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{{PBB|geneid=4922}} {{Infobox_gene}}
{{Infobox protein family
| Symbol = Pro-NT_NN
| Name = Neurotensin/neuromedin N precursor
| image =
| width =
| caption = crystal structure of the vps10p domain of human sortilin/nts3 in complex with neurotensin
| Pfam = PF07421
| Pfam_clan =
| InterPro = IPR008055
| SMART =
| PROSITE =
| MEROPS =
| SCOP =
| TCDB =
| OPM family = 257
| OPM protein = 2oyv
| CAZy =
| CDD =
| PDB =
⚫ }}
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| InChI = 1/C78H121N21O20/c1-7-43(6)63(73(115)96-57(76(118)119)37-42(4)5)97-70(112)55(39-45-21-25-47(101)26-22-45)95-72(114)59-18-13-35-99(59)75(117)52(16-11-33-86-78(83)84)90-64(106)48(15-10-32-85-77(81)82)89-71(113)58-17-12-34-98(58)74(116)51(14-8-9-31-79)91-69(111)56(40-60(80)102)94-66(108)50(28-30-62(104)105)88-68(110)54(38-44-19-23-46(100)24-20-44)93-67(109)53(36-41(2)3)92-65(107)49-27-29-61(103)87-49/h19-26,41-43,48-59,63,100-101H,7-18,27-40,79H2,1-6H3,(H2,80,102)(H,87,103)(H,88,110)(H,89,113)(H,90,106)(H,91,111)(H,92,107)(H,93,109)(H,94,108)(H,95,114)(H,96,115)(H,97,112)(H,104,105)(H,118,119)(H4,81,82,85)(H4,83,84,86)/t43-,48-,49-,50-,51-,52-,53-,54-,55-,56-,57-,58-,59-,63-/m0/s1
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'''Neurotensin''' is a 13 ] ] that is implicated in the regulation of ] and ] release and has significant interaction with the ]. Neurotensin was first isolated from extracts of ] ] based on its ability to cause a visible ] in the exposed ] regions of anesthetized rats.<ref name="pmid4745447">{{cite journal | author = Carraway R, Leeman SE | title = The isolation of a new hypotensive peptide, neurotensin, from bovine hypothalami | journal = J. Biol. Chem. | volume = 248 | issue = 19 | pages = 6854–61 | year = 1973 | pmid = 4745447 | doi = | url = http://www.jbc.org/cgi/content/abstract/248/19/6854}}</ref> '''Neurotensin''' is a 13 ] ] that is implicated in the regulation of ] and ] release and has significant interaction with the ]. Neurotensin was first isolated from extracts of ] ] based on its ability to cause a visible ] in the exposed ] regions of anesthetized rats.<ref name="pmid4745447">{{cite journal |vauthors=Carraway R, Leeman SE | title = The isolation of a new hypotensive peptide, neurotensin, from bovine hypothalami | journal = J. Biol. Chem. | volume = 248 | issue = 19 | pages = 6854–61 | year = 1973 | doi = 10.1016/S0021-9258(19)43429-7 | pmid = 4745447 | url = http://www.jbc.org/cgi/content/abstract/248/19/6854| doi-access = free }}</ref>


Neurotensin is distributed throughout the central nervous system, with highest levels in the ], ] and ]. It induces a variety of effects, including ], ], and ]. It is also involved in ] of dopamine pathways. In the periphery, neurotensin is found in ]s of the small intestine, where it leads to ] and ] ], reduced ] secretion, and ] contraction.<ref name="pmid11811984">{{cite journal |vauthors=Friry C, Feliciangeli S, Richard F, Kitabgi P, Rovere C | title = Production of recombinant large proneurotensin/neuromedin N-derived peptides and characterization of their binding and biological activity | journal = Biochem. Biophys. Res. Commun. | volume = 290 | issue = 4 | pages = 1161–8 |date=February 2002 | pmid = 11811984 | doi = 10.1006/bbrc.2001.6308 }}</ref>
==Structure==

