Demonstration of expression of a neuropeptide-encoding gene in crustacean hemocytes

Wu, Su-Hua; Chen, Yan-Jhou; Huang, Shao-Yen; Tsai, Wei-Shiun; Wu, Hsin-Ju; Hsu, Tsan-Ting; Lee, Chi-Ying

doi:10.1016/j.cbpa.2012.01.007

Cited by 20 publications

(15 citation statements)

References 53 publications

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“…CHH peptide levels in sinus gland and hemolymph samples were quantified using an established sandwich ELISA with 2 anti-CHH antibodies; specificity of the assay for the crayfish CHH has been demonstrated and reported [ 38 , 39 ]. Glucose levels in the hemolymph samples were quantified using an established glucose assay (GAGO20-1KT, Sigma).…”

Section: Methodsmentioning

confidence: 99%

Differential effects of silencing crustacean hyperglycemic hormone gene expression on the metabolic profiles of the muscle and hepatopancreas in the crayfish Procambarus clarkii

Chiu

Tien

et al. 2017

PLoS ONE

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In order to functionally characterize the metabolic roles of crustacean hyperglycemic hormone (CHH), gene expression of CHH in the crayfish (Procambarus clarkii) was knocked down by in vivo injection of CHH double-stranded RNA (dsRNA), followed by metabolomic analysis of 2 CHH target tissues (the muscle and hepatopancreas) using nuclear magnetic resonance spectroscopy. Compared to the levels in untreated and saline-injected (SAI) animals, levels of CHH transcript, but not those of molt-inhibiting hormone (a CHH-family peptide), in the eyestalk ganglia of CHH dsRNA-injected (DSI) animals were significantly decreased at 24, 48, and 72 hour post injection (hpi), with concomitant changes in levels of CHH peptide in the sinus gland (a neurohemal organ) and hemolymph. Green fluorescence protein (GFP) dsRNA failed to affect levels of CHH transcript in the eyestalk ganglia of GFP DSI animals. Number of metabolites whose levels were significantly changed by CHH dsRNA was 149 and 181 in the muscle and 24 and 12 in the hepatopancreas, at 24 and 48 hpi, respectively. Principal component analysis of these metabolites show that metabolic effects of silencing CHH gene expression were more pronounced in the muscle (with the cluster of CHH DSI group clearly being separated from that of SAI group at 24 hpi) than in the hepatopancreas. Moreover, pathway analysis of the metabolites closely related to carbohydrate and energy metabolism indicate that, for CHH DSI animals at 24 hpi, metabolic profile of the muscle was characterized by reduced synthesis of NAD+ and adenine ribonucleotides, diminished levels of ATP, lower rate of utilization of carbohydrates through glycolysis, and a partially rescued TCA cycle, whereas that of the hepatopancreas by unaffected levels of ATP, lower rate of utilization of carbohydrates, and increased levels of ketone bodies. The combined results of metabolic changes in response to silenced CHH gene expression reveal that metabolic functions of CHH on the muscle and hepatopancreas are more diverse than previously thought and are differential between the two tissues.

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Section: Methodsmentioning

confidence: 99%

Differential effects of silencing crustacean hyperglycemic hormone gene expression on the metabolic profiles of the muscle and hepatopancreas in the crayfish Procambarus clarkii

Chiu

Tien

et al. 2017

PLoS ONE

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“…Most of the type I genes described so far encode two transcripts that, in most cases, share the signal peptide sequence, the CHH precursor-related peptide (CPRP) and the N-terminal region (exons I and II), but differ in the C-terminal region, which can be encoded by exon III or exon IV [4,10]. These alternative splicing isoforms have been found in various crustaceans, including Carcinus maenas [10], Macrobrachium rosenbergii [3], Pachygrapsus marmoratus, Potamon ibericum [38], Gecarcinus lateralis [22], Callinectes sapidus [8,53], Scylla olivacea [41], Pandalopsis japonica [16], Procambarus clarkii [19,47,48,50], Portunus trituberculatus [49], and Litopenaeus vannamei [21].…”

