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Neurotensin

Craig F. Ferris

10.1002/cphy.cp060223

Source: Supplement 17: Handbook of Physiology, The Gastrointestinal System, Neural and Endocrine Biology

Originally published: 1989

Published online: January 2011

Full Article on Wiley Online Library



Abstract

The sections in this article are:

1 Isolation
2 Structure
2.1 Sequencing After Enzymatic Digestion
2.2 Hydrolytic Deamidation: Glu‐ Versus Gln‐Neurotensin
3 Synthesis
4 Structure‐Function Relationships
4.1 Importance of Cooh‐Terminal Fragments for Receptor Binding and Biological Activity
4.2 Substitutions and Iodination of [Tyr11]Neurotensin
5 Receptors
5.1 Guinea Pig Small Intestine
5.2 Rat Fundus
5.3 Molecular Structure of Neurotensin Receptors
6 Radioimmunoassay
6.1 Radioiodination
6.2 Development and Use of Region‐Specific Antisera
6.3 Problems in the Radioimmunoassay of Plasma Neurotensin
6.4 Chromatographic and Immunochemical Identification of Neurotensin in Human and Rat Plasma
7 Neurotensin‐Related Peptides
7.1 Phylogenetic Variants
7.2 Intraspecies Variants
7.3 Tissue Precursors
8 Localization and Distribution of Neurotensin
8.1 Studies With Radioimmunoassay
8.2 Studies With Immunohistochemistry
8.3 Localization of Neurotensin in Tumors
9 Release and Circulation of Neurotensin
9.1 Release With Nutrients
9.2 Biphasic Release
9.3 Neurally Mediated Release
9.4 Peptide‐Stimulated Release
9.5 Somatostatin Inhibition of Release
9.6 In Vitro Models for Studying Release
9.7 Release Associated With Gastrointestinal Surgery
10 Metabolism of Neurotensin
11 Biology
11.1 Smooth Muscle Activity
11.2 Small Intestine Motility
11.3 Large Intestine Motility
11.4 Gastric Acid Secretion
11.5 Intestinal Absorption
11.6 Water and Electrolyte Secretion
11.7 Blood Flow
11.8 Pancreatic Function
12 Summary
Figure 1.

Complete amino acid sequence of neurotensin and alignment of fragments obtained by enzymatic cleavage. PCPase, pyrrolidone carboxyl peptidase; P, papain; P‐1, P‐2, P‐3, papain peptides.

Data from Carraway and Leeman 40
Figure 2.

Proposed model for neurotensin‐receptor interaction.

From Carraway and Leeman 42
Figure 3.

Diagrammatic representation of average binding sites for several region‐specific antisera toward neurotensin.

Courtesy of Robert Carraway.
Figure 4. Figure 4.

Gel‐permeation chromatography of bovine plasma extracts on Sephadex G‐25. Multiples of void volume (V0) and elution position for [3H]neurotensin (NT) are indicated. Aliquots of each fraction were assayed for NT with 3 antisera (PGL‐4, HC‐8, and TG‐1).

From Carraway et al. 37
Figure 5.

Chromatographic profiles of neurotensin‐like immunoreactivity from plasma collected at various time intervals before (0 min) and after 15,30,45,60, and 90 min) ingestion of a mixed meal by a healthy subject. Shaded areas, immunoreactivity obtained with COOH‐terminal‐directed antiserum; solid line, immunoreactivity obtained with NH2‐terminal‐directed antiserum. Arrows, elution position of synthetic neurotensin (NT) and neurotensin metabolite NT(1-8).

Data from Theodorsson‐Norheim and Rosell 184
Figure 6.

Arteriovenous difference in neurotensin (NT) concentration in extracted plasma during perfusion of small intestine with 0.9% NaCl or a micellar solution of oleic acid. Concentration of NT is given as mean ± SE (vertical bar) determined by high‐pressure liquid chromatography and radioimmunoassay (antiserum TG‐1) of extracted plasma samples taken simultaneously from superior mesenteric vein and femoral artery during saline or lipid perfusion (n = 3).

From Ferris et al. 58
Figure 7.

Concentration of neurotensin‐like immunoreactivity (NTLI) in intestinal tissues of representative vertebrates as measured with 3 region‐specific antisera. Average concentration measured in acetic acid extracts of small intestinal tissues as a function of animal class is plotted.

From Carraway et al. 47
Figure 8.

