Structure and expression of a shrimp prohormone convertase 2

Tangprasittipap, Amornrat; Chouwdee, Saisunee; Phiwsaiya, Kornsunee; Laiphrom, Seansook; Senapin, Saengchan; Flegel, Timothy W.; Sritunyalucksana, Kallaya

doi:10.1016/j.ygcen.2012.05.005

Cited by 9 publications

(3 citation statements)

References 23 publications

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“…We report a broad expression of PC2 in the embryonic neuroectoderm and the larval CNS of Tribolium, which is similar to PC2-expression during Drosophila embryogenesis and in many secretory neurons of the fly nervous system [7,39]. Expression of PC2-orthologues in invertebrate nervous systems and/or neuroendocrine organs has also been reported from a shrimp, a centipede, C. elegans and the polychaete worm Platynereis [38,[40][41][42], underlining the conserved nature of this gene.…”

Section: A New Pc1/3 Expressing Cell Population Of the Beetle's Suboesupporting

confidence: 55%

Individual function of the ancestral prohormone convertase PC1/3 in Tribolium larval growth and moulting highlights major evolutionary changes between beetle and fly neuroendocrine systems

Fritzsche¹,

Hunnekuhl²

2020

Preprint

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Background: The insect neuroendocrine system acts in the regulation of physiology, development and growth. Molecular evolution of this system hence has the potential to allow for major biological differences between insect groups. Two prohormone convertases, PC1/3 and PC2, are found in animals and both function in the processing of neuropeptide precursors in the vertebrate neurosecretory pathway. Whereas PC2-function is conserved between the fly Drosophila and vertebrates , ancestral PC1/3 was lost in the fly lineage and has not been functionally studied in any protostome. Results: In order to understand its original functions and the changes accompanying the gene loss in the fly, we investigated PC1/3 and PC2 expression and function in the beetle Tribolium castaneum. We found that PC2 is broadly expressed in the nervous system, whereas surprisingly, PC1/3 expression is restricted to specific cell groups in the posterior brain and suboesophageal ganglion. Both proteases have parallel but non-redundant functions in adult beetles’ viability and fertility. Female infertility following RNAi is caused by a failure to deposit sufficient nutritive material to the developing oocytes. Larval RNAi of both genes produced moulting defects where the larvae were not able to shed their old cuticle and became ‘locked-in’. Unexpectedly, PC1/3 RNAi larvae went through supernumerary larval moults despite minimal to zero weight gain. Conclusions: Our results indicate a yet unknown molecular mechanism for the coupling of moulting and growth in insect larvae. Conservation of the evolutionary ancient PC1/3 gene in most insect groups suggests conserved function and that its loss in dipterans may have been accompanied by major changes in the coordination of larval growth and moulting.

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Section: A New Pc1/3 Expressing Cell Population Of the Beetle's Suboesupporting

confidence: 55%

Individual function of the ancestral prohormone convertase PC1/3 in Tribolium larval growth and moulting highlights major evolutionary changes between beetle and fly neuroendocrine systems

Fritzsche¹,

Hunnekuhl²

2020

Preprint

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“…We provide the first genome sequence for the major yield‐limiting shrimp pathogen E. hepatopenaei . This genomic data in conjunction with previously‐published information on the parasite's transmission cycle (Tangprasittipap et al ., ; Tangprasittipap et al ., ), a growing body of genomic data for host shrimp species (You et al ., ; Baranski et al ., ; Castillo‐Juarez et al ., ; Yu et al ., ) and the capacity to study this pathogen in the shrimp host (Salachan et al ., ) will undoubtedly underpin the development of new tools to diagnose, monitor and potentially mitigate the negative impacts of E. hepatopenaei . As a whole our data provide resounding evidence of the consistent loss of glycolysis into the Enterocytozoonidae and closest relatives.…”

Section: Resultsmentioning

confidence: 99%

Decay of the glycolytic pathway and adaptation to intranuclear parasitism within Enterocytozoonidae microsporidia

