Synthesis of fucosyl-containing glycoproteins of the vitelline coat in oocytes of Ciona intestinalis (Ascidia).
نویسندگان
چکیده
The sperm receptors of the ascidian oocyte are located at the outer surface of the vitelline coat (formerly called the chorion). The fucose residues are the receptor's most important components for sperm recognition and binding. We asked whether the fucosyl-containing glycoproteins of the vitelline coat are a product of the oocyte, the follicle cells, or the test cells. Ovaries of Ciona intestinalis were injected with L-[3H]fucose and the progress of its incorporation was followed by using autoradiography and sodium dodecyl sulfate/polyacrylamide gel electrophoresis of the injected gonads and of the isolated vitelline coats. We found that incorporation of fucose begins within the vitellogenic oocytes, and fucose slowly accumulates in the differentiating vitelline coat. At no time could fucose incorporation be detected in the follicle cells or in the test cells. Sodium dodecyl sulfate/polyacrylamide gel electrophoresis of vitelline coats prepared from the injected ovaries showed fucose incorporation into the same three glycoproteins present in vitelline coats from mature oocytes and identified by their affinity for 125I-labeled fucose-binding protein [Pinto, M. R., De Santis, R., D'Alessio, G. & Rosati, F. (1981) Exp. Cell Res. 132, 289-295]. A radioactive band not found in the mature oocyte was also present.
منابع مشابه
Follicle cell proteasome activity and acid extract from the egg vitelline coat prompt the onset of self-sterility in Ciona intestinalis oocytes.
In the hermaphrodite ascidian Ciona intestinalis, the egg vitelline coat (VC) controls gamete self-nonself discrimination. Oocytes, after germinal vesicle breakdown, can be fertilized by both self and nonself sperm. However, a barrier to fertilization by self sperm progressively develops in the VC in the 3 hours after germinal vesicle breakdown. During this period, follicle cells attached to th...
متن کاملThe hsp70 protein is involved in the acquisition of gamete self-sterility in the ascidian Ciona intestinalis.
In the hermaphrodite ascidian Ciona intestinalis, gamete self-incompatibility is a mechanism that prevents self-fertilization and is based on the ability of the oocyte vitelline coat to distinguish and accept only heterologous spermatozoa. The onset of self-sterility occurs during oogenesis and involves or is controlled by the follicle cells. Gamete self-nonself discrimination, a process that c...
متن کاملAllorecognition mechanisms during ascidian fertilization.
Ascidians (primitive chordates) are hermaphroditic animals, releasing sperm and eggs nearly simultaneously. But, many ascidians, including Ciona intestinalis and Halocynthia roretzi, show self-sterility or preference for cross-fertilization rather than self-fertilization. The molecular mechanisms underlying this allorecognition process are only poorly understood. We recently identified the gene...
متن کاملComprehensive egg coat proteome of the ascidian Ciona intestinalis reveals gamete recognition molecules involved in self-sterility.
Despite central roles of egg coat proteins in gamete recognition, their functions and composition are poorly understood. Here, we report that the proteome of the egg coat in the solitary ascidian Ciona intestinalis, called vitelline coat (VC) fraction, contains more than 800 proteins identified by mass spectrometry-based analyses. Over 100 proteins were enriched in the VC fraction compared with...
متن کاملNovel vanadium-binding proteins (vanabins) identified in cDNA libraries and the genome of the ascidian Ciona intestinalis.
Ascidians, especially those belonging to the suborder Phlebobranchia, can accumulate high levels of vanadium. Vanadium-binding proteins (vanabins) were first isolated from a vanadium-accumulating ascidian, Ascidia sydneiensis samea, and then the vanabins were cloned, their expression was studied, and metal-binding assays were conducted. In order to unravel the mechanism of vanadium accumulation...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Proceedings of the National Academy of Sciences of the United States of America
دوره 79 6 شماره
صفحات -
تاریخ انتشار 1982