Abstract
Almost half a century ago, in the first January 1973 issue of Science, the Roger Guillemin group in the Salk Institute (La Jolla, California), published a paper that proved the presence of a bioactive peptide in ovine hypothalamic extracts, with inhibitory effect in the secretion of immunoreactive growth hormone (GH). In the same paper, the structure of this 14-peptide was elucidated and its synthetic form was shown to elicit the same biological response in rats and humans, as well, hence its name: Somatostatin (SST) or Somatotropin-release inhibiting factor” (SRIF) [1]. SST belongs to the homonymous peptide family with cortistatin (CST). CST-17 is the bioactive cleavage product of a CST precursor peptide in humans, being a relatively recent addition. CST-17 shares common structural and functional features with SST (SST: SST-14 and SST-28 are the bioactive peptides, see Fig. 4.1), such as the depression of neuronal activity and some distinct properties as well, such as the activation of cation selective currents, not responsive to SST. It should be emphasized though, that these peptides (SST and CST) are the products of separate genes [3–5].
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Brazeau P, Vale W, Burgus R, et al. Hypothalamic polypeptide that inhibits the secretion of imunoreactive pituitary growth hormone. Science. 1973;179:77–9.
Weckbecker G, Lewis I, Albert R, et al. Opportunities in somatostatin research: biological, chemical and therapeutic aspects. Nat Rev Drug Discov. 2003;2:999–1017. https://doi.org/10.1038/nrd1255.
Bushberg JT, Seibert JA, Leid EM. The essential physics of medical imaging. 2nd ed. Philadelphia: Lippincott Williams & Wilkins; 2002.
De Lecea L, Criado JR, Prospero-Garcia O, et al. A cortical neuropeptide with neuronal depressant and sleep-modulating properties. Nature. 1996;381:242–5.
Gottero C, Prodam F, Destefanis S, et al. Cortistatin-17 and -14 exert the same endocrine activities as somatostatin in humans. Growth Hormon IGF Res. 2004;14:382–7.
IUPAC-IUB Common Biochem Nomenclature. An one-letter notation for amino acid sequences. Tentative rules. Biochemistry. 1968;7:2703–5. https://doi.org/10.1021/bi00848a001.
Elliott DE. Somatostatin. 2001. https://epdf.tips/somatostatin9b1681210755ce0bffeb5c27a17209b838154.html. Accessed 19 Oct 2018.
Bronstein-Sitton N. Somatostatin and the somatostatin receptors: versatile regulators of biological activity. 2018. https://www.alomone.com/article/somatostatin-somatostatin-receptors-versatile-regulators-biological-activity. Accessed 15 Oct 2018.
Barbieri F, Bajetto A, Pattarozzi A, et al. Peptide receptor targeting in cancer: the somatostatin paradigm. Int J Pept. 2013;2013:926295, 20 p. https://doi.org/10.1155/2013/926295.
Körner M, Reubi JC. Somatostatin. In: Kastin A, editor. Handbook of biologically active peptides. 1st ed. USA: Elsevier; 2006. p. 435–43.
Patel YC. Somatostatin and its receptor family. Front Neuroendocrinol. 1999;20:157–98.
Dalm DU, de Jong M. Comparing the use of radiolabeled SSTR agonists and an SSTR antagonist in breast cancer: does the model choice influence the outcome? EJNMMI Radiopharm Chem. 2017;2:11. https://doi.org/10.1186/s41181-017-0030-z.
Tulipano G, Schulz S. Novel insights in somatostatin receptor physiology. Eur J Endocrinol. 2007;156:S3–S11. https://doi.org/10.1530/eje.1.02354.
Reubi JC, Waser B, Mäcke H, et al. Highly increased 125I-JR11 antagonist binding in vitro reveals novel indications for sst2 targeting in human cancers. J Nucl Med. 2017;58:300–6. https://doi.org/10.2967/jnumed.116.177733.
