4.6 Article

Are Cell Junctions Implicated in the Regulation of Vitellogenin Uptake? Insights from an RNAseq-Based Study in Eel, Anguilla australis

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CELLS
卷 11, 期 3, 页码 -

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MDPI
DOI: 10.3390/cells11030550

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vitellogenesis; vitellogenin uptake; tight junction; gap junction; vitellogenin receptor; endocytosis

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  1. University of Otago

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Through comparing the transcriptomes at different stages of eel ovaries, this study found that specific genes encoding cell junction proteins may play a role in regulating Vtg uptake. The expression changes of key proteins supported the mechanical barrier hypothesis, and the endocytic pathway was found to be up-regulated during Vtg uptake. The study also provided new sequence data for A. australis.
At the onset of puberty, ovarian follicles become competent to incorporate large amounts of vitellogenin (Vtg). Using an RNAseq-based approach, transcriptomes from pre-vitellogenic (PV) and early vitellogenic (EV) ovaries from wild-caught eel, Anguilla australis, were compared to investigate the expression of specific genes encoding cell junction proteins that could be involved in regulating Vtg uptake. Partial support was found for the mechanical barrier hypothesis proposing that the access of Vtg to the oolemma is restricted by a tight junction (TJ) network within the granulosa cell layer, which changes between the PV and EV stage. Among 25 genes encoding TJ-constituting proteins, five were down-regulated and two were up-regulated. A chemical barrier hypothesis stating that gap junctions (GJs) are involved in modulating Vtg uptake was not supported, as only five GJs were found to be expressed in the ovary with no significant changes in expression between stages. Furthermore, the endocytic pathway was found to be up-regulated during the PV-EV transition. Finally, the study showed that gene expression patterns may help identify suitable candidates involved in the regulation of Vtg uptake, and provided novel sequence data for A. australis, including putative Vtg receptors corresponding to Lr8 and Lrp13 members of the low-density lipoprotein receptor family.

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