Gel‐permeation chromatography of extracts of mammalian whole brain and small intestine on Sephadex G‐25. Aliquots were assayed by using antisera PGL‐4 (○) and HC‐8 (•). Arrows, elution position for synthetic neurotensin and multiples of the void volume (V0). Number under each peak denotes approximate ratio of the measurements obtained with PGL‐4 to those obtained with HC‐8. Antiserum TG‐1 (data not shown) gave a major peak of immunoreactivity in each case, coincident on and about equal to that seen with HC‐8, peaking at tube 29.

From Carraway et al. 47
Figure 9.

Gel‐permeation chromatography of extracts of rat gastrointestinal tissues on Sephadex G‐25. Ordinate, immunoreactivity as measured with antisera PGL‐4, PGL‐6, and HC‐8. Arrows define lower limits of sensitivity in radioimmunoassay. Abscissa, fraction number, void volume (V0), and elution position for synthetic neurotensin (NT). Samples were acid/acetone extracts of rat tissues. Top, jejunoileum, 150g; bottom, stomach, 30g.

From Carraway and Leeman 43
Figure 10.

Average measurements of neurotensin‐like immunoreactivity (NTLI) at points sampled along small intestine of 4 subjects, determined with antisera HC‐8 (•), TG‐1 (▴), and PGL‐4 (○). Error bars, standard deviation of HC‐8 measurements. Samples consist of mucosa scraped from 12‐cm‐long segments of small intestine at ˜ 30‐cm intervals.

From Hammer et al. 86
Figure 11.

Neurotensin‐immunoreactive endocrine cells in different regions of small intestine of some mammalian species. A: basal portion of villus in dog duodenum. × 624. B: crypts in guinea pig duodenum, × 569. C: crypts in middle portion of human jejunum, × 806. D: villi of rat lower ileum exhibiting a particularly high amount of neurotensin‐immunoreactive cells. × 537.

From Reinecke 149
Figure 12.

Low magnification of ileal N cell of the primate Tupaia belangeri, which stained in adjacent semithin section with antineurotensin. Secretory granules (Sg) are clustered mostly at basal region.

From Helmstaedter et al. 90
Figure 13.

High‐pressure liquid chromatography on circulating metabolites of neurotensin (NT) obtained 2 min after intravenous injection of [3H]NT. Top: NT immunoreactivity expressed as real peptide concentrations by applying cross‐reactions of 20% [NT‐(1-8)], 60% [NT‐(1-11)], 2% [NT‐(19-13)], and 100% (NT). Bottom: 3H‐radioactivity.

From Aronin et al. 13
Figure 14.

Appearance of label in lymph over experimental period. Solid line, data for animals infused with NT (n = 11); dotted line, data for control animals infused with saline (n = 14). Data are expressed as percent of instilled [3H]oleic acid in counts per minute (cpm) recovered in lymph during each 15‐min collection period. Bars, SE.

From Armstrong et al. 11
Figure 15.

Plasma pancreatic polypeptide (PP) during infusions of neurotensin (2.3 ± 0.2 pmol/kg) (filled circles) and in saline controls (n = 5) (open circles).

From Blackburn et al. 26


Figure 1.

Complete amino acid sequence of neurotensin and alignment of fragments obtained by enzymatic cleavage. PCPase, pyrrolidone carboxyl peptidase; P, papain; P‐1, P‐2, P‐3, papain peptides.

Data from Carraway and Leeman 40


Figure 2.

Proposed model for neurotensin‐receptor interaction.

From Carraway and Leeman 42


Figure 3.

Diagrammatic representation of average binding sites for several region‐specific antisera toward neurotensin.

Courtesy of Robert Carraway.


Figure 4.

Gel‐permeation chromatography of bovine plasma extracts on Sephadex G‐25. Multiples of void volume (V0) and elution position for [3H]neurotensin (NT) are indicated. Aliquots of each fraction were assayed for NT with 3 antisera (PGL‐4, HC‐8, and TG‐1).

From Carraway et al. 37


Figure 5.

Chromatographic profiles of neurotensin‐like immunoreactivity from plasma collected at various time intervals before (0 min) and after 15,30,45,60, and 90 min) ingestion of a mixed meal by a healthy subject. Shaded areas, immunoreactivity obtained with COOH‐terminal‐directed antiserum; solid line, immunoreactivity obtained with NH2‐terminal‐directed antiserum. Arrows, elution position of synthetic neurotensin (NT) and neurotensin metabolite NT(1-8).

