Characterization of high-affinity receptors for truncated glucagon-like peptide-1 in rat gastric glands

FEBS Letters ◽  
1990 ◽  
Vol 262 (1) ◽  
pp. 139-141 ◽  
Author(s):  
L.O. Uttenthal ◽  
E. Blázquez
Keyword(s):  
Gastric Glands ◽  
High Affinity ◽  
Glucagon Like Peptide ◽  
Glucagon Like Peptide 1

Functional and structural characterization of the secretin receptors in rat gastric glands: Desensitization and glycoprotein nature

1991 ◽  
Vol 11 (1) ◽  
pp. 33-42 ◽  
Author(s):  
Wafa Bawab ◽  
Eric Chastre ◽  
Christian Gespach
Keyword(s):  
Binding Sites ◽  
Down Regulation ◽  
Gastric Glands ◽  
Physiological Concentration ◽  
Camp Generation ◽  
Secretin Receptor ◽  
Camp System ◽  
Glucagon Like Peptide ◽  
Glucagon Like Peptide 1

We have documented and characterized the down-regulation of the125I-secretin binding sites and the associated desensitization of the secretin receptor-cAMP system in rat gastric glands. Secretin induced a rapid decrease of the high-affinity125I-secretin binding sites with t1/2=30 min at 37°C. Half-maximal down-regulation and desensitization occurred at 10−9 M secretin, a physiological concentration corresponding to the half-maximal activation of the secretin receptor. The Scatchard parameters of the low-affinity125I-secretin binding sites were unaffected by the pretreatment. This desensitization is heterologous in view of the loss of responsiveness to the truncated glucagon-like peptide 1 (TGLP-1), and pharmacologically selective since the sectetin-related analogue VIP (10−7 M) does not alter the secretin-induced cAMP generation in rat gastric glands. The glycoprotein nature of the secretin receptor has also been demonstrated using WGA-agarose affinity chromatography of the solubilized125I-secretin receptor complex.

1969-P: Time-Based Internalized Characterization of Exendin-4-Based Glucagon-Like Peptide-1 Receptor-Targeting Imaging Probe

Diabetes ◽  
2019 ◽  
Vol 68 (Supplement 1) ◽  
pp. 1969-P
Author(s):  
TAKAAKI MURAKAMI ◽  
HIROYUKI FUJIMOTO ◽  
NAOTAKA FUJITA ◽  
KEITA HAMAMATSU ◽  
JUNJI FUJIKURA ◽  
...  
Keyword(s):  
Receptor Targeting ◽  
Imaging Probe ◽  
Glucagon Like Peptide ◽  
Glucagon Like Peptide 1

Structure/Activity Characterization of Glucagon-Like Peptide-1

1994 ◽  
Vol 225 (3) ◽  
pp. 1151-1156 ◽  
Author(s):  
Baptist Gallwitz ◽  
Maike Witt ◽  
Gabriele Paetzold ◽  
Corinna Morys-Wortmann ◽  
Bodo Zimmermann ◽  
...  
Keyword(s):  
Structure Activity ◽  
Glucagon Like Peptide ◽  
Glucagon Like Peptide 1

Presence and characterization of glucagon-like peptide-1(7-36) amide receptors in solubilized membranes of rat adipose tissue.

Endocrinology ◽  
1993 ◽  
Vol 132 (1) ◽  
pp. 75-79 ◽  
Author(s):  
I Valverde ◽  
E Mérida ◽  
E Delgado ◽  
M A Trapote ◽  
M L Villanueva-Peñacarrillo
Keyword(s):  
Adipose Tissue ◽  
Glucagon Like Peptide ◽  
Glucagon Like Peptide 1 ◽  
Rat Adipose Tissue

scholarly journals Dipeptidyl peptidases 8 and 9: specificity and molecular characterization compared with dipeptidyl peptidase IV

2006 ◽  
Vol 396 (2) ◽  
pp. 391-399 ◽  
Author(s):  
Jais R. Bjelke ◽  
Jesper Christensen ◽  
Per F. Nielsen ◽  
Sven Branner ◽  
Anders B. Kanstrup ◽  
...  
Keyword(s):  
Peptide Yy ◽  
Expression System ◽  
Baculovirus Expression System ◽  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv ◽  
Dipeptidyl Peptidases ◽  
Glucagon Like Peptide ◽  
Glucagon Like Peptide 1 ◽  
Dipeptidyl Peptidase Iv Inhibition

Dipeptidyl peptidases 8 and 9 have been identified as gene members of the S9b family of dipeptidyl peptidases. In the present paper, we report the characterization of recombinant dipeptidyl peptidases 8 and 9 using the baculovirus expression system. We have found that only the full-length variants of the two proteins can be expressed as active peptidases, which are 882 and 892 amino acids in length for dipeptidyl peptidase 8 and 9 respectively. We show further that the purified proteins are active dimers and that they show similar Michaelis–Menten kinetics and substrate specificity. Both cleave the peptide hormones glucagon-like peptide-1, glucagon-like peptide-2, neuropeptide Y and peptide YY with marked kinetic differences compared with dipeptidyl peptidase IV. Inhibition of dipeptidyl peptidases IV, 8 and 9 using the well-known dipeptidyl peptidase IV inhibitor valine pyrrolidide resulted in similar Ki values, indicating that this inhibitor is non-selective for any of the three dipeptidyl peptidases.

Somatostatin restrains the secretion of glucagon-like peptide-1 and -2 from isolated perfused porcine ileum

2000 ◽  
Vol 278 (6) ◽  
pp. E1010-E1018 ◽  
Author(s):  
Lene Hansen ◽  
Bolette Hartmann ◽  
Thue Bisgaard ◽  
Hitoshi Mineo ◽  
Peer N. Jørgensen ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Enteric Neurons ◽  
Adrenergic Blockade ◽  
Electrical Nerve Stimulation ◽  
High Affinity ◽  
Neuronal Regulation ◽  
Glucagon Like Peptide ◽  
Glucagon Like Peptide 1 ◽  
Local Release

Suspecting that paracrine inhibition might influence neuronal regulation of the endocrine L cells, we studied the role of somatostatin (SS) in the regulation of the secretion of the proglucagon-derived hormones glucagon-like peptide-1 and -2 (GLP-1 and GLP-2). This was examined using the isolated perfused porcine ileum stimulated with acetylcholine (ACh, 10− 6M), neuromedin C (NC, 10− 8 M), and electrical nerve stimulation (NS) with or without α-adrenergic blockade (phentolamine 10− 5 M), and perfusion with a high-affinity monoclonal antibody against SS. ACh and NC significantly increased GLP secretion, whereas NS had little effect. SS immunoneutralization increased GLP secretion eight- to ninefold but had little influence on the GLP responses to ACh, NC, and NS. Basal SS secretion (mainly SS28) was unaffected by NS alone. Phentolamine + NS and NC abstract strongly stimulated release mainly of SS14, whereas ACh had little effect. Infused intravascularly, SS14 weakly and SS28 strongly inhibited GLP secretion. We conclude that GLP secretion is tonically inhibited by a local release of SS28 from epithelial paracrine cells, whereas SS14, supposedly derived from enteric neurons, only weakly influences GLP secretion.

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