Ontology highlight
ABSTRACT:
PROVIDER: PRJNA887485 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR21871347.fastq.gz | Fastqsanger.gz | |||
| SRR21871348.fastq.gz | Fastqsanger.gz | |||
| SRR21871349.fastq.gz | Fastqsanger.gz | |||
| SRR21871350.fastq.gz | Fastqsanger.gz | |||
| SRR21871351.fastq.gz | Fastqsanger.gz |
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Project description:Hypoxia has become one of the most critical factors limiting the development of aquaculture. Crucian carp (Carassius auratus) is widely consumed fish in China, with excellent tolerance to hypoxic environment. However, the molecular mechanisms underlying hypoxia adaptation and tolerance in crucian carp remain unclear. In this study, we detected the changes of biochemical parameters after hypoxia stress (3 h (H3h), H12h, and H24h) and reoxygenation (reoxygenation for 3 h after hypoxia 24 h (R3h)), mRNA and miRNA expression profiles under H12h compared to the control, and key hypoxia-related genes expression patterns in the liver of crucian carp through biochemical methods, RNA-seq, and qRT-PCR. Compared with the control, increased T-SOD, CAT, GSH-Px, T-AOC, ALT, and AST activities and MDA, TCHO, and TG contents, and decreased TP and ATP contents were observed after hypoxia stress, and LDH activity increased only in the H12h and H24h groups. Based on RNA-seq, 2479 differentially expressed (DE) mRNAs and 60 DE miRNAs were identified, and numerous DE mRNAs involved in HIF signaling pathway (hif-1α, epo, vegfa, and ho), anaerobic metabolism (hk1/hk2, pfk, gapdh, pk, and ldh) and immune response (nlrc3, nlrp12, cxcr1, cxcr4, ccr9, and cxcl12) were significantly upregulated after hypoxia exposure. Integrated analysis found that ho, igfbp1, hsp70, and hk2 were predicted to be regulated by novel_867, dre-miR-125c-3p/novel_173, dre-miR-181b-5p, and dre-miR-338-5p/dre-miR-128-3p, respectively, and targets of DE miRNAs were significantly enriched in MAPK signaling pathway, FoxO signaling pathway, glycolysis/gluconeogenesis, insulin signaling pathway, NOD−like receptor signaling pathway, and cytokine-cytokine receptor interaction. Expression analysis showed that the mRNA levels of vegfa, epo, ho, hsp70, hsp90aa.1, igfbp1, ldh, hk1, pfk, pk, and gapdh exhibited a remarkable increase, whereas sdh and mdh were downregulated in the H3h, H12h, and H24h groups compared with the control. These results contribute to our understanding of the molecular mechanisms of hypoxia tolerance in crucian carp, which are of great significance for genetics and breeding of other fishes tolerant to hypoxia.
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Project description:The freshwater fish crucian carp (Carassius carassius) are able to survive chronic anoxia for several months at low temperatures. Consequently, anoxia-related physiological and biochemical adaptations in this species have been studied for more than half a century. Still, despite for the well-known role of protein phosphorylation in regulating cellular processes, no studies have comprehensively characterized the phosphoproteome in crucian carp. In this study, we report the global phosphoproteome in crucian carp brain and liver during anoxia and reoxygenation. By applying a bottom-up proteomic approach on enriched phosphopeptides we found that the brain phosphoproteome show surprisingly few changes during anoxia-reoxygenation exposure with 110 out of 4316 phosphopeptides being differentially regulated. By contrast, in the liver 395 out of 1293 phosphopeptides were regulated. Although most changes occurred in the liver phosphoproteome, we found evidence for metabolic depression and decreased translation in both brain and liver. We also found regulated phosphoproteins involved in apoptotic regulation and reactive oxygen species handling in both tissues. In the brain, some of the most regulated phosphopeptides belonged to proteins involved in central nervous system development and neuronal activity at the synaptic cleft. Regulated phosphoproteins specific for liver tissue were related to glucose metabolism, including glycolytic flux and glycogenolysis, and the ubiquitin-proteasome system.
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