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Immunostaining of phospho-RIPK3 in L929 cells, murine yolk sacs, ceca, and small intestines.

ABSTRACT: Though phospho-receptor-interacting protein 3 (RIP3 or RIPK3) antibodies are used in western blot, immunostaining of murine phospho-RIPK3 is challenging. Here, we verify and describe a detailed protocol for immunofluorescent detection of phospho-RIPK3 in L929 cells and mouse yolk sacs. We also describe in detail the model construction methods, sample preparation steps, and staining procedures for immunohistochemical labeling of RIPK3 activation in mouse ceca and small intestines by utilizing a specific commercially available antibody. For complete details on the use and execution of this protocol, please refer to Zhang et al. (2021) and Wang et al. (2020).

SUBMITTER: Li L

PROVIDER: S-EPMC9254451 | biostudies-literature |

REPOSITORIES: biostudies-literature

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Murine hematopoietic stem cell activity is derived from pre-circulation embryos but not yolk sacs.

Project description:The embryonic site of definitive hematopoietic stem cell (dHSC) origination has been debated for decades. Although an intra-embryonic origin is well supported, the yolk sac (YS) contribution to adult hematopoiesis remains controversial. The same developmental origin makes it difficult to identify specific markers that discern between an intraembryonic versus YS-origin using a lineage trace approach. Additionally, the highly migratory nature of blood cells and the inability of pre-circulatory embryonic cells (i.e., 5-7 somite pairs (sp)) to robustly engraft in transplantation, even after culture, has precluded scientists from properly answering these questions. Here we report robust, multi-lineage and serially transplantable dHSC activity from cultured 2-7sp murine embryonic explants (Em-Ex). dHSC are undetectable in 2-7sp YS explants. Additionally, the engraftment from Em-Ex is confined to an emerging CD31+CD45+c-Kit+CD41- population. In sum, our work supports a model in which the embryo, not the YS, is the major source of lifelong definitive hematopoiesis.

| S-EPMC6302089 | biostudies-other

RNA-sequencing of murine wild-type and Cdx-mutant E9.5 yolk sacs

Project description:E9.5 yolk sacs were collected from wild type (CD1) and Cdx-mutant (DKO) embryos and processed for RNA-sequencing to identify Cdx-dependent changes in gene expression

2022-02-01 | GSE181090 | GEO

RNA-seq reveals conservation of function among the yolk sacs of human, mouse, and chicken.

Project description:The yolk sac is phylogenetically the oldest of the extraembryonic membranes. The human embryo retains a yolk sac, which goes through primary and secondary phases of development, but its importance is controversial. Although it is known to synthesize proteins, its transport functions are widely considered vestigial. Here, we report RNA-sequencing (RNA-seq) data for the human and murine yolk sacs and compare those data with data for the chicken. We also relate the human RNA-seq data to proteomic data for the coelomic fluid bathing the yolk sac. Conservation of transcriptomes across the species indicates that the human secondary yolk sac likely performs key functions early in development, particularly uptake and processing of macro- and micronutrients, many of which are found in coelomic fluid. More generally, our findings shed light on evolutionary mechanisms that give rise to complex structures such as the placenta. We identify genetic modules that are conserved across mammals and birds, suggesting these modules are part of the core amniote genetic repertoire and are the building blocks for both oviparous and viviparous reproductive modes. We propose that although a choriovitelline placenta is never established physically in the human, the placental villi, the exocoelomic cavity, and the secondary yolk sac function together as a physiological equivalent.

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Single cell transcriptome sequencing of CS11 and CS15 human yolk sacs

Project description:Yolk sac is an important site for early embryonic hematopoiesis. However, our understanding of early hematopoietic development is still very limited. Single cell transcriptome sequencing provides us with a good research method. Here, we performed single cell RNA-seq analysis for Carnegie stage 11 (CS11) and Carnegie stage 15 (CS15) human yolk sacs.