Hubalewska-Dydejczyk A, Signore A, de Jong M, Dierckx RA, Buscombe J, van de Wiele C, editors. Somatostatin analogues: from research to clinical practice. Hoboken: Wiley; 2015.
Günther T, Tulipano G, Dournaud P, et al. International Union of Basic and Clinical Pharmacology. CV. Somatostatin receptors: structure, function, ligands, and new nomenclature. Pharmacol Rev. 2018;70:763–835. https://doi.org/10.1124/pr.117.015388.
Patel RC, Kumar U, Lamb DC, et al. Ligand binding to somatostatin receptors induces receptor-specific oligomer formation in live cells. Proc Natl Acad Sci U S A. 2002;99:3294–9. https://doi.org/10.1073/pnas.042705099.
Reubi JC, Schonbrunn A. Illuminating somatostatin analog action at neuroendocrine tumor receptors. Trends Pharmacol Sci. 2013;34:676–88. https://doi.org/10.1016/j.tips.2013.10.001.
Reubi JC, Waser B, Schaer J-C, et al. Somatostatin receptor sst1-sst5 expression in normal and neoplastic human tissues using receptor autoradiography with subtype-selective ligands. Eur J Nucl Med. 2001;28:836–46. https://doi.org/10.1007/s002590100541.
Csaba Z, Peineau S, Dournaud P. Molecular mechanisms of somatostatin receptor trafficking. J Mol Endocrinol. 2012;48:R1–R12.
Fani M, Nicolas GP, Wild D. Somatostatin receptor antagonists for imaging and therapy. J Nucl Med. 2017;58:61S–6S. https://doi.org/10.2967/jnumed.116.186783.
Hofland LJ, Lamberts SWJ. The pathophysiological consequences of somatostatin receptor internalization and resistance. Endocr Rev. 2003;24:28–47. https://doi.org/10.1210/er.2000-0001.
Zhang X, Kim K-M. Multifactorial regulation of G protein-coupled receptor endocytosis. Biomol Ther. 2017;25:26–43.
Hanyaloglu AC, von Zastrow M. Regulation of GPCRs by endocytic membrane trafficking and its potential implications. Annu Rev Pharmacol Toxicol. 2008;48:537–68. https://doi.org/10.1146/annurev.pharmtox.48.113006.
Breeman WA, de Jong M, Kwekkeboom DJ, et al. Somatostatin receptor-mediated imaging and therapy: basic science, current knowledge, limitations and future perspectives. Eur J Nucl Med. 2001;28:1421–9. https://doi.org/10.1007/s002590100502.
Fani M, Braun F, Waser B, et al. Unexpected sensitivity of sst2 antagonists to N-terminal radiometal modifications. J Nucl Med. 2012;53:1481–9. https://doi.org/10.2967/jnumed.112.102764.
Oshima N, Akizawa H, Kawashima H, et al. Redesign of negatively charged 111In-DTPA-octreotide derivative to reduce renal radioactivity. Nucl Med Biol. 2017;48:16–25.
Melis M, Krenning EP, Bernard BF, et al. Localisation and mechanism of renal retention of radiolabelled somatostatin analogues. Eur J Nucl Med Mol Imaging. 2005;32:1136–43. https://doi.org/10.1007/s00259-005-1793-0.
Fani M, Del Pozzo L, Abiraj K, et al. PET of somatostatin receptor-positive tumors using 64Cu- and 68Ga-somatostatin antagonists: the chelate makes the difference. J Nucl Med. 2011;52:1110–8. https://doi.org/10.2967/jnumed.111.087999.
Ginj M, Zhang H, Waser B, et al. Radiolabeled somatostatin receptor antagonists are preferable to agonists for in vivo peptide receptor targeting of tumors. Proc Natl Acad Sci U S A. 2006;103:16436–41. https://doi.org/10.1073/pnas.0607761103.
Kassis AI. Therapeutic radionuclides: biophysical and radiobiologic principles. Semin Nucl Med. 2008;38:358–66. https://doi.org/10.1053/j.semnuclmed.2008.05.002.
