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Two functionally distinct cholecystokinin receptors show different modes of action on Ca2+ mobilization and phospholipid hydrolysis in isolated rat pancreatic acini. Studies using a new…
Identification of the Receptor Subtype Involved in the Analgesic Effect of Neurotensin
It is confirmed that NTR1 is involved in the NT-elicited turning behavior and demonstrated that the NTR2 mediates NT-induced analgesia, and a close correlation between the analgesic potency of NT analogs and their affinity for the N TR2 was revealed.
Identification of Two Amino Acids of the Human Cholecystokinin-A Receptor That Interact with the N-terminal Moiety of Cholecystokinin*
- K. Kennedy, V. Gigoux, D. Fourmy
- Biology, ChemistryThe Journal of Biological Chemistry
- 31 January 1997
The modeling of the CCK-A receptor and the docking of the peptide agonists indicated that their N terminus was connected to the receptor through a strong bond network involving Trp-39 and Gln-40 thus confirming experimental data, an important step toward the complete delineation of the agonist binding site.
A new CCK analogue differentiates two functionally distinct CCK receptors in rat and mouse pancreatic acini.
- T. Matozaki, J. Martinez, J. Williams
- Biology, ChemistryThe American journal of physiology
- 1 October 1989
The results support the concept that occupancy of distinct affinity sites or states of the CCK receptor is associated with specific biological actions and a model of the CCP receptor is proposed in which two interchangeable affinity states exist.
Structure-activity relationship studies on cholecystokinin: analogues with partial agonist activity.
The findings indicate that the aromatic ring of phenylalanine is important for the binding to brain and pancreatic CCK receptors, whereas the C-terminal primary amide function is not essential for thebinding to pancreaticCCK receptors but is crucial for biological activity of rat pancreatic acini.
CCK-JMV-180: a peptide that distinguishes high-affinity cholecystokinin receptors from low-affinity cholecystokinin receptors.
Melanin-concentrating hormone binding sites in human SVK14 keratinocytes.
- J. Burgaud, R. Poosti, J. Fehrentz, J. Martinez, J. Nahon
- Biology, ChemistryBiochemical and biophysical research…
- 29 December 1997
The widespread expression of MCH binding sites on mammalian cells, particularly on skin carcinoma cells is revealed, however, the low affinity of these sites for the native MCH and MCH-related peptides as well as competitivity with ANP and CNP indicates that further biochemical and functional characterizations are needed to validate them as genuine physiological MCH receptors.
Arginine 336 and Asparagine 333 of the Human Cholecystokinin-A Receptor Binding Site Interact with the Penultimate Aspartic Acid and the C-terminal Amide of Cholecystokinin*
The identified interactions are crucial for stabilizing the high affinity phospholipase C-coupled state of the CCK-AR·CCK complex, and Arg-336 and Asn-333 are directly involved in interactions with nonpeptide antagonists SR-27,897 and L-364,718.
A synthetic peptide derivative that is a cholecystokinin receptor antagonist.
Receptor occupation, calcium mobilization, and amylase release in pancreatic acini: effect of CCK-JMV-180.
- S. Sato, H. A. Stark, J. Martinez, M. Beaven, R. Jensen, J. Gardner
- BiologyThe American journal of physiology
- 1 August 1989
Analysis of the relationship between receptor occupation and calcium mobilization caused by CCK-8 andCCK-JMV-180 in combination indicates that calcium mobilization is caused by occupation of low-affinity CCK receptors.