Data from Theodorsson‐Norheim and Rosell 184


Figure 6.

Arteriovenous difference in neurotensin (NT) concentration in extracted plasma during perfusion of small intestine with 0.9% NaCl or a micellar solution of oleic acid. Concentration of NT is given as mean ± SE (vertical bar) determined by high‐pressure liquid chromatography and radioimmunoassay (antiserum TG‐1) of extracted plasma samples taken simultaneously from superior mesenteric vein and femoral artery during saline or lipid perfusion (n = 3).

From Ferris et al. 58


Figure 7.

Concentration of neurotensin‐like immunoreactivity (NTLI) in intestinal tissues of representative vertebrates as measured with 3 region‐specific antisera. Average concentration measured in acetic acid extracts of small intestinal tissues as a function of animal class is plotted.

From Carraway et al. 47


Figure 8.

Gel‐permeation chromatography of extracts of mammalian whole brain and small intestine on Sephadex G‐25. Aliquots were assayed by using antisera PGL‐4 (○) and HC‐8 (•). Arrows, elution position for synthetic neurotensin and multiples of the void volume (V0). Number under each peak denotes approximate ratio of the measurements obtained with PGL‐4 to those obtained with HC‐8. Antiserum TG‐1 (data not shown) gave a major peak of immunoreactivity in each case, coincident on and about equal to that seen with HC‐8, peaking at tube 29.

From Carraway et al. 47


Figure 9.

Gel‐permeation chromatography of extracts of rat gastrointestinal tissues on Sephadex G‐25. Ordinate, immunoreactivity as measured with antisera PGL‐4, PGL‐6, and HC‐8. Arrows define lower limits of sensitivity in radioimmunoassay. Abscissa, fraction number, void volume (V0), and elution position for synthetic neurotensin (NT). Samples were acid/acetone extracts of rat tissues. Top, jejunoileum, 150g; bottom, stomach, 30g.

From Carraway and Leeman 43


Figure 10.

Average measurements of neurotensin‐like immunoreactivity (NTLI) at points sampled along small intestine of 4 subjects, determined with antisera HC‐8 (•), TG‐1 (▴), and PGL‐4 (○). Error bars, standard deviation of HC‐8 measurements. Samples consist of mucosa scraped from 12‐cm‐long segments of small intestine at ˜ 30‐cm intervals.

From Hammer et al. 86


Figure 11.

Neurotensin‐immunoreactive endocrine cells in different regions of small intestine of some mammalian species. A: basal portion of villus in dog duodenum. × 624. B: crypts in guinea pig duodenum, × 569. C: crypts in middle portion of human jejunum, × 806. D: villi of rat lower ileum exhibiting a particularly high amount of neurotensin‐immunoreactive cells. × 537.

From Reinecke 149


Figure 12.

Low magnification of ileal N cell of the primate Tupaia belangeri, which stained in adjacent semithin section with antineurotensin. Secretory granules (Sg) are clustered mostly at basal region.

From Helmstaedter et al. 90


Figure 13.

High‐pressure liquid chromatography on circulating metabolites of neurotensin (NT) obtained 2 min after intravenous injection of [3H]NT. Top: NT immunoreactivity expressed as real peptide concentrations by applying cross‐reactions of 20% [NT‐(1-8)], 60% [NT‐(1-11)], 2% [NT‐(19-13)], and 100% (NT). Bottom: 3H‐radioactivity.

From Aronin et al. 13


Figure 14.

Appearance of label in lymph over experimental period. Solid line, data for animals infused with NT (n = 11); dotted line, data for control animals infused with saline (n = 14). Data are expressed as percent of instilled [3H]oleic acid in counts per minute (cpm) recovered in lymph during each 15‐min collection period. Bars, SE.

From Armstrong et al. 11


Figure 15.

Plasma pancreatic polypeptide (PP) during infusions of neurotensin (2.3 ± 0.2 pmol/kg) (filled circles) and in saline controls (n = 5) (open circles).

From Blackburn et al. 26
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Article Title: Neurotensin
 

How to Cite

Craig F. Ferris. Neurotensin. Compr Physiol 2011, Supplement 17: Handbook of Physiology, The Gastrointestinal System, Neural and Endocrine Biology: 559-586. First published in print 1989. doi: 10.1002/cphy.cp060223