Kassis AI, Adelstein SJ. Considerations in the selection of radionuclides for cancer therapy. In: Welch MJ, Revanly CS, editors. Handbook of radiopharmaceuticals: Wiley; 2005. p. 767–93. https://doi.org/10.1002/0470846380.ch27.
Howel RW. Auger processes in the 21st century. Int J Radiat Biol. 2008;84:959–75. https://doi.org/10.1080/09553000802395527.
Duparc OH. Pierre Auger-Lise Meitner: comparative contributions to the Auger effect. Int J Mat Res (formerly Z Metallkd). 2009;100:1162–6. https://doi.org/10.3139/146.110163.
Feinendegen LE. Biological damage from the Auger effect, possible benefits. Radiat Environ Biophys. 1975;12:85–99.
Howell RW. Radiation spectra for Auger-electron emitting radionuclides: report No. 2 of AAPM Nuclear Medicine Task Group No. 6. Med Phys. 1992;19:1371–83. https://doi.org/10.1118/1.596927.
Lee BQ, Kibédi T, Stuchbery AE, et al. Atomic radiations in the decay of medical radioisotopes: a physics perspective. Comput Math Methods Med. 2012;2012:651475, 14 p. https://doi.org/10.1155/2012/651475.
McMillan DD, Maeda J, Bell JJ, et al. Validation of 64Cu-ATSM damaging DNA via high-LET Auger electron emission. J Radiat Res. 2015;56:784–91. https://doi.org/10.1093/jrr/rrv042.
Cornelissen B, Vallis KA. Targeting the nucleus: an overview of Auger-electron radionuclide therapy. Curr Drug Discov Technol. 2010;7:263–79. https://doi.org/10.2174/157016310793360657.
Falzone N, Cornelissen B, Vallis KA. Auger emitting radiopharmaceuticals for cancer therapy. In: Gómez-Tejedor G, Fuss M, editors. Radiation damage in biomolecular systems. Biological and medical physics, biomedical engineering. Dordrecht: Springer; 2012.
Piroozfar B, Raisali G, Alirezapour B, et al. The effect of 111In radionuclide distance and Auger electron energy on direct induction of DNA double strand breaks: a Monte Carlo study using Geant4-toolkit. Int J Radiat Biol. 2018;94(4):385–93. https://doi.org/10.1080/09553002.2018.1440329.
Bin Othman M, Mitry NR, Lewington VJ, et al. Re-assessing gallium-67 as a therapeutic radionuclide. Nucl Med Biol. 2017;46:12–8. https://doi.org/10.1016/j.nucmedbio.2016.10.008.
Thisgaard H. Accelerator based production of Auger-electron-emitting isotopes for radionuclide therapy. Dissertation, Risø National Laboratory for Sustainable Energy, Technical University of Denmark. 2008.
Thisgaard H, Jensen M. Sb-119: a potent Auger emitter for targeted radionuclide therapy. Med Phys. 2008;35:3839–46. https://doi.org/10.1118/1.2963993.
Stepanek J, Larsson B, Weinreich R. Auger-electron spectra of radionuclides for therapy and diagnostics. Acta Oncol. 1996;35:863–8. https://doi.org/10.3109/02841869609104038.
Fisher DR, Shen S, Meredith RF. MIRD dose estimate report No. 20: radiation absorbed-dose estimates for 111In- and 90Y-ibritumomab tiuxetan. J Nucl Med. 2009;50:644–52. https://doi.org/10.2967/jnumed.108.057331.
Lahiri S, Maiti M, Ghosh K. Production and separation of 111In: an important radionuclide in life sciences: a mini review. J Radioanal Nucl Chem. 2012;297:309–18. https://doi.org/10.1007/s10967-012-2344-3.
Schlyer DJ. Production of radionuclides in accelerators. In: Welch MJ, Redvanly CS, editors. Handbook of radiopharmaceuticals: radiochemistry and applications. Hoboken: Wiley; 2003. p. 1–71.
