The preimplantation mammalian embryo: Characterization of intercellular junctions and their appearance during development

Ducibella, Tom; Albertini, David F.; Anderson, Everett; Biggers, John D.

doi:10.1016/0012-1606(75)90063-9

Cited by 342 publications

(120 citation statements)

References 34 publications

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“…Grey to silver sections were obtained with a diamond knife, collected on 3% formvar-coated 150-mesh grids, and stained for 15-30 sec with uranyl acetate (Watson, 1958) followed by lead (Sato, 1958). Embryos were processed for freeze fracturing as described by Ducibella, Albertini, Anderson & Biggers (1975 Excluding the non-detectable samples, the mean ± S.E.M. progesterone concentration in blastocysts averaged 2-9 ± 0-3 ng/ml from 110-159 hp.c.…”

Section: Electron Microscopymentioning

confidence: 99%

Accumulation of steroids in rabbit preimplantation blastocysts

Borland¹,

Erickson²,

Ducibella³

1977

Reproduction

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Summary. The concentrations of progesterone, androstenedione, testosterone, oestrone and oestradiol were measured by radioimmunoassay in blastocysts and uterine fluid flushings collected from rabbits 110 to 159 h post coitum (p.c.). None of the blastocysts or uterine flushings contained detectable levels of androstenedione, testosterone or oestrone. All uterine flushings contained large amounts of progesterone and some of the flushings also contained oestradiol.A small amount of progesterone (\ m=~\ 7\ m=. \ 5pg/blastocyst) was first detectable in some blastocysts at 135 h p.c.; progesterone levels/blastocyst then increased progressively, reaching levels of about 122\p=n-\158 pg/blastocyst at 159 h p.c. Micropuncture of blastocysts at 159 h p.c. indicated that \ m=ge\ 90 % of the progesterone in the embryo was in the blastocoelic fluid. Blastocysts from rabbit uterine horns containing oestradiol also contained oestradiol but those in which oestradiol was detected were never observed in uteri lacking the hormone. It is inferred that rabbit blastocysts accumulate both progesterone and oestradiol from uterine fluid.

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Section: Electron Microscopymentioning

confidence: 99%

Accumulation of steroids in rabbit preimplantation blastocysts

Borland¹,

Erickson²,

Ducibella³

1977

Reproduction

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“…The interpretation of the effect of any agent that may modify desmosome formation will always be complicated by the possibility of indirect effects via other tissues . Furthermore, in these models, desmosome development per se cannot be separated from the maturational processes of the interacting cells (1,16,44,65).…”

mentioning

confidence: 99%

Desmosome development in an in vitro model.

Dembitzer¹,

Herz²,

Schermer³

et al. 1980

The Journal of Cell Biology

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“…Adherens junctions arise during embryogenesis at the 8-to 16-cell stage during compaction. Desmosome formation follows shortly thereafter (Ducibella et al, 1975;Jackson et al, 1980;Fleming et al, 1991;Gallicano et al, 1998). It is tempting to propose that kaz/actin binding at preimplantation stages may be a prerequisite for guiding actin to newly forming adherens junction.…”

Section: Fig 12 A-fmentioning

confidence: 99%

“…At the molecular level, the most common feature to each transition is a complete remodeling of specific cytoskeletal components. In fact, decades of research have explicitly shown that the cytoskeleton is a driving force for each transition (Ducibella et al, 1975;Schatten et al, 1985;Bement et al, 1992;Riethmacher et al, 1995;Clayton et al, 1999;Pauken and Capco, 1999;Gallicano, 2001, and references therein). Furthermore, each cytoskeletal system (i.e., actin, microtubules, and intermediate filaments) has adapted specialized features to allow them to push through the developmental transition.…”

Section: Fig 12 A-fmentioning

confidence: 99%

Dynamics and unexpected localization of the plakin binding protein, kazrin, in mouse eggs and early embryos

Gallicano

Foshay

Pengetnze

et al. 2005

Developmental Dynamics

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The cell uses the cytoskeleton in virtually every aspect of cell survival and function. One primary function of the cytoskeleton is to connect to and stabilize intercellular junctions. To accomplish this task, microtubules, actin filaments, and intermediate filaments utilize cytolinker proteins, which physically bind the cytoskeletal filament to the core proteins of the adhesion junction. The plakin family of linker proteins have been in the spotlight recently as critical components for embryo survival and, when mutated, the cause of diseases such as muscular dystrophy and cardiomyopathies. Here, we reveal the dynamics of a recently discovered plakin binding protein, kazrin (kaz), during early mouse development. Kaz was originally found in adult tissues, primarily epidermis, linking periplakin to the plasma membrane and colocalizing with desmoplakin in desmosomes. Using reverse transcriptase-polymerase chain reaction, Western blots, and confocal microscopy, we found kaz in unfertilized eggs associated with the spindle apparatus and cytoskeletal sheets. As quickly as 5 min after egg activation, kaz relocates to a diffuse peri-spindle position, followed 20 -30 min later by clear localization to the presumptive cytokinetic ring. Before the blastocyst stage of development, kaz associates with the nuclear matrix in a cell cycle-dependent manner, and also associates with the cytoplasmic actin cytoskeleton. After blastocyst formation, kaz localization and potential function(s) become highly complex as it is found associating with cell-cell junctions, the cytoskeleton, and nucleus. Postimplantation stages of development reveal that kaz retains a multifunctional, tissue-specific role as it is detected at diverse locations in various embryonic tissue types.

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The preimplantation mammalian embryo: Characterization of intercellular junctions and their appearance during development

Cited by 342 publications

References 34 publications

Accumulation of steroids in rabbit preimplantation blastocysts

Accumulation of steroids in rabbit preimplantation blastocysts

Desmosome development in an in vitro model.

Dynamics and unexpected localization of the plakin binding protein, kazrin, in mouse eggs and early embryos

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