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Familial Testicular Germ Cell Tumor
Published in Dongyou Liu, Handbook of Tumor Syndromes, 2020
Immunohistochemical markers for TGCT consist of PLAP, OCT3/4 (POU5F1), NANOG, SOX2, REX1, AP-2γ (TFAP2C), LIN28, etc., which are expressed in primordial germ cells/gonocytes and embryonic pluripotency-related cells but not in normal adult germ cells. Other diagnostic markers include HMGA1, HMGA2, kinase Aurora-B (which is present in IGCNU, seminomas, and embryonal carcinomas but not in teratomas and YST) [50,51].
Epigenetic Reprogramming of Mammalian Primordial Germ Cells
Published in Cristina Camprubí, Joan Blanco, Epigenetics and Assisted Reproduction, 2018
Sebastian Canovas, Susana M. Chuva de Sousa Lopes
When the mouse embryo reaches the blastocyst stage (E3.5), the cells of the inner cell mass (ICM), express a combination of pluripotency genes (Pou5f1, Nanog, Sox2), that bind the Xist promoter/exon1 silencing it (70). In addition, POUF51 and ZFP42 (or REX1) upregulate the long non-coding Tsix, antisense of Xist. Subsequently Tsix and Xist dimerize forming a double-strand that is targeted for degradation via the RNAi machinery (71). Hence, Xist is downregulated and the silent X chromosome is reactivated. Half a day later (E4.0), each ICM cell undergoes X chromosome inactivation again, this time random X inactivation. Prior to implantation, mouse blastocysts are formed by ICM cells (with random X inactivation) and extraembryonic (trophectoderm and primitive endoderm) cells (with imprinted X inactivation). The Xi is transmitted to the daughter cells by mitosis and so the female embryo develops as mosaic, showing clonal expansion of cells with either a maternal or paternal Xi.
Cell Populations Isolated from Amnion, Chorion, and Wharton’s Jelly of Human Placenta
Published in Ornella Parolini, Antonietta Silini, Placenta, 2016
Francesco Alviano, Roberta Costa, Laura Bonsi
The embryological origin of amniotic epithelium, which derives from the epiblast before gastrulation, may suggest that some cells in this tissue could show pluripotency. Different groups have studied hAECs for the expression of molecular markers of pluripotency, such as OCT-4 (octamer-binding protein 4), SOX2 (SRY-related HMG-box gene 2), FGF4, REX1, and NANOG (Miki et al. 2005; Miki and Strom 2006; Parolini et al. 2008). OCT-4 is known to have a central role in maintaining pluripotency and self-renewal of stem cells, but the only expression of OCT-4 observed in most hAECs is not sufficient to confirm hAEC pluripotential activity. To assess pluripotency in vitro, a clonal expansion from a single hAEC should be demonstrated, but hAECs do not survive as single cells in culture, they do not keep their stem cell characteristics, and they rapidly fall into senescence. The teratoma formation assay could also be used to demonstrate in vitro pluripotency, but hAECs do not form teratomas when injected in immunodeficient mice (Miki et al. 2005; Ilancheran et al. 2007). Based on these data, we can affirm that pluripotency of hAECs has yet to been proven and further investigations are needed (Miki and Strom 2006).
Cognitive impairment with diabetes mellitus and metabolic disease: innovative insights with the mechanistic target of rapamycin and circadian clock gene pathways
Published in Expert Review of Clinical Pharmacology, 2020
mTORC2 has both similarities and differences to mTORC1. mTORC2 is composed of Rictor, mLST8, Deptor, the mammalian stress-activated protein kinase interacting protein (mSIN1), and the protein observed with Rictor-1 (Protor-1) [54]. mTORC2 controls cytoskeleton remodeling through PKCα and cell migration through the Rac guanine nucleotide exchange factors P-Rex1 and P-Rex2 and through Rho signaling [64]. mTORC2 activates protein kinases that includes glucocorticoid induced protein kinase 1 (SGK1), a member of the protein kinase A/protein kinase G/protein kinase C (AGC) family of protein kinases. Protor-1, a Rictor-binding subunit of mTORC2, activates SGK1 [65,66]. The kinase domain of mTOR phosphorylates mSIN1 and prevents lysosomal degradation of this protein. Rictor and mSIN1 also can phosphorylate Akt at serine473 and foster threonine308 phosphorylation by phosphoinositide-dependent kinase 1 (PDK1) to enhance cell survival.
Protein biomarkers for subtyping breast cancer and implications for future research
Published in Expert Review of Proteomics, 2018
Claudius Mueller, Amanda Haymond, Justin B. Davis, Alexa Williams, Virginia Espina
The Rac activator, P-REX1, was found by mass spectrometry profiling of MCF7 cell lines during a screening for phosphatidylinositol 3,4,5-triphosphate-regulated proteins [115]. Using the RPPA data from the TCGA primary breast cancer cohort [116], P-REX1 was found to be inversely correlated with PI3K pathway inhibition and P-REX1 levels decreased with loss of PTEN. Both protein and mRNA levels of P-REX1 were positively correlated with ER [115]. P-REX1 was also shown to be elevated in ER+ luminal breast tumors. P-REX1 will need to be verified in larger cohorts of microdissected tumors to fully assess its tumor or stroma-related biology.