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http://dx.doi.org/10.1002/mrd.21388 | DOI Listing |
Adv Exp Med Biol
November 2018
Center for Applied and Experimental Genomics, Department of Biology, San Diego State University, San Diego, CA, USA.
Embryonic development depends on the orchestration of hundreds of regulatory and structural genes to initiate expression at the proper time, in the correct spatial domain(s), and in the amounts required for cells and tissues to become specified, determined, and ultimately to differentiate into a multicellular embryo. One of the key approaches to studying embryonic development is the generation of transgenic animals in which recombinant DNA molecules are transiently or stably introduced into embryos to alter gene expression, to manipulate gene function or to serve as reporters for specific cell types or subcellular compartments. In some model systems, such as the mouse, well-defined approaches for generating transgenic animals have been developed.
View Article and Find Full Text PDFOne of the hypotheses suggests that test cells play a part in a larval tunic formation like morula cells in adult ascidians. It was shown that the antibodies against morula cell proteins of 26 and 48 kDa of the ascidian Styela rustica react on the paraffin sections with both the granules of morula cells and test cells of ascidians S. rustica and Boltenia echinata.
View Article and Find Full Text PDFMol Reprod Dev
March 2012
University of Washington, Department of Biology, Seattle, WA 98195, USA.
Mol Reprod Dev
March 2012
Friday Harbor Laboratories, University of Washington, Friday Harbor, Washington, USA.
Most mature ascidian oocytes undergo germinal vesicle breakdown (GVBD) when released by the ovary into sea water (SW). Acidic SW blocks this but they can be stimulated by raising the pH, increasing intracellular cAMP levels by cell permeant forms, inhibiting its breakdown or causing synthesis. Boltenia villosa oocytes undergo GVBD in response to these drugs.
View Article and Find Full Text PDFInt J Dev Biol
March 2011
Department of Biology, St. Francis-Xavier University, 2320 Notre Dame Ave., Antigonish, Nova Scotia, Canada.
Heat shock protein 90 (HSP90) is a ubiquitously expressed molecular chaperone that controls the folding, assembly and activity of proteins, many of which are involved in signal transduction. Recent work has shown that HSP90 is present extracellularly, indicating a heretofore under-appreciated requirement for extracellular chaperoning, particularly among migratory cells. We applied immunological and surgical techniques to document the differential expression of HSP90 during ascidian development.
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