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Somatostatin

Gloria Shaffer Tannenbaum, Jacques Epelbaum

10.1002/cphy.cp070509

Source: Supplement 24: Handbook of Physiology, The Endocrine System, Hormonal Control of Growth

Originally published: 1999

Published online: January 2011

Full Article on Wiley Online Library



Abstract

The sections in this article are:

1 Historical Background
1.1 Discovery in Hypothalamus
1.2 Multiple Sites of Origin
1.3 Plurality of Effects
1.4 Identification of Various Forms
2 Anatomical Distribution of Somatostatin Cells
2.1 Phytogeny
2.2 Distribution in Central Nervous System
2.3 Colocalizations
2.4 Ontogeny
3 Molecular Biology and Biosynthesis of Hypothalamic Somatostatin
3.1 Gene Structure and Chromosomal Localization
3.2 Post‐Translational Processing and Active Forms
3.3 Metabolism and Inactivation
3.4 Phytogeny of Somatostatin Peptides
4 Actions of Somatostatin
4.1 On Pituitary Gland
4.2 On Hypothalamus
4.3 On Somatic Growth
5 Somatostatin Receptors
5.1 Historical Background
5.2 Molecular Cloning of Somatostatin Receptor Genes
5.3 Molecular Pharmacology
5.4 Localization of Somatostatin Receptors in the Hypothalamo–Hypophysial Complex
5.5 Regulation of Somatostatin Receptor Gene Expression
6 Mechanisms of Action
7 Regulation of Somatostatin Secretion and Gene Expression
7.1 By Growth Hormone
7.2 By Insulin‐like Growth Factors
7.3 By Other Hormones
7.4 By Neurotransmitters, Neuropeptides, and Cytokines
7.5 By Growth Hormone Secretogogues
7.6 Autoregulation
7.7 Sexual Dimorphism
7.8 Nutritional and Metabolic Factors
7.9 Aging
8 Somatostatin Implications in Disease
8.1 Inhibition of Growth Hormone Secretion and Tumor‐Associated Symptoms in Acromegaly
8.2 In Vivo Imaging of Tumors
8.3 Diagnostic Efficacy in Growth Hormone Deficiency
9 Conclusion
Figure 1. Figure 1.

Schematic representation of the major neural and feedback regulatory components of the growth hormone (GH) neuroendocrine axis. See text for details of interactions between somatostatin (SRIF) and GH‐releasing hormone (GHRH) (both at the level of the pituitary gland and within the hypothalamus), and of the feedback effects of GH and the insulin‐like growth factors (IGFs) in GH regulation. PVN, periventricular nucleus; ARC, arcuate nucleus.
Figure 2. Figure 2.

Schematic localization of somatostatin‐and GHRH‐containing hypophysiotropic neurons, and photomicrographs of their in situ hybridization visualization in the rat hypothalamus. Hypophysiotropic neurons synthesizing somatostatin are located along the entire dorsoventral extent of the rostral periventricular nucleus as shown in the boxed coronal section (adapted from ref. 338). GHRH mRNA‐containing neurons are restricted to the ventrolateral portion of the arcuate nucleus in the medial part of the hypothalamus (see boxed area). These neurons are easily visualized by in situ hybridization using oligonucleotide probes (insets). GHRH neurons express much less peptide than the somatostatin neurons. AHA, anterior hypothalamic area; Arc, arcuate nucleus; DM, dorsomedial nucleus; f, fornix; LA, lateral hypothalamus; ME, median eminence; MTu, medial tuberal nucleus; OX, optic chiasma; Pa, paraventricular nucleus; Pe, periventricular nucleus; scn, suprachiasmatic nucleus; SO, supraoptic nucleus; VM, ventromedial nucleus; 3V, third ventricle.
Figure 3. Figure 3.

Schematic organization of the rat somatostatin gene. The coding region consists of two exons of 367 bp and 238 bp separated by an intron of 621 bp. A variant TATA box is located 26 bases upstream from the transcriptional initiation site. A cAMP responsive element (CRE)‐binding protein (CREB) can bind to the consensus CRE. A second enhancer called UE 1 is also located in the proximal part of the promoter region, and two islet transcription factors, ISL‐1 and a second one, called either ISF‐1, IDX‐1, or IPF‐1, can bind to UE 1 and enhance somatostatin transcription. Two additional homeodomain protein‐binding sequences, SMS‐TAAT1 (SMS 1) and SMS‐TTAT2 (SMS 2) are also located more distally. Finally, two proximal silencer elements (PS 1 and PS 2) are also located on the somatostatin gene. The glucocorticoid receptor (GR) activates somatostatin gene transcription, and a portion of the promoter (‐71 to −250 bp) is required for this effect (for further details, see text).
Figure 4. Figure 4.

