Adipokinetic hormone

Adipokinetic hormones (AKHs) are metabolic neuropeptides, mediating mobilization of energy substrates in many insects.[1]

History

An English group first purified AKH in 1976. The chemical structure was determined to be a peptide hormone formed from 10 amino acids. This was the first insect peptide hormone to be identified.[2] After AKH was identified in cockroaches, locust AKH was inserted into a cockroach. A similar increase in lipid mobilization was observed. Conversely, cockroach AKH led to similar activity within a locust.[2] AKH was initially discovered in the locusts Locusta migratoria and Schistocerca gregaria. It is generally associated with aiding flight.[3] Lipids are transported from the hemolymph and metabolized by flight muscle in order to maintain flight. However, a high concentration of lipids remains in the hemolymph, implying that an agent may be responsible for activating lipid transport into the hemolymph. This was thought most likely to be a function of hormonal regulation.[2] The hormone itself is part of a larger family, often referred to as red pigment concentrating hormones (RPCH) discovered in crustaceans.[4] The consensus nomenclature is based on the name of the species in which the hormone was discovered and validated[5].

Sequence

More than 100 AKH sequences are known. The typical makeup of hormones in this family includes a length between 8 and 10 amino acids, blocked N (pyroglutamic acid) and C (amidation) termini, with hydrophic residues at position 2, asparagine or threonine at position 3, phenylalanine or tyrosine at position 4, and serine or threonine at position 5.[3][6] AKH sequence characteristics also include tryptophan at position 8 and in about two-thirds of the known AKHs, proline at position 6.[7][8] AKHs can be modified (C-mannosylated tryptophan[9], proline hydroxylation[10], threonine phosphorylation[11], possible proline isomerisation[12], threonine O-sulfonation[13]). Mass spectrometry is increasingly used for de novo sequencing of these hormones.[14][15][16][17] Sequence prediction from genomic and transcriptomic data assist in hormone identification [18][19][20]. AKH sequences differ slightly in insect families (Scarabaeoidea[21], Cucujiformia[22], Lepidoptera[23], Diptera[24], Hemiptera[25], Polyphaga[26]).

Significance

AKH has become an important area of study, particularly in insect crop pests and insects that act as intermediate or vector hosts for parasites that can affect humans or animals [27][28]. In experiments where locusts were injected with AKH and lipopolysaccharide (LPS–an immune elicitor found in the cell walls of bacteria) a stronger immune response was observed than in locusts that only received an LPS injection.[29][30] The spread of malaria by the female mosquito, Anopheles gambiae, is partly dependent on the adipokinetic hormone, Anoga-HrTH (pGlu-Leu-Thr-Phe-Thr-Pro-Ala-Trp-NH2). No crystal structure of this important neuropeptide is available. The NMR restrained molecular dynamic was used to investigate its conformational space in aqueous solution and when bound to a membrane surface. The results showed that Anoga-HrTH has an almost cyclic conformation that is stabilized by a hydrogen bond between the C-terminus and Thr3. When the agonist docks to its receptor, this H-bond is broken and the molecule adopts a more extended structure. Preliminary AKHR docking calculations give the free energy of binding to be −47.30 kJ/mol. Information about the 3D structure and binding mode of Anoga-HrTH to its receptor are vital for the design of suitable mimetics which can act as insecticides.[31]

Literature

  • "AKH: A hormone for all seasons?". Advances in invertebrate (neuro)endocrinology : a collection of reviews in the post-genomic era. Oakville, ON, Canada: Apple Academic Press. 2020. p. 129. ISBN 9780429264450.