Kocher DC. Radioactive decay data tables. DOE/TIC-11026, 115. 1981.
Tuck DG. Critical survey of stability constants of complexes of indium. Pure Appl Chem. 1983;55:1477–528.
Anderson CJ, Welch MJ. Radiometal-labeled agents (non-technetium) for diagnostic imaging. Chem Rev. 1999;99:2219–34. https://doi.org/10.1021/cr980451q.
Dilworth JR, Pascu SI. The radiopharmaceutical chemistry of gallium (III) and indium (III) for SPECT imaging. In: Long N, Wong W-T, editors. The chemistry of molecular imaging. 1st ed: Wiley; 2015. p. 165–76. https://doi.org/10.2967/jnumed.110.075101.
Harrison RC. Indium chemistry in radiopharmaceutical development. In: Cox PH, Mather SJ, Sampson CB, Lazarus CR, editors. Progress in radiopharmacy. Leiden: Martinus Nijhoff Publishers; 1986. p. 173–96.
Liu S. The role of coordination chemistry in the development of target-specific radiopharmaceuticals. Chem Soc Rev. 2004;33:445–61. https://doi.org/10.1039/b309961j.
Martell AE, Hancock RD. Factors governing the formation of complexes with unidentate ligands in aqueous solution. Some general considerations. In: Metal complexes in aqueous solutions. Springer US; 1996. p. 15–61.
Vegt E, de Jong M, Wetzels JFM, et al. Renal toxicity of radiolabeled peptides and antibody fragments: mechanisms, impact on radionuclide therapy, and strategies for prevention. J Nucl Med. 2010;51:1049–58. https://doi.org/10.2967/jnumed.110.075101.
Deferm C, Onghena B, Hoogerstraete V, et al. Speciation of indium (III) chloro complexes in the solvent extraction process from chloride aqueous solutions to ionic liquids. Dalton Trans. 2017;46:4412–21. https://doi.org/10.1039/c7dt00618g.
Ferri D. Complex formation equilibriums between indium (III) and chloride ions. Acta Chem Scand. 1972;26:733–46.
Harris WR, Chen Y, Wein K. Equilibrium constants for the binding of indium (III) to human serum transferrin. Inorg Chem. 1994;33:4991–8.
Yeh SM, Meares CF, Goodwin DA. Decomposition rates of radiopharmaceutical indium chelates in serum. J Radioanal Chem. 1979;53:327–36. https://doi.org/10.1007/bf02517931.
Layne WW, Hnatowich DJ, Doherty PW, et al. Evaluation of the viability of In-111-labeled DTPA coupled to fibrinogen. J Nucl Med. 1982;23:627–30.
Hsieh W-Y, Liu S. Synthesis, characterization, and structures of indium In(DTPA-BA2) and yttrium Y(DTPA-BA2)(CH3OH) complexes (BA benzylamine): models for 111In- and 90Y-labeled DTPA-biomolecule conjugates. Inorg Chem. 2004;43:6006–14.
Narita H, Tanaka M, Shiwaku H, et al. Structural properties of the inner coordination sphere of indium chloride complexes in organic and aqueous solutions. Dalton Trans. 2014;43:1630–5. https://doi.org/10.1039/c3dt52474d.
Sun Y, Motekaitis RJ, Martell AE, et al. N,N′-bis(2-mercaptoethyl)ethylenediamine-N,N′-diacetic acid; an effective ligand for indium(III). Inorgan Chim Acta. 1995;228:77–9. https://doi.org/10.1016/0020-1693(94)04392-9.
Ivanova VY, Chevela VV, Bezryadin SG. Complex formation of indium (III) with citric acid in aqueous solution. Russ Chem Bull. 2015;64:1842–9. https://doi.org/10.1007/s11172-015-1082-4.
Silva AMN, Kong X, Parkin MC, et al. Iron (III) citrate speciation in aqueous solution. Dalton Trans. 2009;0:8616–25. https://doi.org/10.1039/b910970f.
