Neurotensin

Neurotensin
Identifiers
Symbols	NTS; NMN-125; NN; NT; NT/N; NTS1
External IDs	OMIM: 162650 MGI: 1328351 HomoloGene: 4506 GeneCards: NTS Gene
Gene Ontology Molecular function • neuropeptide hormone activity Cellular component • extracellular region • extracellular region • soluble fraction • transport vesicle • cytoplasmic vesicle Biological process • signal transduction • regulation of blood vessel size Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	4922	67405
Ensembl	ENSG00000133636	ENSMUSG00000019890
UniProt	P30990	Q9D3P9
RefSeq (mRNA)	NM_006183.4	NM_024435.2
RefSeq (protein)	NP_006174.1	NP_077755.1
Location (UCSC)	Chr 12: 86.27 – 86.28 Mb	Chr 10: 101.94 – 101.95 Mb
PubMed search	[1]	[2]

Neurotensin
Identifiers
CAS number	39379-15-2
PubChem	16129680
Properties
Molecular formula	C78H121N21O20
Molar mass	1672.92
Y (verify) (what is: Y/N?) Except where noted otherwise, data are given for materials in their standard state (at 25 °C, 100 kPa)
Infobox references

Neurotensin is a 13 amino acid neuropeptide that is implicated in the regulation of luteinizing hormone and prolactin release and has significant interaction with the dopaminergic system. Neurotensin was first isolated from extracts of bovine hypothalamus based on its ability to cause a visible vasodilation in the exposed cutaneous regions of anesthetized rats.^[1]

Structure

The sequence of bovine neurotensin was determined to be pyroGlu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Tyr-Ile-Leu-OH.^[2] Neurotensin is synthesized as part of a 169-170 amino acid precursor protein that also contains the related neuropeptide neuromedin N.^[3][4] The peptide coding domains are located in tandem near the carboxyl terminal end of the precursor and are bounded and separated by paired basic amino acid (lysine-arginine) processing sites.

Clinical significance

It has been associated with colorectal cancer.^[5]

Neurotensin has been implicated in the modulation of dopamine signaling, and produces a spectrum of pharmacological effects resembling those of antipsychotic drugs, leading to the suggestion that neurotensin may be an endogenous neuroleptic. Neurotensin-deficient mice display defects in responses to several antipsychotic drugs consistent with the idea that neurotensin signaling is a key component underlying at least some antipsychotic drug actions.^[6] These mice exhibit modest defects in prepulse inhibition (PPI) of the startle reflex, a model that has been widely used to investigate antipsychotic drug action in animals. Antipsychotic drug administration augments PPI under certain conditions. Comparisons between normal and neurotensin-deficient mice revealed striking differences in the ability of different antipsychotic drugs to augment PPI. While the atypical antipsychotic drug clozapine augmented PPI normally in neurotensin-deficient mice, the conventional antipsychotic haloperidol and the newer atypical antipsychotic quetiapine were ineffective in these mice, in contrast to normal mice where these drugs significantly augmented PPI. These results suggest that certain antipsychotic drugs require neurotensin for at least some of their effects. Neurotensin-deficient mice also display defects in striatal activation following haloperidol, but not clozapine administration in comparison to normal wild type mice, indicating that striatal neurotensin is required for the full spectrum of neuronal responses to a subset of antipsychotic drugs.^[7]

See also

• Neurotensin receptor

References

External links

• MeSH Neurotensin