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Gene expression in primed and chemically reset (cR) naïve human iPSCs, and naïve-converted cells after co-culture with mouse embryonic stem cells

ABSTRACT: Gene expression in primed and chemically reset (cR) naïve human iPSCs, and naïve-converted cells after co-culture with mouse embryonic stem cells

PROVIDER: PRJNA893005 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR22007816_1.fastq.gz	Fastqsanger.gz
	SRR22007816_2.fastq.gz	Fastqsanger.gz
	SRR22007817_1.fastq.gz	Fastqsanger.gz
	SRR22007817_2.fastq.gz	Fastqsanger.gz
	SRR22007818_1.fastq.gz	Fastqsanger.gz

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Gene expression in primed and chemically reset (cR) naïve human iPSCs, and naïve-converted cells after co-culture with mouse embryonic stem cells

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Project description:Functional-assay limitations are an emerging issue in characterizing human pluripotent stem cells (hPSCs). With rodent PSCs, chimera formation, using pre-implantation embryos, is the gold-standard assay of pluripotency. In hPSCs, this can only be monitored via teratoma formation or in vitro differentiation, as ethical concerns preclude generation of human-animal chimera. To circumvent this issue, we established a functional assay utilizing interspecific blastocyst injection and in vitro culture (interspecies in vitro chimera assay). The assay uses mouse pre-implantation embryos and human PSCs to make interspecies chimeras cultured in vitro to the early egg cylinder stage. When hiPSCs, both conventional and naive type, which called M-bM-^@M-^\reset cellM-bM-^@M-^], were injected into mouse embryos and cultured. The cells were never integrated into the epiblast of egg cylinder stage-embryo. These results suggest that hPSCs, including naM-CM-/ve type, are unable to form chimera with mouse embryo. Reset cells were converted from conventional human iPSC line PB004, and then compared their gene expression profile with or without transgene overexpression induced by doxycyclin treatment.

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Project description:Functional-assay limitations are an emerging issue in characterizing human pluripotent stem cells (hPSCs). With rodent PSCs, chimera formation, using pre-implantation embryos, is the gold-standard assay of pluripotency. In hPSCs, this can only be monitored via teratoma formation or in vitro differentiation, as ethical concerns preclude generation of human-animal chimera. To circumvent this issue, we established a functional assay utilizing interspecific blastocyst injection and in vitro culture (interspecies in vitro chimera assay). The assay uses mouse pre-implantation embryos and human PSCs to make interspecies chimeras cultured in vitro to the early egg cylinder stage. When hiPSCs, both conventional and naive type, which called “reset cell”, were injected into mouse embryos and cultured. The cells were never integrated into the epiblast of egg cylinder stage-embryo. These results suggest that hPSCs, including naïve type, are unable to form chimera with mouse embryo.

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Project description:How Protein kinase A (PKA) is reset to a basal state following 3’5’cyclic adenosine monophosphate(cAMP)-mediated activation is unknown. Here we describe the mechanism of cAMP-PKA signal termination leading to reset of PKA by holoenzyme formation through the obligatory action of phosphodiesterases (PDEs). We report a catalytic subunit (Cα)-assisted mechanism for the reset of type I PKA and describe for the first time multiple structures of the reset holoenzyme that capture an ensemble of conformational end-states through the integration of electron microscopy with structural mass spectrometry.Together, integrative cryo-EM with mass spectrometry showcases the high domain-specific dynamics of the regulatory subunit (RIα) and their interactions with Cα. Our integrated structure and dynamics approaches reveal that the tetrameric cAMP-free reset holoenzyme adopts multiple, distinct conformations of the RIα with contributions from the N-terminal linker and CNB-B domains. Our findings highlight the interplay between RIα, Cα and PDEs (PDE8) in signalosomes and the impact of substrate and nucleotides and offer a new paradigm for PDE-mediated regulation of cAMP-PKA signaling.

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