Thompson LCA, Pacer R. The solubility of indium hydroxide in acidic and basic media at 25°C. J Inorg Nucl Chem. 1963;25:1041–4. https://doi.org/10.1016/0022-1902(63)80039-1.
Maloney TJ, Camp AE Jr. Purification of indium 111. US Patent 6,162,648, 19 Dec 2000. 2000.
Brom M, Joosten L, Oyen WJG, et al. Improved labelling of DTPA- and DOTA conjugated peptides and antibodies with 111In in HEPES and MES buffer. EJNMMI Res. 2012;2:4. https://doi.org/10.1186/2191-219X-2-4.
Balon HR, Brown TLY, Goldsmith SJ, et al. The SNM practice guideline for somatostatin receptor scintigraphy 2.0. J Nucl Med Technol. 2011;39:317–24.
Limouris GS, Chatziioannou A, Kontogeorgakos D, et al. Selective hepatic arterial infusion of In-111-DTPA-Phe1-octreotide in neuro-endocrine liver metastases. Eur J Nucl Med Mol Imaging. 2008;35:1827–37.
OctreoScan™ package insert, Petten, The Netherlands, Mallinckrodt Medical B.V. September 2017 (revision).
Bakker WH, Albert R, Bruns C, et al. [111In-DTPA-D-Phe1]-octreotide, a potential radiopharmaceutical for imaging of somatostatin receptor-positive tumors: synthesis, radiolabeling and in vitro validation. Life Sci. 1991;49:1583–91. https://doi.org/10.1016/0024-3205(91)90052-d.
Maecke HR, Riesen A, Ritter W. The molecular structure of indium-DTPA. J Nucl Med. 1989;30:1235–1.
Siddons CJ. Metal ion complexing properties of amide donating ligands. Dissertation, University of North Carolina at Wilmington. 2004.
Bavelaar BM, Lee BQ, Gill MR, et al. Subcellular targeting of theranostic radionuclides. Front Pharmacol. 2018;9:996. https://doi.org/10.3389/fphar.2018.00996.
Capello A, Krenning EP, Wout AP, et al. Peptide receptor radionuclide therapy in vitro using [111In-DTPA0]-octreotide. J Nucl Med. 2003;44:98–104.
Reubi JC. Peptide receptors as molecular targets for cancer diagnosis and therapy. Endocr Rev. 2003;24:389–427. https://doi.org/10.1210/er.2002-0007.
Reubi JC, Schär J-C, Waser B, et al. Affinity profiles for human somatostatin receptor subtypes SST1–SST5 of somatostatin radiotracers selected for scintigraphic and radiotherapeutic use. Eur J Nucl Med. 2000;27:273–82. https://doi.org/10.1007/s002590050034.
van Essen M, Sundin A, Krenning EP. Neuroendocrine tumours: the role of imaging for diagnosis and therapy. Nat Rev Endocrinol. 2014;10:102–14. https://doi.org/10.1038/nrendo.2013.246.
Mariani G, Bodei L, Adelstein SJ, et al. Emerging roles for radiometabolic therapy of tumors based on auger electron emission. J Nucl Med. 2000;41:1519–21.
Eckelman WC, Frank JA, Brechbiel M. Theory and practice of imaging saturable binding sites. Invest Radiol. 2002;37:101–6.
Gokce A, Nakamura RM, Tubis M, et al. Synthesis of indium-labeled antibody-chelate conjugates for radioassays. Int J Nucl Med Biol. 1982;9:85–95. https://doi.org/10.1016/0047-0740(82)90034-1.
Jonard P, Jamar F, Walrand S. Effect of peptide amount on biodistribution of Y-86-DOTA-Tyr3-octreotide (SMT487). J Nucl Med. 2000;41:260 p.
Breeman DWAP, Kwekkeboom DJ, Kooij PPM, et al. Effect of dose and specific activity on tissue, distribution of indium-111-pentetreotide in rats. J Nucl Med. 1995;36:623–7.