⚫ The sequence of bovine neurotensin was determined to be pyroGlu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Tyr-Ile-Leu-OH.<ref name="pmid1167549">{{cite journal | author = Carraway R, Leeman SE | title = The amino acid sequence of a hypothalamic peptide, neurotensin | journal = J. Biol. Chem. | volume = 250 | issue = 5 | pages = 1907–11 | year = 1975 | pmid = 1167549 | doi = | url = http://www.jbc.org/cgi/content/abstract/250/5/1907}}</ref> Neurotensin is synthesized as part of a 169-170 amino acid precursor protein that also contains the related neuropeptide ].<ref name="pmid3472221">{{cite journal | author = Dobner PR, Barber DL, Villa-Komaroff L, McKiernan C | title = Cloning and sequence analysis of cDNA for the canine neurotensin/neuromedin N precursor | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 84 | issue = 10 | pages = 3516–20 | year = 1987 | pmid = 3472221 | doi = 10.1073/pnas.84.10.3516| pmc = 304902 }}</ref><ref name="pmid2832414">{{cite journal | author = Kislauskis E, Bullock B, McNeil S, Dobner PR | title = The rat gene encoding neurotensin and neuromedin N. Structure, tissue-specific expression, and evolution of exon sequences | journal = J. Biol. Chem. | volume = 263 | issue = 10 | pages = 4963–8 | year = 1988 | pmid = 2832414 | doi = | url = http://www.jbc.org/cgi/content/abstract/263/10/4963}}</ref> The peptide coding domains are located in tandem near the ] end of the ] and are bounded and separated by paired basic ] (lysine-arginine) processing sites.
== Sequence and biosynthesis ==

Neurotensin shares significant sequence similarity in its 6 ] ]s with several other neuropeptides, including ] (which is derived from the same precursor). This C-terminal region is responsible for the full ], the ] portion having a modulatory role. The neurotensin/neuromedin N ] can also be processed to produce large 125–138 ] ] with the neurotensin or neuromedin N ] at their C terminus. These large peptides appear to be less potent than their smaller counterparts, but are also less sensitive to degradation and may represent endogenous, long-lasting ]s in a number of pathophysiological situations.

⚫ The sequence of bovine neurotensin was determined to be pyroGlu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Tyr-Ile-Leu-OH.<ref name="pmid1167549">{{cite journal | vauthors = Carraway R, Leeman SE | title = The amino acid sequence of a hypothalamic peptide, neurotensin | journal = J. Biol. Chem. | volume = 250 | issue = 5 | pages = 1907–11 | year = 1975 | doi = 10.1016/S0021-9258(19)41780-8 | pmid = 1167549 | doi-access = free }}</ref> Neurotensin is synthesized as part of a 169 or 170 amino acid precursor protein that also contains the related neuropeptide ].<ref name="pmid3472221">{{cite journal |vauthors=Dobner PR, Barber DL, Villa-Komaroff L, McKiernan C | title = Cloning and sequence analysis of cDNA for the canine neurotensin/neuromedin N precursor | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 84 | issue = 10 | pages = 3516–20 | year = 1987 | pmid = 3472221 | doi = 10.1073/pnas.84.10.3516| pmc = 304902 | bibcode = 1987PNAS...84.3516D | doi-access = free }}</ref><ref name="pmid2832414">{{cite journal | vauthors = Kislauskis E, Bullock B, McNeil S, Dobner PR | title = The rat gene encoding neurotensin and neuromedin N. Structure, tissue-specific expression, and evolution of exon sequences | journal = J. Biol. Chem. | volume = 263 | issue = 10 | pages = 4963–8 | year = 1988 | doi = 10.1016/S0021-9258(18)68881-7 | pmid = 2832414 | doi-access = free }}</ref> The peptide coding domains are located in tandem near the ] end of the ] and are bounded and separated by paired basic ] (lysine-arginine) processing sites.


