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Properties of the pituitary adenylate cyclase-activating polypeptide I and II receptors, vasoactive intestinal peptide1, and chimeric amino-terminal pituitary adenylate cyclase-activating polypeptide/vasoactive intestinal peptide1 receptors: evidence for multiple receptor states. 1996

J Van Rampelbergh, and P Gourlet, and P De Neef, and P Robberecht, and M Waelbroeck
Department of Biochemistry and Nutrition, Medical School, Université Libre de Bruxelles, Belgium.

We analyzed the functional and binding properties of the "normal" pituitary adenylate cyclase-activating polypeptide (N-PACAP) type I, PACAP type II/vasoactive intestinal peptide (VIP)1, and chimeric N-PACAP/VIP1 receptors expressed in Chinese hamster ovary cells. The binding properties of the three receptors were investigated using three radioiodinated tracers: 125I-VIP, 125I-PACAP-27, and 125I-PACAP-29 (125I-PACAP-27-Gly28,Lys29-amide). The three tracers labeled very different receptor densities; 125I-PACAP-29 labeled more receptors than either 125I-VIP or 125I-PACAP-27 in the three cell lines. Analysis of the competition curves suggested that the three tracers labeled in a different manner three PACAP I receptor states, two PACAP II/VIP1 receptor states, and three chimeric N-PACAP/VIP1 receptor states in transfected Chinese hamster ovary cells. The previously described PACAP1A and PACAP1B receptors, which differ by their affinities for PACAP-27 and PACAP-38, actually correspond to different PACAP I receptor states. The three receptors were able to increase adenylate cyclase activity when activated by PACAP-38, PACAP-27, or VIP. In contrast with the two parent receptors, the chimeric N-PACAP/VIP1 receptor was activated by PACAP-38 at lower concentrations than PACAP-27, suggesting that the amino-terminal and core receptor domains influence each other and that the conformation of one or both domains was altered in the chimeric compared with wild-type receptors. Comparison of the binding and functional properties of three clones expressing different chimeric N-PACAP/VIP1 receptors densities indicated that 125I-PACAP-29 was necessary to correctly estimate the receptor number and that 125I-PACAP-27 or 125I-VIP labeled only a fraction of the functional receptors. We suspect (but could not demonstrate) that this might also be true for PACAP I and PACAP II/VIP1 receptors.

UI MeSH Term Description Entries
D007457 Iodine Radioisotopes Unstable isotopes of iodine that decay or disintegrate emitting radiation. I atoms with atomic weights 117-139, except I 127, are radioactive iodine isotopes. Radioisotopes, Iodine
D007700 Kinetics The rate dynamics in chemical or physical systems.
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D010957 Plasmids Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS. Episomes,Episome,Plasmid
D011979 Receptors, Pituitary Hormone Cell surface proteins that bind pituitary hormones with high affinity and trigger intracellular changes influencing the behavior of cells. Since many pituitary hormones are also released by neurons as neurotransmitters, these receptors are also found in the nervous system. Pituitary Hormone Receptors,Receptors, Pituitary Hormones,Pituitary Hormones Receptors
D011993 Recombinant Fusion Proteins Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes. Fusion Proteins, Recombinant,Recombinant Chimeric Protein,Recombinant Fusion Protein,Recombinant Hybrid Protein,Chimeric Proteins, Recombinant,Hybrid Proteins, Recombinant,Recombinant Chimeric Proteins,Recombinant Hybrid Proteins,Chimeric Protein, Recombinant,Fusion Protein, Recombinant,Hybrid Protein, Recombinant,Protein, Recombinant Chimeric,Protein, Recombinant Fusion,Protein, Recombinant Hybrid,Proteins, Recombinant Chimeric,Proteins, Recombinant Fusion,Proteins, Recombinant Hybrid
D004789 Enzyme Activation Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme. Activation, Enzyme,Activations, Enzyme,Enzyme Activations
D006224 Cricetinae A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS. Cricetus,Hamsters,Hamster
D000262 Adenylyl Cyclases Enzymes of the lyase class that catalyze the formation of CYCLIC AMP and pyrophosphate from ATP. Adenyl Cyclase,Adenylate Cyclase,3',5'-cyclic AMP Synthetase,Adenylyl Cyclase,3',5' cyclic AMP Synthetase,AMP Synthetase, 3',5'-cyclic,Cyclase, Adenyl,Cyclase, Adenylate,Cyclase, Adenylyl,Cyclases, Adenylyl,Synthetase, 3',5'-cyclic AMP
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein

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