Wout AP, Breeman D, Kwekkeboom J, et al. Effect of dose and specific activity on tissue, distribution of indium-111-pentetreotide in rats. J Nucl Med. 1995;36:623–7.
Lewis JS, Lewis MR, Cutler PD, et al. Radiotherapy and dosimetry of 64Cu-TETA-Tyr3-octreotate in a somatostatin receptor-positive, tumor-bearing rat model. Clin Cancer Res. 1999;11:3608–16. https://doi.org/10.1158/1078-0432.CCR-04-1084.
Kwekkeboom J, Bakker DH, Kooij WP, et al. [177Lu-DOTA0-Tyr3]-octreotate: comparison with [111In-DTPA0]-octreotide in patients. Eur J Nucl Med. 2001;28:1319–25.
Akizawa H, Arano Y, Mifune M. Effect of molecular charges on renal uptake of 111In-DTPA-conjugated peptides. Nucl Med Biol. 2001;28:761–8.
Christensen EI, Birn H. Megalin and cubilin: multifunctional endocytic receptors. Nat Rev Mol Cell Biol. 2002;3:258–67. https://doi.org/10.1038/nrm778.
De Jong M, Barone R, Krenning E, et al. Megalin is essential for renal proximal tubule reabsorption of [111In-DTPA0]-Octreotide. J Nucl Med. 2005;46:1696–700.
Dong C, Zhao H, Yang S, et al. 99mTc-labeled dimeric octreotide peptide: a radiotracer with high tumor uptake for single-photon emission computed tomography imaging of somatostatin receptor subtype 2-positive tumors. Mol Pharm. 2013;10:2925–33. https://doi.org/10.1021/mp400040z.
Chen P, Wang J, Hope K, et al. Nuclear localizing sequences promote nuclear translocation and enhance the radiotoxicity of the anti-CD33 monoclonal antibody HuM195 labeled with 111In in human myeloid leukemia cells. J Nucl Med. 2006;47:827–36.
Ginj M, Hinni K, Tschumi S, et al. Trifunctional somatostatin-based derivatives designed for targeted radiotherapy using Auger electron emitters. J Nucl Med. 2005;46:2097–103.
Hillyar C. Auger electron radionuclide therapy utilizing F3 peptide to target the nucleolus. Dissertation, Jesus College, University of Oxford. 2015.
Cornelissen B, Able S, Kersemans V, et al. Nanographene oxide-based radioimmunoconstructs for in vivo targeting and SPECT imaging of HER2-positive tumors. Biomaterials. 2013;34:1146–54. https://doi.org/10.1016/j.biomaterials.2012.10.054.
Kersemans V, Kersemans K, Cornelissen B. Cell penetrating peptides for in vivo molecular imaging applications. Curr Pharm Des. 2008;14:2415–27. https://doi.org/10.2174/138161208785777432.
Nayak TK, Atcher RW, Prossnitz ER, et al. Enhancement of somatostatin-receptor-targeted 177Lu-[DOTA0-Tyr3]-octreotide therapy by gemcitabine pretreatment-mediated receptor uptake, up-regulation and cell cycle modulation. Nucl Med Biol. 2008;35:673–8. https://doi.org/10.1016/j.nucmedbio.2008.05.003.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2021 Springer Nature Switzerland AG
About this chapter
Cite this chapter
Zanglis, A. (2021). [111In-DTPA0-D-Phe1]-Octreotide: The Ligand—The Receptor—The Label. In: Limouris, G.S. (eds) Liver Intra-arterial PRRT with 111In-Octreotide. Springer, Cham. https://doi.org/10.1007/978-3-030-70773-6_4
Download citation
DOI: https://doi.org/10.1007/978-3-030-70773-6_4
Published:
Publisher Name: Springer, Cham
Print ISBN: 978-3-030-70772-9
Online ISBN: 978-3-030-70773-6
eBook Packages: MedicineMedicine (R0)