==Clinical significance== ==Clinical significance==
⚫ It has been associated with ].<ref name="pmid17000667">{{cite journal |author=Wang X, Wang Q, Ives KL, Evers BM |title=Curcumin inhibits neurotensin-mediated interleukin-8 production and migration of HCT116 human colon cancer cells |journal=Clin. Cancer Res. |volume=12 |issue=18 |pages=5346–55 |year=2006 |pmid=17000667 |doi=10.1158/1078-0432.CCR-06-0968 |pmc=2613866}}</ref>


⚫ Neurotensin is a potent ] for ].<ref name="pmid17000667">{{cite journal |vauthors=Wang X, Wang Q, Ives KL, Evers BM | title = Curcumin inhibits neurotensin-mediated interleukin-8 production and migration of HCT116 human colon cancer cells | journal = Clin. Cancer Res. | volume = 12 | issue = 18 | pages = 5346–55 |date=September 2006 | pmid = 17000667 | pmc = 2613866 | doi = 10.1158/1078-0432.CCR-06-0968 }}</ref>
⚫ 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.<ref>{{cite journal | author = Kinkead, B, Dobner PR, Egnatashvili, V, Murray, T, Deitemeyer, N, Nemeroff, CB | title = Neurotensin-deficient mice have deficits in prepulse inhibition: restoration by clozapine but no haloperidol, olanzapine, or quetiapine | journal = J. Pharmacol. Exp. Ther. | volume = 315 | issue = 1 | pages = 256–264 | year = 2005 | pmid = 15987829 | doi = 10.1124/jpet.105.087437| url = http://jpet.aspetjournals.org/cgi/content/abstract/315/1/256}}</ref> 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.<ref>{{cite journal | author = Dobner, PR, Fadel, J, Deitemeyer, N, Carraway, RE, Deutch, AY | title = Neurotensin-deficient mice show altered responses to antipsychotic drugs | journal = Proc. Natl. Acad. Sci. USA | volume = 98 | issue = 14 | pages = 8048–8053 | year = 2001 | pmid = 11427716 | doi = 10.1073/pnas.141042198| url = http://www.pnas.org/content/98/14/8048 | pmc = 35465}}</ref>

⚫ Neurotensin has been implicated in the modulation of ] signaling, and produces a spectrum of pharmacological effects resembling those of ]s, leading to the suggestion that neurotensin may be an endogenous ]. 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.<ref>{{cite journal | author = Kinkead, B, Dobner PR, Egnatashvili, V, Murray, T, Deitemeyer, N, Nemeroff, CB | title = Neurotensin-deficient mice have deficits in prepulse inhibition: restoration by clozapine but no haloperidol, olanzapine, or quetiapine | journal = J. Pharmacol. Exp. Ther. | volume = 315 | issue = 1 | pages = 256–264 | year = 2005 | pmid = 15987829 | doi = 10.1124/jpet.105.087437| s2cid = 15095566 | url = http://jpet.aspetjournals.org/cgi/content/abstract/315/1/256}}</ref> These mice exhibit modest defects in ] (PPI) of the ], 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 ] and the newer atypical antipsychotic ] 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 ] 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.<ref>{{cite journal | author = Dobner, PR, Fadel, J, Deitemeyer, N, Carraway, RE, Deutch, AY | title = Neurotensin-deficient mice show altered responses to antipsychotic drugs | journal = Proc. Natl. Acad. Sci. USA | volume = 98 | issue = 14 | pages = 8048–8053 | year = 2001 | pmid = 11427716 | doi = 10.1073/pnas.141042198| pmc = 35465| bibcode = 2001PNAS...98.8048D | doi-access = free }}</ref>

Neurotensin is an endogenous neuropeptide involved in ] that can induce ] and ] in experimental models of ].<ref name="pmid15090966">{{cite journal |vauthors=Katz LM, Young A, Frank JE, Wang Y, Park K | title = Neurotensin-induced hypothermia improves neurologic outcome after hypoxic-ischemia | journal = Crit. Care Med. | volume = 32 | issue = 3 | pages = 806–10 |date=March 2004 | pmid = 15090966 | doi = 10.1097/01.CCM.0000114998.00860.FD | s2cid = 41533372 }}</ref>

