Parp-1deficiency in ES cells promotes invasive and metastatic lesions accompanying induction of trophoblast giant cells during tumorigenesis in uterine environment

2013 ◽  
Vol 63 (8) ◽  
pp. 408-414 ◽  
Author(s):  
Tadashige Nozaki ◽  
Hiroaki Fujimori ◽  
Junhui Wang ◽  
Hiroshi Suzuki ◽  
Hiroshi Imai ◽  
...  
Keyword(s):  
Es Cells ◽  
Giant Cells ◽  
Metastatic Lesions ◽  
Uterine Environment ◽  
Trophoblast Giant Cells

The mechanism of mouse egg-cylinder morphogenesis in vitro

Development ◽  
1981 ◽  
Vol 61 (1) ◽  
pp. 277-287
Author(s):  
A. J. Copp
Keyword(s):  
Giant Cell ◽  
Cell Formation ◽  
Cell Movement ◽  
Giant Cells ◽  
Cell Number ◽  
Dependent Change ◽  
Morphogenesis In Vitro ◽  
Trophoblast Giant Cells

The number of trophoblast giant cells in outgrowths of mouse blastocysts was determined before, during and after egg-cylinder formation in vitro. Giant-cell numbers rose initially but reached a plateau 12 h before the egg cylinder appeared. A secondary increase began 24 h after egg-cylinder formation. Blastocysts whose mural trophectoderm cells were removed before or shortly after attachment in vitro formed egg cylinders at the same time as intact blastocysts but their trophoblast outgrowths contained fewer giant cells at this time. The results support the idea that egg-cylinder formation in vitro is accompanied by a redirection of the polar to mural trophectoderm cell movement which characterizes blastocysts before implantation. The resumption of giant-cell number increase in trophoblast outgrowths after egg-cylinder formation may correspond to secondary giant-cell formation in vivo. It is suggested that a time-dependent change in the strength of trophoblast cell adhesion to the substratum occurs after blastocyst attachment in vitro which restricts the further entry of polar cells into the outgrowth and therefore results in egg-cylinder formation.

Replication Timing Predicts Underreplicated Domains in Polyploid Trophoblast Giant Cells

Placenta ◽  
2013 ◽  
Vol 34 (9) ◽  
pp. A8
Author(s):  
Roberta Hannibal ◽  
Edward Chuong ◽  
Juan Carlos Rivera Mulia ◽  
David Gilbert ◽  
Anton Valouev ◽  
...  
Keyword(s):  
Replication Timing ◽  
Giant Cells ◽  
Trophoblast Giant Cells

scholarly journals A molecular mechanism of mouse placental spongiotrophoblast differentiation regulated by prolyl oligopeptidase

Zygote ◽  
2019 ◽  
Vol 27 (1) ◽  
pp. 49-53
Author(s):  
Yuki Maruyama ◽  
Atsushi P. Kimura
Keyword(s):  
Molecular Mechanism ◽  
Critical Role ◽  
Specific Inhibitor ◽  
Cell Types ◽  
Giant Cells ◽  
Akt Pathway ◽  
Prolyl Oligopeptidase ◽  
Trophoblast Stem ◽  
Trophoblast Stem Cell ◽  
Trophoblast Giant Cells

SummaryIn eutherian mammals, the placenta plays a critical role in embryo development by supplying nutrients and hormones and mediating interaction with the mother. To establish the fine connection between mother and embryo, the placenta needs to be formed normally, but the mechanism of placental differentiation is not fully understood. We previously revealed that mouse prolyl oligopeptidase (POP) plays a role in trophoblast stem cell (TSC) differentiation into two placental cell types, spongiotrophoblasts (SpT) and trophoblast giant cells. Here, we focused on SpT differentiation and attempted to elucidate a molecular mechanism. ForAscl2,Arnt, andEgfrgenes that are indispensable for SpT formation, we found that a POP-specific inhibitor, SUAM-14746, significantly decreasedAscl2expression, which was consistent with a significant decrease in expression ofFlt1, a gene downstream ofAscl2. Although this downregulation was unlikely to be mediated by the PI3K-Akt pathway, our results indicated that POP controls TSC differentiation into SpT by regulating theAscl2gene.

scholarly journals Reciprocal expression of 17α-hydroxylase-C17,20-lyase and aromatase cytochrome P450 during bovine trophoblast differentiation: a two-cell system drives placental oestrogen synthesis