Section: Introduction Q3mentioning

confidence: 97%

Hyperglycemic activity of the recombinant crustacean hyperglycemic hormone B1 isoform (CHH-B1) of the Pacific white shrimp Litopenaeus vannamei

et al. 2015

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“…superba , E . crystallorophias ) and from non-crustacean species (see Fig 6 ) [ 5 , 7 , 8 , 9 , 24 , 25 , 47 , 59 ], conclusions reached as summarized here could provide valuable information for understanding how functional diversification evolved within a peptide family.…”

Section: Discussionmentioning

confidence: 63%

“…g ., molting, osmoregulation, and reproduction [ 16 , 17 , 18 , 19 , 20 , 21 , 22 , 23 ], may also be regulated by CHH. In addition, recent studies discovered expression of CHHs, some of which with unique sequences not previously reported, in circulating hemocytes [ 24 , 25 ]; it was also demonstrated that in vivo injection of recombinant CHH significantly increased pathogen clearance ability and survival rate of pathogen-infected shrimps [ 26 ]. The combined results suggest that novel function(s) of CHH have yet to be characterized.…”

Section: Introductionmentioning

confidence: 99%

Functional Assessment of Residues in the Amino- and Carboxyl-Termini of Crustacean Hyperglycemic Hormone (CHH) in the Mud Crab Scylla olivacea Using Point-Mutated Peptides

Liu¹,

Huang²,

Toullec³

et al. 2015

PLoS ONE

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To assess functional importance of the residues in the amino- and carboxyl-termini of crustacean hyperglycemic hormone in the mud crab Scylla olivacea (Sco-CHH), both wild-type and point-mutated CHH peptides were produced with an amidated C-terminal end. Spectral analyses of circular dichroism, chromatographic retention time, and mass spectrometric analysis of the recombinant peptides indicate that they were close in conformation to native CHH and were produced with the intended substitutions. The recombinant peptides were subsequently used for an in vivo hyperglycemic assay. Two mutants (R13A and I69A rSco-CHH) completely lacked hyperglycemic activity, with temporal profiles similar to that of vehicle control. Temporal profiles of hyperglycemic responses elicited by 4 mutants (I2A, F3A, D12A, and D60A Sco-CHH) were different from that elicited by wild-type Sco-CHH; I2A was unique in that it exhibited significantly higher hyperglycemic activity, whereas the remaining 3 mutants showed lower activity. Four mutants (D4A, Q51A, E54A, and V72A rSco-CHH) elicited hyperglycemic responses with temporal profiles similar to those evoked by wild-type Sco-CHH. In contrast, the glycine-extended version of V72A rSco-CHH (V72A rSco-CHH-Gly) completely lost hyperglycemic activity. By comparing our study with previous ones of ion-transport peptide (ITP) and molt-inhibiting hormone (MIH) using deleted or point-mutated mutants, detail discussion is made regarding functionally important residues that are shared by both CHH and ITP (members of Group I of the CHH family), and those that discriminate CHH from ITP, and Group-I from Group-II peptides. Conclusions summarized in the present study provide insights into understanding of how functional diversification occurred within a peptide family of multifunctional members.

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Demonstration of expression of a neuropeptide-encoding gene in crustacean hemocytes

Cited by 20 publications

References 53 publications

Differential effects of silencing crustacean hyperglycemic hormone gene expression on the metabolic profiles of the muscle and hepatopancreas in the crayfish Procambarus clarkii

Differential effects of silencing crustacean hyperglycemic hormone gene expression on the metabolic profiles of the muscle and hepatopancreas in the crayfish Procambarus clarkii

Hyperglycemic activity of the recombinant crustacean hyperglycemic hormone B1 isoform (CHH-B1) of the Pacific white shrimp Litopenaeus vannamei

Functional Assessment of Residues in the Amino- and Carboxyl-Termini of Crustacean Hyperglycemic Hormone (CHH) in the Mud Crab Scylla olivacea Using Point-Mutated Peptides

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