== Gene expression ==
Neurotensin gene expression has been shown to be modulated by ] in both human SK-N-SH ] cell cultures as well as in mice through interactions with ] (cAMP) signaling. Specifically, estrogen increased cAMP activity and cAMP response element-binding protein ] in neuroblastoma cells prior to the induction of neurotensin gene ]. Additionally, neurotensin gene transcription was blocked in ] lacking the RIIβ subunit of the ] holoenzyme. These findings may indicate mechanisms of cross-talk signaling in brain hormone activity and expression of hormone-related genes.<ref>{{Cite journal|last1=Watters|first1=Jyoti J.|last2=Dorsa|first2=Daniel M.|date=1998-09-01|title=Transcriptional Effects of Estrogen on Neuronal Neurotensin Gene Expression Involve cAMP/Protein Kinase A-Dependent Signaling Mechanisms|url= |journal=Journal of Neuroscience|language=en|volume=18|issue=17|pages=6672–6680|doi=10.1523/JNEUROSCI.18-17-06672.1998|issn=0270-6474|pmc=6792960|pmid=9712639}}</ref> Other sex hormone-related changes in neurotensin expression have been associated with activity in the ]. In female rats, neurotensin expression was shown to be at its highest in the medial preoptic area (mPOA) during the proestrus phase of the ].<ref>{{Cite journal|last1=Smith|first1=Matthew J.|last2=Wise|first2=Phyllis M.|date=2001-07-01|title=Neurotensin Gene Expression Increases during Proestrus in the Rostral Medial Preoptic Nucleus: Potential for Direct Communication with Gonadotropin-Releasing Hormone Neurons*|journal=Endocrinology|volume=142|issue=7|pages=3006–3013|doi=10.1210/endo.142.7.8256|pmid=11416022|issn=0013-7227|doi-access=free}}</ref>

Altered expression of neurotensin genes as well as neurotensin receptor genes have been exhibited in postpartum female mice. While ] (Ntsr1) mRNA in the ] (PVN) was lowered, neurotensin, but not neurotensin mRNA, was shown to be higher in the PVN. Neurotensin mRNA as well as the peptide itself were also expressed higher in the medial preoptic area (mPOA). These expression patterns were not shown in the virgin female control group, and align with other research implicating neurotensin gene expression variation in the regulation of maternal behaviors.<ref>{{Cite journal|last1=Driessen|first1=Terri M.|last2=Zhao|first2=Changjiu|last3=Whittlinger|first3=Anna|last4=Williams|first4=Horecia|last5=Gammie|first5=Stephen C.|date=2014-01-08|title=Endogenous CNS Expression of Neurotensin and Neurotensin Receptors Is Altered during the Postpartum Period in Outbred Mice|journal=PLOS ONE|language=en|volume=9|issue=1|pages=e83098|doi=10.1371/journal.pone.0083098|issn=1932-6203|pmc=3885409|pmid=24416154|bibcode=2014PLoSO...983098D |doi-access=free}}</ref>

Other patterns of neurotensin expression related to the medial preoptic area show relation to the modulation of social reward. Analysis of neurotensin gene-labelled neurons revealed that neurotensin-containing neuronal projections from the mPOA to the ] (VTA) in mice were associated with the encoding of odor cues as well as social attraction, further implicating neurotensin in hormonal as well as reward signaling.<ref>{{Cite journal|last1=McHenry|first1=Jenna A.|last2=Otis|first2=James M.|last3=Rossi|first3=Mark A.|last4=Robinson|first4=J. Elliott|last5=Kosyk|first5=Oksana|last6=Miller|first6=Noah W.|last7=McElligott|first7=Zoe A.|last8=Budygin|first8=Evgeny A.|last9=Rubinow|first9=David R.|last10=Stuber|first10=Garret D.|date=March 2017|title=Hormonal gain control of a medial preoptic area social reward circuit|url= |journal=Nature Neuroscience|language=en|volume=20|issue=3|pages=449–458|doi=10.1038/nn.4487|issn=1546-1726|pmc=5735833|pmid=28135243}}</ref>