Reproduction ◽  
2006 ◽  
Vol 131 (4) ◽  
pp. 669-679 ◽  
Author(s):  
G Schuler ◽  
G R Özalp ◽  
B Hoffmann ◽  
N Harada ◽  
P Browne ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Cell Types ◽  
Staining Intensity ◽  
Giant Cells ◽  
Cell System ◽  
Cellular Level ◽  
Specific Staining ◽  
Cytoplasmic Staining ◽  
Distinct Cell ◽  
Trophoblast Giant Cells

No definitive information is yet available on the steroidogenic capacity of the two morphologically distinct cell types forming the bovine trophoblast, the uninucleated trophoblast cells (UTCs) and the trophoblast giant cells (TGCs). Hence, in order to localise 17α-hydroxylase-C17,20-lyase (P450c17) on a cellular level and to monitor its expression as a function of gestational age, placentomes from pregnant (days 80–284; n = 19), prepartal (days 273–282; 24–36 h prior to the onset of labour; n = 3) and parturient cows (n = 5) were immunostained for P450c17 using an antiserum against the recombinant bovine enzyme. At all stages investigated, P450c17 was exclusively found in the UTCs of chorionic villi (CV), where staining was ubiquitous between days 80 and 160, but was largely restricted to primary CV and the branching sites of secondary CV between days 160 and 240. Thereafter, a distinct ubiquitous staining reoccurred in the UTCs of all CV in late pregnant, prepartal and parturient animals. Using an antiserum against human aromatase cytochrome P450 (P450arom), specific cytoplasmic staining was observed in TGCs. In placentomes from pregnant cows, staining intensity was higher in mature compared with immature TGCs and was more pronounced in the trophoblast covering big stem villi compared with the trophoblast at other sites of the villous tree. In placentomes of a parturient cow, specific staining was only found in mature TGCs that survived the normal, but substantial, prepartal decline in TGC numbers. These results clearly showed that bovine UTCs and TGCs exhibit different steroidogenic capacities, constituting a ‘two-cell’ organisation for oestrogen synthesis. P450c17 expression appears to be quickly down-regulated and P450arom is up-regulated when UTCs enter the TGC differentiation pathway.

scholarly journals Periodic Expression of the Cyclin-dependent Kinase Inhibitor p57Kip2 in Trophoblast Giant Cells Defines a G2-like Gap Phase of the Endocycle

2000 ◽  
Vol 11 (3) ◽  
pp. 1037-1045 ◽  
Author(s):  
Naka Hattori ◽  
Tyler C. Davies ◽  
Lynn Anson-Cartwright ◽  
James C. Cross
Keyword(s):  
Dna Replication ◽  
Protein Targeting ◽  
Kinase Inhibitor ◽  
Phosphorylation Site ◽  
Giant Cells ◽  
S Phase ◽  
Stable Form ◽  
Cdk Inhibitor ◽  
Cyclin Dependent Kinase ◽  
Trophoblast Giant Cells

Endoreduplication is an unusual form of cell cycle in which rounds of DNA synthesis repeat in the absence of intervening mitoses. How G1/S cyclin-dependent kinase (Cdk) activity is regulated during the mammalian endocycle is poorly understood. We show here that expression of the G1/S Cdk inhibitor p57Kip2 is induced coincidentally with the transition to the endocycle in trophoblast giant cells.Kip2 mRNA is constitutively expressed during subsequent endocycles, but the protein level fluctuates. In trophoblast giant cells synchronized for the first few endocycles, the p57Kip2 protein accumulates only at the end of S-phase and then rapidly disappears a few hours before the onset of the next S-phase. The protein becomes stabilized by mutation of a C-terminal Cdk phosphorylation site. As a consequence, introduction of this stable form of p57Kip2 into giant cells blocks S-phase entry. These data imply that p57Kip2 is subject to phosphorylation-dependent turnover. Surprisingly, although this occurs in endoreduplicating giant cells, p57Kip2 is stable when ectopically expressed in proliferating trophoblast cells, indicating that these cells lack the mechanism for protein targeting and/or degradation. These data show that the appearance of p57Kip2punctuates the completion of DNA replication, whereas its turnover is subsequently required to initiate the next round of endoreduplication in trophoblast giant cells. Cyclical expression of a Cdk inhibitor, by terminating G1/S Cdk activity, may help promote the resetting of DNA replication machinery.

Sign in / Sign up

Export Citation Format

Share Document