Characterization of the shrimp neuroparsin (MeNPLP): RNAi silencing resulted in inhibition of vitellogenesis

The full-length Metapenaeus ensis neuroparsin (MeNPLP) cDNA was cloned which encodes a shrimp protein homologous to the insect neuroparsin and vertebrate insulin-like growth factor binding protein (IGFBP). MeNPLP cDNA is 1389 bp in length and the longest open reading frame is 303 bp in length. The f...

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Main Authors: Shi Ping Yang, Jian-Guo He, Cheng Bo Sun, Siuming Francis Chan
Format: Article
Language:English
Published: Wiley 2014-01-01
Series:FEBS Open Bio
Subjects:
Online Access:http://www.sciencedirect.com/science/article/pii/S2211546314000874
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spelling doaj-d9c43e001ebd4dc3a044c49120822e6b2020-11-25T03:41:52ZengWileyFEBS Open Bio2211-54632014-01-014C97698610.1016/j.fob.2014.09.005Characterization of the shrimp neuroparsin (MeNPLP): RNAi silencing resulted in inhibition of vitellogenesisShi Ping Yang0Jian-Guo He1Cheng Bo Sun2Siuming Francis Chan3Fisheries College, Guangdong Ocean University, Zhanjiang, Guangdong, ChinaSchool of Life Sciences, Zhongshan University, Guangzhou, ChinaFisheries College, Guangdong Ocean University, Zhanjiang, Guangdong, ChinaFisheries College, Guangdong Ocean University, Zhanjiang, Guangdong, ChinaThe full-length Metapenaeus ensis neuroparsin (MeNPLP) cDNA was cloned which encodes a shrimp protein homologous to the insect neuroparsin and vertebrate insulin-like growth factor binding protein (IGFBP). MeNPLP cDNA is 1389 bp in length and the longest open reading frame is 303 bp in length. The first 27 aa are predicted to be the signal peptide and aa 28–101 is the mature peptide with an estimated molecular weight of 7.83 kDa and pI of 5. It shows high amino acid sequence similarity (42–68%) to the neuroparsin of insects and N-terminal end of the IGFBP of vertebrates. The cysteine residues in MeNPLP responsible for disulfide bond formation are conserved as in other neuroparsin-like proteins. The expression level of MeNPLP is the highest in the hepatopancreas, followed by the nerve cord, brain, heart, ovary, and muscle. However, it was not expressed in the testis. Using an insect neuroparsin antibody, MeNPLP could only be detected in the hepatopancreatic tubules, suggesting that MeNPLP may be a secretary product. Although MeNPLP expression was stimulated in the ovary, it was inhibited in the hepatopancreas after treatment with neurotransmitter serotonin (5-HT). In vivo gene silencing of MeNPLP could cause a significant decrease of vitellogenin transcript level in the hepatopancreas and ovary. As a result, a corresponding decrease in vitellogenin protein level was observed in the hemolymph and ovary. In conclusion, this study has provided the first evidence that MeNPLP is involved in the initial stage of ovary maturation in shrimp.http://www.sciencedirect.com/science/article/pii/S2211546314000874ShrimpNeuroparsinIGF-like binding proteinRNA interferenceVitellogenin
collection DOAJ
language English
format Article
sources DOAJ
author Shi Ping Yang
Jian-Guo He
Cheng Bo Sun
Siuming Francis Chan
spellingShingle Shi Ping Yang
Jian-Guo He
Cheng Bo Sun
Siuming Francis Chan
Characterization of the shrimp neuroparsin (MeNPLP): RNAi silencing resulted in inhibition of vitellogenesis
FEBS Open Bio
Shrimp
Neuroparsin
IGF-like binding protein
RNA interference
Vitellogenin
author_facet Shi Ping Yang
Jian-Guo He
Cheng Bo Sun
Siuming Francis Chan
author_sort Shi Ping Yang
title Characterization of the shrimp neuroparsin (MeNPLP): RNAi silencing resulted in inhibition of vitellogenesis
title_short Characterization of the shrimp neuroparsin (MeNPLP): RNAi silencing resulted in inhibition of vitellogenesis
title_full Characterization of the shrimp neuroparsin (MeNPLP): RNAi silencing resulted in inhibition of vitellogenesis
title_fullStr Characterization of the shrimp neuroparsin (MeNPLP): RNAi silencing resulted in inhibition of vitellogenesis
title_full_unstemmed Characterization of the shrimp neuroparsin (MeNPLP): RNAi silencing resulted in inhibition of vitellogenesis
title_sort characterization of the shrimp neuroparsin (menplp): rnai silencing resulted in inhibition of vitellogenesis
publisher Wiley
series FEBS Open Bio
issn 2211-5463
publishDate 2014-01-01
description The full-length Metapenaeus ensis neuroparsin (MeNPLP) cDNA was cloned which encodes a shrimp protein homologous to the insect neuroparsin and vertebrate insulin-like growth factor binding protein (IGFBP). MeNPLP cDNA is 1389 bp in length and the longest open reading frame is 303 bp in length. The first 27 aa are predicted to be the signal peptide and aa 28–101 is the mature peptide with an estimated molecular weight of 7.83 kDa and pI of 5. It shows high amino acid sequence similarity (42–68%) to the neuroparsin of insects and N-terminal end of the IGFBP of vertebrates. The cysteine residues in MeNPLP responsible for disulfide bond formation are conserved as in other neuroparsin-like proteins. The expression level of MeNPLP is the highest in the hepatopancreas, followed by the nerve cord, brain, heart, ovary, and muscle. However, it was not expressed in the testis. Using an insect neuroparsin antibody, MeNPLP could only be detected in the hepatopancreatic tubules, suggesting that MeNPLP may be a secretary product. Although MeNPLP expression was stimulated in the ovary, it was inhibited in the hepatopancreas after treatment with neurotransmitter serotonin (5-HT). In vivo gene silencing of MeNPLP could cause a significant decrease of vitellogenin transcript level in the hepatopancreas and ovary. As a result, a corresponding decrease in vitellogenin protein level was observed in the hemolymph and ovary. In conclusion, this study has provided the first evidence that MeNPLP is involved in the initial stage of ovary maturation in shrimp.
topic Shrimp
Neuroparsin
IGF-like binding protein
RNA interference
Vitellogenin
url http://www.sciencedirect.com/science/article/pii/S2211546314000874
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AT jianguohe characterizationoftheshrimpneuroparsinmenplprnaisilencingresultedininhibitionofvitellogenesis
AT chengbosun characterizationoftheshrimpneuroparsinmenplprnaisilencingresultedininhibitionofvitellogenesis
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