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|style="background: #F8EABA; text-align: center;" colspan="2"||Except where noted otherwise, data are given for|
materials in their standard state
(at 25 °C, 100 kPa)
Infobox disclaimer and 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.
The sequence of bovine neurotensin was determined to be pyroGlu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Tyr-Ile-Leu-OH. Neurotensin is synthesized as part of a 169-170 amino acid precursor protein that also contains the related neuropeptide neuromedin N. 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.
It has been associated with colorectal cancer.
References & Bibliography
- Carraway R, Leeman SE (1973). The isolation of a new hypotensive peptide, neurotensin, from bovine hypothalami. J. Biol. Chem. 248 (19): 6854–61.
- Carraway R, Leeman SE (1975). The amino acid sequence of a hypothalamic peptide, neurotensin. J. Biol. Chem. 250 (5): 1907–11.
- Dobner PR, Barber DL, Villa-Komaroff L, McKiernan C (1987). Cloning and sequence analysis of cDNA for the canine neurotensin/neuromedin N precursor. Proc. Natl. Acad. Sci. U.S.A. 84 (10): 3516–20.
- Kislauskis E, Bullock B, McNeil S, Dobner PR (1988). The rat gene encoding neurotensin and neuromedin N. Structure, tissue-specific expression, and evolution of exon sequences. J. Biol. Chem. 263 (10): 4963–8.
- Wang X, Wang Q, Ives KL, Evers BM (2006). Curcumin inhibits neurotensin-mediated interleukin-8 production and migration of HCT116 human colon cancer cells. Clin. Cancer Res. 12 (18): 5346–55.