Nitric oxide inhibits larval settlement in Amphibalanus amphitrite cyprids by repressing muscle locomotion and molting
Online Publication Date2015-10-02
Print Publication Date2015-11
Permanent link to this recordhttp://hdl.handle.net/10754/584258
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AbstractNitric oxide (NO) is a universal signaling molecule and plays a negative role in the metamorphosis of many biphasic organisms. Recently, the NO/NO (cyclic guanosine monophosphate) signaling pathway was reported to repress larval settlement in the barnacle Amphibalanus amphitrite. To understand the underlying molecular mechanism, we analyzed changes in the proteome of A. amphitrite cyprids in response to different concentrations of the NO donor sodium nitroprusside (SNP; 62.5, 250 and 1000 μM) using a label-free proteomics method. Compared with the control, the expression of 106 proteins differed in all three treatments. These differentially expressed proteins were assigned to 13 pathways based on KEGG pathway enrichment analysis. SNP treatment stimulated the expression of heat shock proteins and arginine kinase, which are functionally related to NO synthases, increased the expression levels of glutathione transferases for detoxification, and activated the iron-mediated fatty acid degradation pathway and the citrate cycle through ferritin. Moreover, NO repressed the level of myosins and cuticular proteins, which indicated that NO might inhibit larval settlement in A. amphitrite by modulating the process of muscle locomotion and molting.
CitationZhang, Gen, Yue-Him Wong, Yu Zhang, Li-sheng He, Ying Xu, and Pei-yuan Qian. "Nitric oxide inhibits larval settlement in Amphibalanus amphitrite cyprids by repressing muscle locomotion and molting." PROTEOMICS (2015).
SponsorsThis work was supported by grants from the China Ocean Mineral Resources Research and Development Association (DY125-15-T-02) and the Research Grants Council of the Hong Kong Special Administrative Region (GRF661611, GRF662413 and 16101015) to PY Qian, as well as grants from the Hundred Talent Program (SIDSSE-BR-201304) and the Knowledge Innovation Program of the Chinese Academy of Sciences (SIDSSE-201304) to LS He.
CollectionsPublications Acknowledging KAUST Support
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