The novel VIP-like hypothalamic polypeptide PACAP interacts with high affinity receptors in the human neuroblastoma cell line NB-OK
- Universite Libre de Bruxelles (Belgium)
We investigated the ability of two forms of Pituitary Adenylate Cyclase Activating Polypeptide (PACAP-38, the 38 amino acid peptide isolated from ovine hypothalamus, and PACAP-27, a shorter N-terminal (1-27) amidated version) to interact with specific receptors in membranes from the human neuroblastoma cell line NB-OK. ({sup 125}I)PACAP-27 bound rapidly and specifically to one class of high affinity sites (Kd 0.5 nM). VIP inhibited ({sup 125}I)PACAP-27 binding 300- to 1000-fold less potently than PACAP-27 and PACAP-38. One microM PHI prevented tracer binding only partially and secretin, glucagon and GRF(1-29)NH2 were ineffective in this respect. PACAP-27 and PACAP-38 stimulated adenylate cyclase activity dose dependently and with similar efficacy (Kact 0.2-0.3 nM), this activation being compatible with the occupancy of specific high affinity PACAP receptor. VIP was markedly less potent and less efficient on this enzyme than PACAP. Chemical cross-linking of ({sup 125}I)PACAP-27 followed by SDS-PAGE and autoradiography revealed specific cross-linking with a 68 kDa protein.
- OSTI ID:
- 6324766
- Journal Information:
- Peptides (Fayetteville, New York); (USA), Vol. 11:4; ISSN 0196-9781
- Country of Publication:
- United States
- Language:
- English
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POLYPEPTIDES
RECEPTORS
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AFFINITY
AMINO ACID SEQUENCE
AUTORADIOGRAPHY
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ENZYME ACTIVITY
HYPOTHALAMUS
IODINE 125
MAN
TUMOR CELLS
ANIMAL CELLS
ANIMALS
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ELECTRON CAPTURE RADIOISOTOPES
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MAMMALS
MEMBRANE PROTEINS
MOLECULAR STRUCTURE
NERVOUS SYSTEM
NUCLEI
ODD-EVEN NUCLEI
ORGANIC COMPOUNDS
ORGANS
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PRIMATES
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550201* - Biochemistry- Tracer Techniques