The CCK(-like) receptor in the animal kingdom: Functions, evolution and structures
In this review, the cholecystokinin (CCK)(-like) receptors throughout the animal kingdom are compared on the level of physiological functions, evolutionary basis and molecular structure. In vertebrates, the CCK receptor is an important member of the G-protein coupled receptors as it is involved in t...
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Published in | Peptides (New York, N.Y. : 1980) Vol. 32; no. 3; pp. 607 - 619 |
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Main Authors | , , , , , , |
Format | Journal Article Conference Proceeding Web Resource |
Language | English |
Published |
New York, NY
Elsevier Inc
01.03.2011
Elsevier |
Subjects | |
Online Access | Get full text |
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Summary: | In this review, the cholecystokinin (CCK)(-like) receptors throughout the animal kingdom are compared on the level of physiological functions, evolutionary basis and molecular structure. In vertebrates, the CCK receptor is an important member of the G-protein coupled receptors as it is involved in the regulation of many physiological functions like satiety, gastrointestinal motility, gastric acid secretion, gall bladder contraction, pancreatic secretion, panic, anxiety and memory and learning processes. A homolog for this receptor is also found in nematodes and arthropods, called CK receptor and sulfakinin (SK) receptor, respectively. These receptors seem to have evolved from a common ancestor which is probably still closely related to the nematode CK receptor. The SK receptor is more closely related to the CCK receptor and seems to have similar functions. A molecular 3D-model for the CCK receptor type 1 has been built together with the docking of the natural ligands for the CCK and SK receptors in the CCK receptor type 1. These molecular models can help to study ligand–receptor interactions, that can in turn be useful in the development of new CCK(-like) receptor agonists and antagonists with beneficial health effects in humans or potential for pest control. |
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Bibliography: | http://dx.doi.org/10.1016/j.peptides.2010.11.025 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 ObjectType-Article-2 ObjectType-Feature-3 ObjectType-Review-1 ObjectType-Feature-1 scopus-id:2-s2.0-79951516283 |
ISSN: | 0196-9781 1873-5169 1873-5169 |
DOI: | 10.1016/j.peptides.2010.11.025 |