasma of patients using a multiplex electrochemical testing system based on DNA aptamers. DNA aptamers are a new class of synthetic affinity probes obtained by in vitro or in vivo selection procedure by the systematic evolution of ligands by exponential enrichment (SELEX).Materials and methods.A set of aptamers obtained previously by selection for postoperative lung cancer tissue was used to create a multiplex electrochemical biochip. Identification of aptamer target proteins was performed using a modified affinity enrichment method (AptaBID). Molecular targets for the used set of aptamers to lung cancer were defined as vimentin, defensin, a light chain of myosin, tubulin alpha 1-B, neutrophil elastase and A1 elongation factor 1.Measurements of the presence of these biomarker proteins in blood plasma were carried out using electrochemical detection. The difference between peak heights before and after plasma deposition on the electrodes modified by aptamers was considered as a response of the system to the presence of protein onco-markers in blood plasma. Blood plasma of healthy volunteers was used as control.Results. Research showed that in the blood plasma of all the patients with lung cancer the content of biomarker proteins that bind to aptamers on electrode surfaces was increased. The increased content of these proteins in the blood plasma of patients suggests the presence of invasiveness and metastasis of tumors and their chemo-resistance.

Periodic interactions of GH-releasing factor and somatostatin can augment GH release in vitro

1987 ◽  
Vol 253 (5) ◽  
pp. E508-E514
Author(s):  
J. Weiss ◽  
M. J. Cronin ◽  
M. O. Thorner
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Human Growth ◽  
Male Rat ◽  
Base Line ◽  
Additive Effects ◽  
Growth Hormone Releasing Factor ◽  
The Impact

Growth hormone (GH) is secreted as pulses in vivo. To understand the signals governing this periodicity, we have established a perifusion-based model of pulsatile GH release. Male rat anterior pituitaries were dispersed and perifused with pulses of human growth hormone-releasing factor-(1--40) (GHRF), with or without a continuous or discontinuous somatostatin tonus. An experiment was composed of a 1-h base-line collection followed by four 3-h cycles; each contained single or paired 10-min infusion(s) of 3 nM GHRF. In testing the impact of somatostatin, the protocol was identical except that 0.3 nM somatostatin was added 30 min into the base-line period and then was either continued throughout the study or withdrawn during the periods of GHRF infusion. GH base lines with somatostatin were lower than vehicle base lines (P less than 0.05). GHRF pulses generated consistent peaks of GH release between 200 and 300 ng. min-1. (10(7) cells)-1, and these peaks were not altered by continuous somatostatin. In contrast, withdrawal of somatostatin during GHRF administration elicited markedly higher GH peaks (P less than 0.05) and more total GH release (P less than 0.05). This response could not be accounted for by the additive effects of GHRF and somatostatin withdrawal.

In vivo and in vitro evidence of growth hormone-releasing factor-like produced locally in the adenohypophyseal cells of the rat

Neuropeptides ◽  
1991 ◽  
Vol 19 (4) ◽  
pp. 223-229 ◽  
Author(s):  
J. Carretero ◽  
F. Sánchez ◽  
R. Vázquez ◽  
L. Cacicedo ◽  
F. Sánchez-Franco ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Growth Hormone Releasing Factor

Effects of growth hormone releasing factor on pancreatic secretion in vivo and in vitro

1989 ◽  
Vol 24 (3) ◽  
pp. 301-311 ◽  
Author(s):  
Stanislaw J. Konturek ◽  
Jan Bilski ◽  
Jolanta Jaworek ◽  
Tokru Mochizuki ◽  
Chizuko Yanaihara ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Pancreatic Secretion ◽  
Growth Hormone Releasing Factor

In vitro and in vivo Growth Hormone Responsiveness to Growth Hormone-Releasing Factor in Male and Female Zucker Rats

1989 ◽  
Vol 50 (4) ◽  
pp. 454-459 ◽  
Author(s):  
Geneviève Renier ◽  
Pierrette Gaudreau ◽  
Nathalie Deslauriers ◽  
Paul Brazeau
Keyword(s):  
Growth Hormone ◽  
Zucker Rats ◽  
Male And Female ◽  
Growth Hormone Releasing Factor ◽  
In Vivo Growth ◽  
Hormone Responsiveness

scholarly journals Elongated neutrophil-derived structures are blood-borne microparticles formed by rolling neutrophils during sepsis

2020 ◽  
Vol 218 (3) ◽  
Author(s):  
Alex Marki ◽  
Konrad Buscher ◽  
Cristina Lorenzini ◽  
Matthew Meyer ◽  
Ryosuke Saigusa ◽  
...  
Keyword(s):  
Blood Plasma ◽  
Vessel Wall ◽  
Submicron Particles ◽  
New Class ◽  
Vessel Lumen ◽  
Molecular Pattern ◽  
Healthy Donors ◽  
In Blood Plasma

Rolling neutrophils form tethers with submicron diameters. Here, we report that these tethers detach, forming elongated neutrophil-derived structures (ENDS) in the vessel lumen. We studied ENDS formation in mice and humans in vitro and in vivo. ENDS do not contain mitochondria, endoplasmic reticulum, or DNA, but are enriched for S100A8, S100A9, and 57 other proteins. Within hours of formation, ENDS round up, and some of them begin to present phosphatidylserine on their surface (detected by annexin-5 binding) and release S100A8–S100A9 complex, a damage-associated molecular pattern protein that is a known biomarker of neutrophilic inflammation. ENDS appear in blood plasma of mice upon induction of septic shock. Compared with healthy donors, ENDS are 10–100-fold elevated in blood plasma of septic patients. Unlike neutrophil-derived extracellular vesicles, most ENDS are negative for the tetraspanins CD9, CD63, and CD81. We conclude that ENDS are a new class of bloodborne submicron particles with a formation mechanism linked to neutrophil rolling on the vessel wall.

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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