title: The CHH-superfamily of multifunctional peptide hormones controlling crustacean metabolism, osmoregulation, moulting, and reproduction.
abstract: Apart from providing an up-to-date review of the literature, considerable emphasis was placed in this article on the historical development of the field of "crustacean eyestalk hormones". A role of the neurosecretory eyestalk structures of crustaceans in endocrine regulation was recognized about 80 years ago, but it took another half a century until the first peptide hormones were identified. Following the identification of crustacean hyperglycaemic hormone (CHH) and moult-inhibiting hormone (MIH), a large number of homologous peptides have been identified to this date. They comprise a family of multifunctional peptides which can be divided, according to sequences and precursor structure, into two subfamilies, type-I and -II. Recent results on peptide sequences, structure of genes and precursors are described here. The best studied biological activities include metabolic control, moulting, gonad maturation, ionic and osmotic regulation and methyl farnesoate synthesis in mandibular glands. Accordingly, the names CHH, MIH, and GIH/VIH (gonad/vitellogenesis-inhibiting hormone), MOIH (mandibular organ-inhibiting hormone) were coined. The identification of ITP (ion transport peptide) in insects showed, for the first time, that CHH-family peptides are not restricted to crustaceans, and data mining has recently inferred their occurrence in other ecdysozoan clades as well. The long-held tenet of exclusive association with the eyestalk X-organ-sinus gland tract has been challenged by the finding of several extra nervous system sites of expression of CHH-family peptides. Concerning mode of action and the question of target tissues, second messenger mechanisms are discussed, as well as binding sites and receptors. Future challenges are highlighted.
authors.affiliation: School of Biological Sciences, Bangor University, LL57 2UW Bangor, UK. s.g.webster@bangor.ac.uk
authors.forename: Simon George
authors.initials: SG
authors.lastname: Webster
authors.forename: Rainer
authors.initials: R
authors.lastname: Keller
authors.forename: Heinrich
authors.initials: H
authors.lastname: Dircksen
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D060829:Arthropod Proteins / Q000235:genetics / Q000502:physiology*; D001665:Binding Sites; D003445:Crustacea / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D007447:Invertebrate Hormones / Q000235:genetics / Q000502:physiology*; D008969:Molecular Sequence Data; D018978:Molting; D036361:Peptide Hormones / Q000235:genetics / Q000502:physiology*; D012098:Reproduction; D016415:Sequence Alignment; D015398:Signal Transduction; D014882:Water-Electrolyte Balance
chemical_list: D060829:Arthropod Proteins; D007447:Invertebrate Hormones; D036361:Peptide Hormones