Schematic description of preprosomatostatin post‐translational processing and metabolism in brain. The convertases Furin and PACE‐4 appear to be involved in the constitutive pathway to generate somatostatin‐28, while PC1 and/or PC2, which are concentrated in secretory vesicles, might be considered as somatostatin‐14 convertases. The cleavage of somatostatin‐28 to somatostatin‐14 and somatostatin‐28 [1–12] appears minimal in mammalian brain. The somatostatin peptides are degraded primarily by two enzymes, EC 24.15 and EC 24.16.
Figure 5. Figure 5.

Phylogenic comparison of the amino acid sequences of preprosomatostatin 1 and preprosomatostatin 2. Similarities between sequences were optimized by inserting gaps. Conserved amino acids as compared to human sequences are in bold. Somatostatin‐14 and cortistatin 14‐ or 17‐related sequences are underlined. Somatostatin‐28 and cortistatin‐29 are indicated by dotted lines. The degree of conservation among species is very high in the case of preprosomatostatin‐1 derived peptides, being total for the C‐terminal somatostatin‐14 sequence in all species. Over 95% of the entire sequence is conserved in mammals, more than 85% in birds and amphibians, and more than 40% in fishes. In contrast, the degree of conservation is limited in the case of preprosomatostatin‐2. The somatostatin‐like peptides are not totally conserved, and the degree of conservation reaches barely 30% between mammals and amphibians and 20% in fishes for the entire sequence. (Amino acid sequences are deduced from the cDNA sequences according to ref. 479 with the exception of rat [111] and human [157] cortistatins).
Figure 6. Figure 6.

Postulated ultradian rhythms of hypothalamic somatostatin and GHRH secretion into hypophysial portal blood, with the net result on pituitary GH release as observed in the peripheral circulation.
Figure 7. Figure 7.

Somatostatin sst2 receptor model depicting the pharmacological properties of the somatostatin receptor family. Important residues are outlined and their functions specified (see text for further details and references).
Figure 8. Figure 8.

Schematic drawing of the signaling pathway of the GH neuroendocrine axis for generation of the ultradian GH rhythm in the rat. From the hypothalamus, somatostatin (SRIF) and GHRH are released into the portal blood according to the concentration time courses indicated (approximately 3.3‐h intervals). At the pituitary, the reciprocal release patterns of GHRH and SRIF result in a GH profile in the circulation as shown. The feedback of GH on the release of SRIF is mediated via GH receptors on SRIF cells in the periventricular nucleus (PVN) of the hypothalamus, delayed by the time τ. SRIF is secreted both into the portal blood, and within the hypothalamus at the level of the arcuate nucleus (ARC), according to a partition coefficient denoted by γ. In the ARC, the GHRH neurons show an approximately 1‐h rhythm, the release being amplitude‐modulated (M) by SRIF. SRIF neurons are located in the ARC as well as the PVN, as suggested by the vertical dashed line dividing the hypothalamus (for further description of the model see reference 483).


Figure 1.

Schematic representation of the major neural and feedback regulatory components of the growth hormone (GH) neuroendocrine axis. See text for details of interactions between somatostatin (SRIF) and GH‐releasing hormone (GHRH) (both at the level of the pituitary gland and within the hypothalamus), and of the feedback effects of GH and the insulin‐like growth factors (IGFs) in GH regulation. PVN, periventricular nucleus; ARC, arcuate nucleus.



Figure 2.

Schematic localization of somatostatin‐and GHRH‐containing hypophysiotropic neurons, and photomicrographs of their in situ hybridization visualization in the rat hypothalamus. Hypophysiotropic neurons synthesizing somatostatin are located along the entire dorsoventral extent of the rostral periventricular nucleus as shown in the boxed coronal section (adapted from ref. 338). GHRH mRNA‐containing neurons are restricted to the ventrolateral portion of the arcuate nucleus in the medial part of the hypothalamus (see boxed area). These neurons are easily visualized by in situ hybridization using oligonucleotide probes (insets). GHRH neurons express much less peptide than the somatostatin neurons. AHA, anterior hypothalamic area; Arc, arcuate nucleus; DM, dorsomedial nucleus; f, fornix; LA, lateral hypothalamus; ME, median eminence; MTu, medial tuberal nucleus; OX, optic chiasma; Pa, paraventricular nucleus; Pe, periventricular nucleus; scn, suprachiasmatic nucleus; SO, supraoptic nucleus; VM, ventromedial nucleus; 3V, third ventricle.