2020-02-16 | GSE137010 | GEO

Genome-wide analysis of gene expression of Flk1Cre;ETV2 CKO mouse yolk sacs.

Project description:To identify genes critical for vascular development, we generated mice where ETV2 is inactivated in FLK1+ cells by a loxP-Cre recombination approach. Results provide a detailed insight into the function of ETV2 in emrbyonic vasculare formation. Total RNA obtained from E9.5 yolk sacs from Flk1Cre;ETV2 CKO and control mice.

2014-11-17 | E-GEOD-51407 | biostudies-arrayexpress

Rates of pinocytic capture of simple proteins by rat yolk sacs incubated in vitro.

Project description:The rates of pinocytic uptake of a number of small 125I-labelled simple proteins (insulin, ribonuclease A and lysozyme) by rat yolk sacs incubated in vitro were determined both before and after treating these proteins with reagents that are known to increase the rate of capture of 125I-labelled bovine serum albumin. Uptake of the untreated forms of all three proteins was extremely rapid, indicating that adsorptive pinocytosis is the principal mechanism by which yolk-sac cells capture these simple proteins, but these rates show no simple correlation with molecular charge. In contrast with albumin, the rates of uptake of treated proteins were either unchanged or lower than that of the corresponding untreated protein preparations; polymeric forms of 125I-labelled lysozyme larger than dimers were ingested at rates significantly lower than that of the monomer.

| S-EPMC1163305 | biostudies-other

RNA-sequencing of murine wild-type and Cdx-mutant E9.5 yolk sacs

Project description:RNA-sequencing of murine wild-type and Cdx-mutant E9.5 yolk sacs

| PRJNA750664 | ENA

Genome-wide analysis of gene expression of Flk1Cre;ETV2 CKO mouse yolk sacs.

2014-11-17 | GSE51407 | GEO

Comparison of gene expression pattern between Wild-type and Hypb knockout embryo yolk sacs

Project description:This study aimed at exploring the physiological function of mammalian HYPB by means of knockout mouse model. Homogenous disruption of mouse Hypb gene leads to embryonic lethality at E10.5-E11.5. Severe vascular defects were observed in the Hypb-/- embryos, yolk sac and placenta.In the mutant embryo and yolk sac, disorganized and abnormally dilated capillaries cannot be remodeled into large blood vessels or intricate networks. Thus, our results suggest that the mammalian HYPB HMT plays an important role in embryonic vascularization. Keywords: knockout, mouse embryo development, angiogenesis, yolk sac, E9.0, E10.5

2009-12-28 | GSE10113 | GEO

Effects of weak bases on the degradation of endogenous and exogenous proteins by rat yolk sacs.

Project description:In rat yolk sacs incubated in vitro, the rates of degradation of endogenous [3H]leucine-labelled proteins and of pinocytically ingested 125I-labelled bovine serum albumin were both decreased in the presence of either ammonium, methylammonium or ethylammonium ions (0-20 mM) or much lower concentrations of chloroquine (0-500 microM). These effects were also accompanied by an inhibition of pinocytosis, as measured by the rate of uptake of 125I-labelled polyvinylpyrrolidone, and by a fall in the [ATP]/[ADP] ratio within the tissue. Re-incubation in inhibitor-free medium of yolk sacs previously exposed to a weak base restored pinocytic and proteolytic capacities, except for tissues exposed to chloroquine at concentrations above 0.1 mM (these appeared to be cytotoxic); an attendent rise in [ATP]/[ADP] ratios to near normal values was also observed. Weak bases, at concentrations that fully arrested the breakdown of 125I-labelled albumin, failed to inhibit by more than 45% the degradation of [3H]leucine-labelled endogenous proteins. Since 125I-labelled bovine serum albumin has been shown to be degraded entirely intralysosomally by yolk sacs, this suggests either that the hydrolysis of endogenous proteins is shared between lysosomes and some other site or that, unlike 125I-labelled albumin, some endogenous proteins can be degraded within lysosomes at abnormally high pH.

| S-EPMC1161975 | biostudies-other

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