Boakye

Jaroenlak

Prachumwat

et al. 2017

Environmental Microbiology

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Glycolysis and oxidative phosphorylation are the fundamental pathways of ATP generation in eukaryotes. Yet in microsporidia, endoparasitic fungi living at the limits of cellular streamlining, oxidative phosphorylation has been lost: energy is obtained directly from the host or, during the dispersive spore stage, via glycolysis. It was therefore surprising when the first sequenced genome from the Enterocytozoonidae - a major family of human and animal-infecting microsporidians - appeared to have lost genes for glycolysis. Here, we sequence and analyse genomes from additional members of this family, shedding new light on their unusual biology. Our survey includes the genome of Enterocytozoon hepatopenaei, a major aquacultural parasite currently causing substantial economic losses in shrimp farming, and Enterospora canceri, a pathogen that lives exclusively inside epithelial cell nuclei of its crab host. Our analysis of gene content across the clade suggests that Ent. canceri's adaptation to intranuclear life is underpinned by the expansion of transporter families. We demonstrate that this entire lineage of pathogens has lost glycolysis and, uniquely amongst eukaryotes, lacks any obvious intrinsic means of generating energy. Our study provides an important resource for the investigation of host-pathogen interactions and reductive evolution in one of the most medically and economically important microsporidian lineages.

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“…Toullec et al [15] reported that PC2 is the key endoprotease responsible for the maturation of crustacean hyperglycemic hormone (CHH). Homologues of PC2 have been characterized in only few invertebrates, including the nematode Caenorhabditis elegans [16], gastropod mollusk species Lymnaea stagnalis [17], Aplysia californica [14], H. asinina [18], arthropod species Lucilia cuprina [19], Drosophila melanogaster [20], Orconectes limosus [15], and Penaeus monodon [21].…”

Section: Introductionmentioning

confidence: 99%

Molecular characterization and spatiotemporal expression of prohormone convertase 2 in the Pacific abalone, Haliotis discus hannai

2020

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Prohormone convertases (PCs) are subtilisin-like proteases responsible for the intracellular processing of prohormones and proneuropeptides in vertebrates and invertebrates. The full-length PC2 cDNA sequence was cloned from pleuropedal ganglion of Haliotis discus hannai, consisted of 2254-bp with an open reading frame of 1989-bp and encoded a protein of 662 amino acid residues. The architecture of Hdh PC2 displayed key features of PCs, including a signal peptide, a pro-segment domain with sites for autocatalytic activation, a catalytic domain, and a pro-protein domain (P-domain). It shares the highest homology of its amino acid sequence with the PC2 from H. asinina and to lesser extent with that of Homo sapiens and Rana catesbeiana PC2. Sequence alignment analysis indicated that Hdh PC2 was highly conserved in the catalytic domain, including a catalytic triad of serine proteinases of the subtilisin family at positions Asp-195, His-236, and Ser-412. The cloned sequence contained a canonical integrin binding sequence, and four cysteine residues involved in the formation of an intramolecular disulfide link. Phylogenetic analysis revealed that the Hdh PC2 is robustly clustered with the Has PC2. Quantitative PCR assay demonstrated that the Hdh PC2 was predominantly expressed in the pleuropedal ganglion rather than in other examined tissues. Although PC2 mRNA was expressed throughout the gametogenetic cycle of male and female abalone, the expression level was significantly higher in the ripening stage of female abalone. Also, a significantly higher expression was observed in the pleuropedal ganglion and gonadal tissues at a higher effective accumulative temperature (1000˚C). In situ hybridization revealed that the PC2 mRNA expressing neurosecretory cells were distributed in the cortex region of the pleuropedal ganglion. According to the results, it can be concluded that pleuropedal ganglion is the highest site of PC2 activity, and this enzyme might be involved in the abalone reproduction process.

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Structure and expression of a shrimp prohormone convertase 2

Cited by 9 publications

References 23 publications

Individual function of the ancestral prohormone convertase PC1/3 in Tribolium larval growth and moulting highlights major evolutionary changes between beetle and fly neuroendocrine systems

Individual function of the ancestral prohormone convertase PC1/3 in Tribolium larval growth and moulting highlights major evolutionary changes between beetle and fly neuroendocrine systems

Decay of the glycolytic pathway and adaptation to intranuclear parasitism within Enterocytozoonidae microsporidia

Molecular characterization and spatiotemporal expression of prohormone convertase 2 in the Pacific abalone, Haliotis discus hannai

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