Figure 3.

Schematic organization of the rat somatostatin gene. The coding region consists of two exons of 367 bp and 238 bp separated by an intron of 621 bp. A variant TATA box is located 26 bases upstream from the transcriptional initiation site. A cAMP responsive element (CRE)‐binding protein (CREB) can bind to the consensus CRE. A second enhancer called UE 1 is also located in the proximal part of the promoter region, and two islet transcription factors, ISL‐1 and a second one, called either ISF‐1, IDX‐1, or IPF‐1, can bind to UE 1 and enhance somatostatin transcription. Two additional homeodomain protein‐binding sequences, SMS‐TAAT1 (SMS 1) and SMS‐TTAT2 (SMS 2) are also located more distally. Finally, two proximal silencer elements (PS 1 and PS 2) are also located on the somatostatin gene. The glucocorticoid receptor (GR) activates somatostatin gene transcription, and a portion of the promoter (‐71 to −250 bp) is required for this effect (for further details, see text).



Figure 4.

Schematic description of preprosomatostatin post‐translational processing and metabolism in brain. The convertases Furin and PACE‐4 appear to be involved in the constitutive pathway to generate somatostatin‐28, while PC1 and/or PC2, which are concentrated in secretory vesicles, might be considered as somatostatin‐14 convertases. The cleavage of somatostatin‐28 to somatostatin‐14 and somatostatin‐28 [1–12] appears minimal in mammalian brain. The somatostatin peptides are degraded primarily by two enzymes, EC 24.15 and EC 24.16.



Figure 5.

Phylogenic comparison of the amino acid sequences of preprosomatostatin 1 and preprosomatostatin 2. Similarities between sequences were optimized by inserting gaps. Conserved amino acids as compared to human sequences are in bold. Somatostatin‐14 and cortistatin 14‐ or 17‐related sequences are underlined. Somatostatin‐28 and cortistatin‐29 are indicated by dotted lines. The degree of conservation among species is very high in the case of preprosomatostatin‐1 derived peptides, being total for the C‐terminal somatostatin‐14 sequence in all species. Over 95% of the entire sequence is conserved in mammals, more than 85% in birds and amphibians, and more than 40% in fishes. In contrast, the degree of conservation is limited in the case of preprosomatostatin‐2. The somatostatin‐like peptides are not totally conserved, and the degree of conservation reaches barely 30% between mammals and amphibians and 20% in fishes for the entire sequence. (Amino acid sequences are deduced from the cDNA sequences according to ref. 479 with the exception of rat [111] and human [157] cortistatins).



Figure 6.

Postulated ultradian rhythms of hypothalamic somatostatin and GHRH secretion into hypophysial portal blood, with the net result on pituitary GH release as observed in the peripheral circulation.



Figure 7.

Somatostatin sst2 receptor model depicting the pharmacological properties of the somatostatin receptor family. Important residues are outlined and their functions specified (see text for further details and references).



Figure 8.

Schematic drawing of the signaling pathway of the GH neuroendocrine axis for generation of the ultradian GH rhythm in the rat. From the hypothalamus, somatostatin (SRIF) and GHRH are released into the portal blood according to the concentration time courses indicated (approximately 3.3‐h intervals). At the pituitary, the reciprocal release patterns of GHRH and SRIF result in a GH profile in the circulation as shown. The feedback of GH on the release of SRIF is mediated via GH receptors on SRIF cells in the periventricular nucleus (PVN) of the hypothalamus, delayed by the time τ. SRIF is secreted both into the portal blood, and within the hypothalamus at the level of the arcuate nucleus (ARC), according to a partition coefficient denoted by γ. In the ARC, the GHRH neurons show an approximately 1‐h rhythm, the release being amplitude‐modulated (M) by SRIF. SRIF neurons are located in the ARC as well as the PVN, as suggested by the vertical dashed line dividing the hypothalamus (for further description of the model see reference 483).

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Article Title: Somatostatin
 

How to Cite

Gloria Shaffer Tannenbaum, Jacques Epelbaum. Somatostatin. Compr Physiol 2011, Supplement 24: Handbook of Physiology, The Endocrine System, Hormonal Control of Growth: 221-265. First published in print 1999. doi: 10.1002/cphy.cp070509