Asynchrony between pronuclear development and protein synthetic changes in zygotes of the mouse derived from oocytes aged postovulation in vivo and fertilized in vivo
| Autor: | C. W. Op Het Veld, M. B. H. Koopman, M. L. Boerjan |
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| Jazyk: | angličtina |
| Rok vydání: | 1990 |
| Předmět: |
Male
Ovulation Time Factors Ratón Zygote Ovary Superovulation Pronuclear zygotes Biology Laboratorium voor Erfelijkheidsleer LHRH Gonadotropin-Releasing Hormone chemistry.chemical_compound Mice In vivo Postovulatory aging Genetics medicine Animals Sodium dodecyl sulfate Gel electrophoresis Embryo Cell Biology Oocyte Molecular biology medicine.anatomical_structure chemistry Fertilization Protein Biosynthesis Oocytes Electrophoresis Polyacrylamide Gel Female Laboratory of Genetics Developmental Biology |
| Zdroj: | Molecular reproduction and development, 27, 344-350 Molecular reproduction and development 27 (1990) |
| ISSN: | 1040-452X |
| Popis: | The pattern of proteins synthesized by one-cell embryos derived from unaged oocytes and oocytes aged postovulation in vivo was analyzed by means of 35S-methionine labeling and gel electrophoresis. The oocytes were obtained after ovulation induction by an injection of luteinizing hormone-releasing hormone (LHRH) at proestrus or after a superovulation procedure. The analysis was performed in unfertilized aged and unaged secondary oocytes and in zygotes derived from them. The patterns of proteins synthesized by secondary oocytes from all experimental groups were very similar: The oocytes showed a predominant synthesis of 35 kDa proteins. Zygotes from aged as well as unaged LHRH-induced oocytes also showed a predominant synthesis of one group of polypeptides with a relative molecular weight of about 35 kDa. The proteins of the 35 kDa protein complex migrated in an upper (u), middle (m), or lower (l) band in 10% polyacrylamide sodium dodecyl sulfate (SDS) gels. The u- and m-band 35 kDa proteins were shown to be synthesized by secondary oocytes. Early pronuclear zygotes from unaged LHRH-induced oocytes synthesized u- and m- but no l-band 35 kDa proteins. In contrast, part (38%, n = 47) of the early pronuclear zygotes from aged LHRH-induced oocytes did synthesize the l-band 35 kDa proteins. Late pronuclear zygotes (LPZ) from aged as well as unaged oocytes synthesized predominantly the l-band 35 kDa proteins. However, although only 5.8% (n = 51) of LPZ from unaged oocytes synthesize m- and l-band 35 kDa proteins, these bands of proteins are present in 25% (n = 24) of the LPZ from aged oocytes. Thus, in zygotes from aged oocytes, at least part of the fertilization-dependent changes in the 35 kDa protein synthetic pattern are advanced with reference to the morphological stage of pronuclear progression. Most (80.6%, n = 36) of the early pronuclear zygotes from unaged superovulated oocytes synthesized u- and m-band 35 kDa proteins, like early pronuclear zygotes from unaged LHRH-induced oocytes. However, 16.7% did not synthesize any of the 35 kDa proteins at all. Thus with respect to the protein synthetic pattern of 35 kDa proteins, zygotes from unaged superovulated oocytes are different from zygotes derived from unaged LHRH-induced oocytes. |
| Databáze: | OpenAIRE |
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