Neurotensin has also been implicated in learning processes. A study examining song development in male zebra finches showed variations in neurotensin and ] gene expression across different stages of song development. The early stage of transition between sensory and sensorimotor periods was marked by decreases in both neurotensin and neurotensin receptor mRNA expression, which may indicate a role of neurotensin in initiating sensorimotor learning. During the sensorimotor subsong stage, neurotensin gene expression and neurotensin receptor 1 (Ntsr1) gene expression exhibited complementary expression patterns in song-related brain regions, which may indicate changes in neuronal responses to neurotensin across development.<ref>{{Cite journal|last1=Merullo|first1=Devin P.|last2=Asogwa|first2=Chinweike N.|last3=Sanchez-Valpuesta|first3=Miguel|last4=Hayase|first4=Shin|last5=Pattnaik|first5=Bikash R.|last6=Wada|first6=Kazuhiro|last7=Riters|first7=Lauren V.|date=2018|title=Neurotensin and neurotensin receptor 1 mRNA expression in song-control regions changes during development in male zebra finches|url= |journal=Developmental Neurobiology|language=en|volume=78|issue=7|pages=671–686|doi=10.1002/dneu.22589|issn=1932-846X|pmc=6023781|pmid=29569407}}</ref>

Neurotensin also plays a role in peripheral tissues outside of the nervous system, mainly in the gastrointestinal tract, and has been implicated in cancer development. DNA promoter ] has been shown to be a major regulator in the expression of neurotensin receptor 1 and 2 genes in colorectal cancer cells. Additionally, knock-down of the NTSR1 gene as well as treatment with a NTSR1 ] inhibited colorectal cancer cell proliferation and migration.<ref>{{Cite journal|last1=Kim|first1=Ji Tae|last2=Weiss|first2=Heidi L.|last3=Evers|first3=B. Mark|date=2017-06-01|title=Diverse expression patterns and tumorigenic role of neurotensin signaling components in colorectal cancer cells|journal=International Journal of Oncology|volume=50|issue=6|pages=2200–2206|doi=10.3892/ijo.2017.3990|issn=1019-6439|pmc=5435327|pmid=28498396}}</ref> ]s or fibroid tumors in uterine tissue have also been associated with higher expression of neurotensin and NTSR1.<ref>{{Cite journal|last1=Rodríguez|first1=Yurena|last2=Almeida|first2=Teresa A.|last3=Valladares|first3=Francisco|last4=Báez|first4=Delia|last5=Montes de Oca|first5=Francisco|last6=García|first6=Candelaria|last7=Dorta|first7=Idaira|last8=Hernández|first8=Mariano|last9=Reyes|first9=Ricardo|last10=Bello|first10=Aixa R.|date=2010-10-01|title=Neurotensin and Neurotensin Receptor 1 Expression in Human Myometrium and Uterine Leiomyomas1|journal=Biology of Reproduction|volume=83|issue=4|pages=641–647|doi=10.1095/biolreprod.110.084962|pmid=20592307|issn=0006-3363|doi-access=free}}</ref>


==See also== ==See also==
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==References== ==References==
{{Reflist|2}} {{Reflist}}


==External links== ==External links==
* {{MeshName|Neurotensin}} * {{MeshName|Neurotensin}}
* {{Cite web |last=Saplakoglu |first=Yasemin |date=2022-09-07 |title=A Good Memory or a Bad One? One Brain Molecule Decides. |url=https://www.quantamagazine.org/a-good-memory-or-a-bad-one-one-brain-molecule-decides-20220907/|website=Quanta Magazine |language=en}}


{{Neuropeptides}} {{Neuropeptides}}
{{Neuropeptidergics}}

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