Abstract
Recent binding studies in the central nervous system and other tissues provide evidence that the mammalian bombesin-like peptides, gastrin-releasing peptide (GRP) and neuromedin-B (NMB), exert their numerous physiological effects through at least two different receptors. We describe the structure and expression of a cloned NMB-preferring bombesin receptor (NMB-R) with properties distinct from a GRP-preferring bombesin receptor (GRP-R) reported previously. In particular, the NMB-R shows higher affinity binding to NMB than to GRP in BALB 3T3 fibroblasts expressing the cloned NMB-R. The distinct regional distribution of NMB-R and GRP-R mRNA in the brain suggests that both bombesin receptor subtypes play independent roles in mediating many of the dramatic effects of bombesin-like peptides in the central nervous system.
MeSH terms
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Amino Acid Sequence
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Animals
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Base Sequence
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Brain / cytology
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Brain / metabolism
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Brain / ultrastructure
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Central Nervous System / cytology
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Central Nervous System / metabolism
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Central Nervous System / ultrastructure
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DNA / analysis
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DNA / genetics*
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DNA / metabolism
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Fibroblasts / cytology
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Fibroblasts / metabolism
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Fibroblasts / ultrastructure
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Gastrin-Releasing Peptide
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Gene Expression
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Mice
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Mice, Inbred BALB C
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Molecular Sequence Data
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Neurokinin B / analogs & derivatives*
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Neurokinin B / metabolism
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Neurokinin B / physiology
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Nucleic Acid Hybridization
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Peptides / metabolism
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Peptides / physiology
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RNA, Messenger / genetics
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RNA, Messenger / metabolism
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Receptors, Bombesin
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Receptors, Neurokinin-3
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Receptors, Neurotransmitter / drug effects
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Receptors, Neurotransmitter / genetics
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Receptors, Neurotransmitter / metabolism*
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Receptors, Neurotransmitter / physiology
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Transfection
Substances
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Peptides
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RNA, Messenger
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Receptors, Bombesin
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Receptors, Neurokinin-3
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Receptors, Neurotransmitter
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Gastrin-Releasing Peptide
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Neurokinin B
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neuromedin B
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DNA