References

  1. ↑ "AKH: A hormone for all seasons?". Advances in invertebrate (neuro)endocrinology : a collection of reviews in the post-genomic era. Oakville, ON, Canada: Apple Academic Press. 2020. p. 129. ISBN 9780429264450.
  2. 1 2 3 "Chapter Eleven - HEMOLYMPH TRANSPORT OF METABOLITES: ENDOCRINE REGULATION". June 7, 2008. Archived from the original on 2008-06-07.
  3. 1 2 Stone, Judith V.; Mordue, William; Batley, Karen E.; Morris, Howard R. (September 1976). "Structure of locust adipokinetic hormone, a neurohormone that regulates lipid utilisation during flight". Nature. 263 (5574): 207–211. Bibcode:1976Natur.263..207S. doi:10.1038/263207a0. ISSN 0028-0836. PMID 958472. S2CID 4226013.
  4. ↑ Marco, Heather G.; Glendinning, Susan; Ventura, Tomer; Gäde, Gerd (1 September 2024). "The gonadotropin-releasing hormone (GnRH) superfamily across Pancrustacea/Tetraconata: A role in metabolism?". Molecular and Cellular Endocrinology. 590 112238. doi:10.1016/j.mce.2024.112238. ISSN 1872-8057. PMID 38616035.
  5. ↑ Coast, Geoffrey M.; Schooley, David A. (March 2011). "Toward a consensus nomenclature for insect neuropeptides and peptide hormones". Peptides. 32 (3): 620–631. doi:10.1016/j.peptides.2010.11.006. ISSN 1873-5169. PMID 21093513.
  6. ↑ "AKH: A hormone for all seasons?". Advances in invertebrate (neuro)endocrinology : a collection of reviews in the post-genomic era. Oakville, ON, Canada: Apple Academic Press. 2020. p. 129. ISBN 9780429264450.
  7. ↑ König, Simone (30 July 2005). "Prediction of insect adipokinetic hormone sequences assists in de novo structure elucidation". Rapid Communications in Mass Spectrometry. 19 (14): 2103–2104. Bibcode:2005RCMS...19.2103K. doi:10.1002/rcm.2017. ISSN 0951-4198. PMID 15988719.
  8. ↑ Eisenacher, Martin; de Braaf, Jürgen; König, Simone (2006). "Mass analysis sequence prediction (MAPSP)". Bioinformatics. 22 (8): 1002–1003. doi:10.1093/bioinformatics/btl052. PMID 16500935.
  9. ↑ Munte, Claudia E.; Gäde, Gerd; Domogalla, Barbara; Kremer, Werner; Kellner, Roland; Kalbitzer, Hans R. (March 2008). "C-mannosylation in the hypertrehalosaemic hormone from the stick insect Carausius morosus". The FEBS Journal. 275 (6): 1163–1173. doi:10.1111/j.1742-4658.2008.06277.x. ISSN 1742-464X. PMID 18266868.
  10. ↑ König, Simone; Marco, Heather G.; Gäde, Gerd (10 December 2023). "Oxidation Products of Tryptophan and Proline in Adipokinetic Hormones-Artifacts or Post-Translational Modifications?". Life. 13 (12): 2315. Bibcode:2023Life...13.2315K. doi:10.3390/life13122315. ISSN 2075-1729. PMC 10744910. PMID 38137917.
  11. ↑ Gäde, Gerd; Simek, Petr; Clark, Kevin D.; Auerswald, Lutz (1 February 2006). "Unique translational modification of an invertebrate neuropeptide: a phosphorylated member of the adipokinetic hormone peptide family". The Biochemical Journal. 393 (Pt 3): 705–713. doi:10.1042/BJ20050735. ISSN 1470-8728. PMC 1360723. PMID 16271039.
  12. ↑ König, Simone; Bayer, Malte; Marco, Heather; Gäde, Gerd (July 2019). "The hypertrehalosaemic neuropeptide conformational twins of cicadas consist of only L-amino acids: are they cis-trans isomers?". Amino Acids. 51 (7): 1023–1028. doi:10.1007/s00726-019-02742-1. ISSN 1438-2199. PMID 31073692.
  13. ↑ Gäde, Gerd; König, Simone; Kulkarni, Sameer S.; Payne, Richard J.; Marco, Heather G. (15 May 2026). "Threonine sulfation: a rare post translational modification in insect adipokinetic hormones". Scientific Reports. 16 (1): 22190. Bibcode:2026NatSR..1622190G. doi:10.1038/s41598-026-50205-x. ISSN 2045-2322. PMC 13369874. PMID 42141068.
  14. ↑ König, Simone; Albers, Christian; Gäde, Gerd (15 November 2005). "Mass spectral signature for insect adipokinetic hormones". Rapid Communications in Mass Spectrometry. 19 (21): 3021–3024. Bibcode:2005RCMS...19.3021K. doi:10.1002/rcm.2167. ISSN 0951-4198. PMID 16193531.
  15. ↑
    Alavez-Rosas, David; Vargas-Abasolo, Reyna; Albores-Flores, Claudia I.; Meneses-Arias, María Guadalupe; Gutiérrez-Cabrera, Ana Erika; Benelli, Giovanni; Cruz-López, Leopoldo; Córdoba-Aguilar, Alex (2023). "Chemical ecology of triatomines: current knowledge and implications for Chagas disease vector management". Journal of Pest Science. 97 (2). Springer Science and Business Media LLC: 507. Bibcode:2023JPesS..97..507A. doi:10.1007/s10340-023-01678-6. ISSN 1612-4758. S2CID 260819708.
    This review cites this research.
    Marco, Heather G.; König, Simone; Gäde, Gerd (January 2022). "Mass Spectrometric Proof of Predicted Peptides: Novel Adipokinetic Hormones in Insects". Molecules. 27 (19): 6469. doi:10.3390/molecules27196469. ISSN 1420-3049. PMC 9573411. PMID 36235010.
