scholarly journals The synthesis, oxidation and characterization of GLP-1 peptide receptor fragments

2018 ◽  
Author(s):  
János Szolomájer ◽  
Zoltán Kele ◽  
Gábor K. Tóth ◽  
Pál Stráner ◽  
András Perczel
Keyword(s):  
Peptide Receptor ◽  
Receptor Fragments

Opioid Peptide Receptor Studies. 13. Characterization of Opioid Antagonists With the [35S]GTP-γ-S Binding Assay

Analgesia ◽  
1999 ◽  
Vol 4 (1) ◽  
pp. 27-32 ◽  
Author(s):  
John S. Partilla ◽  
F. Ivy Carrol ◽  
James B. Thomas ◽  
Kenner C. Rice ◽  
Dennis M. Zimmerman ◽  
...  
Keyword(s):  
Binding Assay ◽  
Opioid Peptide ◽  
Opioid Antagonists ◽  
Peptide Receptor

Characterization of the bombesin-like peptide receptor family in primates

Genomics ◽  
2004 ◽  
Vol 84 (1) ◽  
pp. 139-146 ◽  
Author(s):  
Hideki Sano ◽  
Scott D Feighner ◽  
Donna L Hreniuk ◽  
Hisashi Iwaasa ◽  
Andreas W Sailer ◽  
...  
Keyword(s):  
Peptide Receptor ◽  
Receptor Family

scholarly journals Neutrophil elastase produces 52-kD and 30-kD glucocorticoid receptor fragments in the cytosol of human leukemia cells

Blood ◽  
1987 ◽  
Vol 70 (3) ◽  
pp. 860-868
Author(s):  
CW Distelhorst ◽  
KE Janiga ◽  
KJ Howard ◽  
SE Strandjord ◽  
EJ Campbell
Keyword(s):  
Glucocorticoid Receptor ◽  
Neutrophil Elastase ◽  
Glucocorticoid Receptors ◽  
Leukemia Cell ◽  
Specific Inhibitor ◽  
Leukemia Cells ◽  
Human Leukemia ◽  
Receptor Fragments ◽  
Limited Digestion

Characterization of glucocorticoid receptors in leukemia cells is important to understand mechanisms of glucocorticoid resistance but has been impeded by receptor fragmentation in cytosol extracts. We recently found that formation of 52- and 30-kilodalton (kD) glucocorticoid receptor fragments in cytosol of leukemia cells is due to proteolysis and is blocked by diisopropylfluorophosphate (DFP). In the present study, we identify a 28-kD serine protease in cytosol of leukemia cells that binds [3H]DFP and correlates with the formation of 52- and 30-kD receptor fragments. This protease is immunoprecipitated by antiserum to neutrophil elastase. Limited digestion of [3H]dexamethasone-21-mesylate- labeled receptors by purified neutrophil elastase produces 52- and 30- kD receptor fragments. Receptor fragmentation in the cytosol of leukemia cells in inhibited by methoxysuccinyl-alanyl-alanyl-prolyl- valyl-chloromethylketone, a highly specific inhibitor of neutrophil elastase. The addition of as few as 5% neutrophils to a lymphoid cell suspension provides sufficient elastase to produce receptor fragmentation. Our findings indicate that neutrophil elastase is responsible for receptor fragmentation in the cytosol of leukemia cells. The neutrophil elastase may be endogenous to the leukemia cells or may come from neutrophils that contaminate leukemia cell suspensions.

scholarly journals Identification and Characterization of a New Growth Hormone–Releasing Peptide Receptor in the Heart

1999 ◽  
Vol 85 (9) ◽  
pp. 796-802 ◽  
Author(s):  
V. Bodart ◽  
J. F. Bouchard ◽  
N. McNicoll ◽  
E. Escher ◽  
P. Carrière ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Peptide Receptor ◽  
Identification And Characterization

scholarly journals Characterization of an oligopeptide chemoattractant receptor on human blood monocytes using a new radioligand

Blood ◽  
1984 ◽  
Vol 63 (3) ◽  
pp. 588-592 ◽  
Author(s):  
MC Benyunes ◽  
R Snyderman
Keyword(s):  
Human Blood ◽  
Polymorphonuclear Leukocytes ◽  
Specific Radioactivity ◽  
Blood Monocytes ◽  
Chemotactic Peptide ◽  
Peripheral Blood Monocytes ◽  
Peptide Receptor ◽  
Human Polymorphonuclear Leukocytes ◽  
Dissociation Constant Kd

Abstract The study of chemoattractant receptors on human monocytes had been limited by the lack of a radioligand suitable for use with the small numbers of cells routinely available from human donors. A new synthetic oligopeptide radioligand f[35S]met-leu-phe, with a higher specific radioactivity than was available with the tritiated compound, was used to characterize a chemoattractant receptor on freshly isolated human blood monocytes. These cells bind f[35S]met-leu-phe with a dissociation constant (KD) of 30.2 +/- 5.6 nM and contain 84,000 +/- 11,300 receptors per cell. f[35S]met-leu-phe does not bind specifically to blood lymphocytes. The specificity of the oligopeptide receptor on monocytes is indistinguishable from the oligopeptide chemoattractant receptor on human polymorphonuclear leukocytes. Using f[35S]met-leu- phe, it will now be feasible to study the chemotactic peptide receptor on small numbers of partially purified peripheral blood monocytes from patients with defects of immune function.

Characterization of a putative molluscan insulin-related peptide receptor

Gene ◽  
1995 ◽  
Vol 162 (2) ◽  
pp. 181-188 ◽  
Author(s):  
Edwin Roovers ◽  
Muriel E. Vincent ◽  
Ellen van Kesteren ◽  
Wijnand P.M. Geraerts ◽  
Rudi J. Planta ◽  
...  
Keyword(s):  
Peptide Receptor ◽  
Related Peptide
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