Crustacean hyperglycemic hormone (CHH) neuropeptidesfamily: Functions, titer, and binding to target tissues

There was an error published in J. Exp. Biol. 217, In Fig. 3, the letters and numbers indicating which means were significantly different are missing from panel A. The correct figure is printed below.We apologise to the authors and readers for this omission. ) characteristic of late premolt animals and animals did not molt by 90 days post-ESA. There was no effect of ESA or MLA on the expression of Cm-elongation factor 2 (EF2), Cm-NOS, the beta subunit of GC-I (Cm-GC-Iβ), a membrane receptor GC (Cm-GC-II) and a soluble NO-insensitive GC (Cm-GC-III) in green morphs. Red morphs were affected by prolonged ESA and MLA treatments, as indicated by large decreases in Cm-EF2, Cm-GC-II and Cm-GC-III mRNA levels. ESA accelerated the transition of green morphs to the red phenotype in intermolt animals. ESA delayed molting in premolt green morphs, whereas intact and MLA animals molted by 30 days post treatment. There were significant effects on YO gene expression in intact animals: Cm-GC-Iβ mRNA increased during premolt and Cm-GC-III mRNA decreased during premolt and increased during postmolt. Cm-MIH transcripts were detected in eyestalk ganglia, the brain and the thoracic ganglion from green intermolt animals, suggesing that MIH in the brain and thoracic ganglion prevents molt induction in green ESA animals.

Section: Control Of Moltingmentioning

confidence: 99%

Molt regulation in green and red color morphs of the crab,Carcinus maenas: gene expression of molt-inhibiting hormone signaling components

Abuhagr

Blindert

Nimitkul

et al. 2013

“…The CHH neuropeptide family is mainly represented in crustaceans but is also found in insects and its biological and chemical aspects were recently reviewed in relation to a variety of physiological processes (Chung et al, 2010;Dircksen, 2009;Giulianini and Edomi, 2006;Katayama et al, 2013;Webster et al, 2012). CHHs are produced in the X-organ and secreted to an adjacent hemal sinus termed the sinus gland.…”

Section: Introductionmentioning

confidence: 99%

Different transcription regulation routes are exerted by L- and D-amino acid enantiomers of peptide hormones

Tom

Manfrin

Mosco

et al. 2014

Conversion of one or more amino acids in eukaryotic peptides to the D-enantiomer configuration is catalyzed by specific L/D-peptide isomerases and it is a poorly investigated post-translational modification. No common modified amino acid or specific modified position has been recognized, and mechanisms underlying changes in the peptide function provided by this conversion are not widely studied. The 72 amino acid crustacean hyperglycemic hormone (CHH) in Astacidea crustaceans exhibits a co-existence of two peptide enantiomers with either D-or L-phenylalanine as their third residue. It is a pleiotropic hormone regulating several physiological processes in different target tissues and along different time scales. CHH enantiomers differently affect time courses and intensities of examined processes. The short-term effects of the two isomers on gene expression were examined in the hepatopancreas, gills, hemocytes and muscles of the astacid Pontastacus leptodactylus. Gene expression in muscles and hemocytes was not affected by either of the isomers. Two modes of action for CHH were elucidated in the hepatopancreas and the gills: specific gene induction in both organs by D-CHH, and targeted attenuation caused by both enantiomers in the gills. Consequently, a two-receptor system is proposed for conveying the effect of the two CHH isomers.

“…The most widely studied crustacean neurohormone, crustacean hyperglycaemic hormone (CHH) has long been known to be centrally involved in regulation of energy metabolism in many malacostracan crustaceans (reviewed by Böcking et al, 2002;Fanjul-Moles, 2006;Chung et al, 2010;Webster et al, 2012). In recent years, a variety of other functions for these hormones have been established, involving (for example) inhibition of ecdysteroid (Webster and Keller, 1986;Chang et al, 1990;Chung and Webster, 2003;Chung and Webster, 2005), methyl farnesoate (Liu et al, 1997) and ovarian protein synthesis (Khayat et al, 1998;Avarre et al, 2001).…”

Section: Introductionmentioning

confidence: 99%

Roles of crustacean hyperglycaemic hormone in ionic and metabolic homeostasis in the Christmas Island Blue crabDiscoplax celeste

Turner

Webster

Morris

2012

SUMMARYThere is a growing body of evidence implicating the involvement of crustacean hyperglycaemic hormone (CHH) in ionic homeostasis in decapod crustaceans. However, little is known regarding hormonally influenced osmoregulatory processes in terrestrial decapods. As many terrestrial decapods experience opposing seasonal demands upon ionoregulatory physiologies, we reasoned that these would make interesting models in which to study the effect of CHH upon these phenomena. In particular, those (tropical) species that also undergo seasonal migrations might be especially informative, as we know relatively little regarding the nature of CHHs in terrestrial decapods, and hormonally mediated responses to seasonal changes in metabolic demands might also be superimposed or otherwise integrated with those associated with ionic homeostasis. Using Discoplax celeste as a model crab that experiences seasonal extremes in water availability, and exhibits diurnal and migratory activity patterns, we identified two CHHs in the sinus gland. We biochemically characterised (cDNA cloning) one CHH and functionally characterised (in terms of dose-dependent hyperglycaemic responses and glucose-dependent negative feedback loops) both CHHs. Whole-animal in situ branchial chamber 22 NaCl perfusion experiments showed that injection of both CHHs increased gill Na + uptake in a seasonally dependent manner, and 51Cr-EDTA clearance experiments demonstrated that CHH increased urine production by the antennal gland. Seasonal and salinity-dependent differences in haemolymph CHH titre further implicated CHH in osmoregulatory processes. Intriguingly, CHH appeared to have no effect on gill Na + /K + -ATPase or V-ATPase activity, suggesting unknown mechanisms of this hormoneʼs action on Na + transport across gill epithelia.Supplementary material available online at