  16. ↑ König, Simone; Bayer, Malte; Marco, Heather; Gäde, Gerd (July 2019). "The hypertrehalosaemic neuropeptide conformational twins of cicadas consist of only l-amino acids: are they cis–trans isomers?". Amino Acids. 51 (7): 1023–1028. doi:10.1007/s00726-019-02742-1. PMID 31073692. S2CID 254074930.
  17. ↑ König, Simone; Marco, Heather G.; Gäde, Gerd (5 July 2023). "The proline effect and the tryptophan immonium ion assist in de novo sequencing of adipokinetic hormones". Scientific Reports. 13 (1): 10894. Bibcode:2023NatSR..1310894K. doi:10.1038/s41598-023-38056-2. ISSN 2045-2322. PMC 10322821. PMID 37407598.
  18. ↑ Marco, Heather G.; König, Simone; Gäde, Gerd (1 October 2022). "Mass Spectrometric Proof of Predicted Peptides: Novel Adipokinetic Hormones in Insects". Molecules. 27 (19): 6469. doi:10.3390/molecules27196469. ISSN 1420-3049. PMC 9573411. PMID 36235010.
  19. ↑ Marco, Heather G.; König, Simone; Gäde, Gerd (November 2023). "Predicted novel hypertrehalosaemic peptides of cockroaches are verified by mass spectrometry". Amino Acids. 55 (11): 1641–1654. doi:10.1007/s00726-023-03337-7. ISSN 1438-2199. PMC 10689539. PMID 37882863.
  20. ↑ Jiang, Shixiong; Marco, Heather G.; Scheich, Nina; He, Shulin; Wang, Zongqing; Gäde, Gerd; McMahon, Dino P. (2023). "Comparative analysis of adipokinetic hormones and their receptors in Blattodea reveals novel patterns of gene evolution". Insect Molecular Biology. 32 (6): 615–633. doi:10.1111/imb.12861. ISSN 1365-2583. PMID 37382487.
  21. ↑ Gäde, Gerd; Šimek, Petr; Marco, Heather G. (December 2016). "Novel members of the adipokinetic hormone family in beetles of the superfamily Scarabaeoidea". Amino Acids. 48 (12): 2785–2798. doi:10.1007/s00726-016-2314-0. ISSN 1438-2199. PMID 27539647.
  22. ↑ Gäde, Gerd; Šimek, Petr; Marco, Heather G. (2019). "Structural diversity of adipokinetic hormones in the hyperdiverse coleopteran Cucujiformia". Archives of Insect Biochemistry and Physiology. 102 (4) e21611. doi:10.1002/arch.21611. ISSN 1520-6327. PMID 31471923.
  23. ↑ Marco, Heather G.; Šimek, Petr; Gäde, Gerd (17 December 2020). "Unique Members of the Adipokinetic Hormone Family in Butterflies and Moths (Insecta, Lepidoptera)". Frontiers in Physiology. 11 614552. doi:10.3389/fphys.2020.614552. ISSN 1664-042X. PMC 7773649. PMID 33391031.
  24. ↑ Gäde, Gerd; Šimek, Petr; Marco, Heather G. (31 March 2020). "The Adipokinetic Peptides in Diptera: Structure, Function, and Evolutionary Trends". Frontiers in Endocrinology. 11 153. doi:10.3389/fendo.2020.00153. ISSN 1664-2392. PMC 7136388. PMID 32296388.
  25. ↑ Gäde, Gerd; Marco, Heather G. (2022). "The Adipokinetic Peptides of Hemiptera: Structure, Function, and Evolutionary Trends". Frontiers in Insect Science. 2 891615. doi:10.3389/finsc.2022.891615. ISSN 2673-8600. PMC 10926376. PMID 38468778.
  26. ↑ Gäde, Gerd; König, Simone; Marco, Heather G. (March 2025). "Structural Diversity of Adipokinetic Hormones in the Coleopteran Suborder Polyphaga (Excluding Cucujiformia)". Archives of Insect Biochemistry and Physiology. 118 (3) e70049. doi:10.1002/arch.70049. ISSN 1520-6327. PMC 11926582. PMID 40114522.
  27. ↑ Marco, Heather G.; König, Simone; Gäde, Gerd (May 2026). "The adipokinetic hormones of stored product pest insects: can this help to combat these insects?". Journal of Stored Products Research. 117 102998. doi:10.1016/j.jspr.2026.102998.
  28. ↑ Gäde, Gerd; Goldsworthy, Graham J. (October 2003). "Insect peptide hormones: a selective review of their physiology and potential application for pest control". Pest Management Science. 59 (10): 1063–1075. Bibcode:2003PMSci..59.1063G. doi:10.1002/ps.755. ISSN 1526-498X. PMID 14561063.
  29. ↑ Goldsworthy, G., K. Opoku-Ware, and L. Mullen, Adipokinetic hormone enhances laminarin and bacterial lipopolysaccharide-induced activation of the prophenoloxidase cascade in the African migratory locust Locusta migratoria. Journal of Insect Physiology, 2002. 48: p. 601-608
  30. ↑ Goldsworthy, G.J., K. Opoku-Ware, and L.M. Mullen, Adipokinetic hormone and the immune responses of locusts to infection. Annals of the New York Academy of Science, 2005. 1040: p. 106-113
  31. ↑ Mugumbate G, Jackson GE, van der Spoel D, Kövér KE, Szilágyi L. Anopheles gambiae, Anoga-HrTH hormone, free and bound structure--a nuclear magnetic resonance experiment. Peptides. 2013 Mar;41:94-100. DOI: 10.1016/j.peptides.2013.01.008.
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