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MiRNA sequencing for CSF-derived EVs microRNAs in patients with moyamoya disease and arteriosclerotic cerebral ischemia

ABSTRACT: MiRNA sequencing for CSF-derived EVs microRNAs in patients with moyamoya disease and arteriosclerotic cerebral ischemia

PROVIDER: PRJNA794123 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR17425765.fastq.gz	Fastqsanger.gz
	SRR17425766.fastq.gz	Fastqsanger.gz
	SRR17425767.fastq.gz	Fastqsanger.gz
	SRR17425768.fastq.gz	Fastqsanger.gz
	SRR17425769.fastq.gz	Fastqsanger.gz

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MiRNA sequencing for CSF-derived EVs microRNAs in patients with moyamoya disease and arteriosclerotic cerebral ischemia

Project description:We aimed to clarify what specific changes occur in the expression level of extracellular vesicles (EVs) -derived microRNAs (miRNAs) in intracranial cerebrospinal fluid (CSF) in moyamoya disease. Patients with arteriosclerotic cerebral ischemia were used as controls to eliminate the effects of cerebral ischemia. Comprehensive expression analysis of miRNAs extracted from EVs by the next-generation sequencer was performed.

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Project description:We obtained the profiles of neuronal phosphoproteome after cerebral ischemia onset by isolating mice hippocampus. Hippocampus combined from either ten sham or ten focal cerebral ischemia 2 h mice were lysed, digested, labeled with different TMT tags, then pooled and analyzed by LC/LC-MS/MS. Five percent of the pool was used for whole proteome analysis, and the remaining 95% was subjected to phosphoproteome profiling. In total, we quantified 5,174 proteins and 9,062 phosphopeptides. Interesting, 21 proteins were upregulated and 7 proteins were downregulated in hippocampus lysates of cerebral ischemia 2 h relative to sham base on fold change. S100a9, Alpha-2-HS-glycoprotein (Ahsg), Fibrinogen beta chain (Fga) and Complement Component C3(c3) are the top significantly changed, which were highly consistent with previous reports in cerebral ischemia injury. Using wolfpsort software to analysis the Subcellular Location, 57% of detected proteins were location to extracellular, 15% were cytoplasmic protein, another 11% were transport to nucleus, and the others were location to plasma membranes (10%), mitochondria (4%) and endoplasmic reticulum (3%). Moreover,184 phosphorylation sites of 135 proteins were upregulated and 689 phosphorylation sites of 420 proteins were downregulated in hippocampus during cerebral ischemia 2 h compare with sham operation. Employing wolfpsort software analysis the subcellular location, 50% of phosphorylated proteins were location to nucleus, 26% were cytoplasmic protein, another 16% were transport to plasma membranes, and the others were location to mitochondria (4%), extracellular (3%) and cytoskeleton (1%). Motif analysis showed that 85% were belongs to serine-type phosphorylation, about 14 were threonine-type phosphorylation and 1% were tyrosine-type phosphorylation.

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