Differential expression of ZPC in the bovine ovary, oocyte, and embryo

Kölle, Sabine; Sinowatz, Fred; Boie, Gudrun; Palma, G.A.

doi:10.1002/(sici)1098-2795(199804)49:4<435::aid-mrd11>3.0.co;2-t

Cited by 31 publications

(12 citation statements)

References 51 publications

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“…An abrupt increase both in ZPC protein and ZPC mRNA was observed only during the final 48 h of follicular development. In bovine ovaries, the follicle cells, especially the cumulus and corona radiata cells, contribute to ZPC mRNA synthesis to an increasing extent during follicular development, whereas during the early phases of development, the mRNA encoding ZPC is predominantly localized in the oocyte [40].…”

Section: Discussionmentioning

confidence: 99%

“…To date, studies on the hormonal regulation of ZPC production have been limited. The immunohistochemical study of bovine follicles suggested that synthesis of ZPC in follicle cells was influenced by the medium used [40]. A cumulus-oocyte complex matured in vitro in a medium supplemented with FSH, LH, and heat-inactivated estrus cow serum showed high amounts of ZPC as well as enhanced frequencies of in vitro fertilization and blastocyst development.…”

Section: Discussionmentioning

confidence: 99%

“…This might be due to the disruption of the morphology of the granulosa cells and the oocyte. It is quite interesting in this regard that the soluble form of ZPC is present in bovine follicular fluid [40]. Efforts are currently underway to investigate the topology of ZPC secretion, in which selective secretion of ZPC to the apical surface of the granulosa cells forms the perivitelline membrane.…”

Section: Discussionmentioning

confidence: 99%

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Effects of Testosterone on Production of Perivitelline Membrane Glycoprotein ZPC by Granulosa Cells of Japanese Quail (Coturnix japonica)1

Pan

Sasanami

Kono

et al. 2001

Biology of Reproduction

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Avian perivitelline membrane, an investment homologous to the zona pellucida of mammalian oocytes, is composed of at least two glycoproteins. Previous studies have indicated that one of the components, a glycoprotein homologous to mammalian ZPC, is produced and secreted by the granulosa cells of developing follicles of the chicken ovary. In the present study, we evaluated the expression and regulation of ZPC in Japanese quail (Coturnix japonica) granulosa cells both in vivo and in vitro. Western blot analysis of the SDS-solubilized granulosa layer using anti-quail ZPC antiserum showed that the amount of ZPC increased in parallel with follicular development. Northern blot analysis of total RNA using cDNA of quail ZPC showed that the increase in mRNA expression was also correlated with follicular development. To investigate the regulation of ZPC production, the granulosa cells were cultured in a medium containing steroid hormones such as progesterone, estradiol-17ss, or testosterone. By measuring ZPC protein and mRNA with Western and Northern blot analyses, respectively, we found that addition of testosterone maintained ZPC contents in the culture of the granulosa cells, and that ZPC mRNA expression was high in the culture with testosterone compared to the control. These results suggest that testosterone stimulates ZPC protein production at the gene transcription level.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Effects of Testosterone on Production of Perivitelline Membrane Glycoprotein ZPC by Granulosa Cells of Japanese Quail (Coturnix japonica)1

Pan

Sasanami

Kono

et al. 2001

Biology of Reproduction

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“…In some shrews, at least, the acrosome is shed already within the cumulus, and binding to the zona is established apparently by barbs of the perforatorium [57]-structures that, as a matter of some interest, occur also in other insectivores (unpublished results), elephant shrews [58], and even megabats [59]. Moreover, it is intriguing that a zona protein, ZPC, is synthesized by cells of the mature bovine follicle [60], since the cumulus oophorus can induce the acrosome reaction in at least some ''higher'' eutherian mammals as well. Therefore, sometimes acrosomal hydrolases may be released or exposed before contact with the zona.…”

Section: A) the Behavior Of Fertilizing Spermatozoamentioning

confidence: 99%

Mammalian Fertilization Misread? Sperm Penetration of the Eutherian Zona Pellucida Is Unlikely to be a Lytic Event

Bedford

1998

Biology of Reproduction

136

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“…Chicken ZPC differs from those of other species, in that it is expressed and secreted by granulosa cells surrounding an oocyte during rapidly growing stages [25,26], which contrasts with the oocyte-specific expression of mouse zona proteins [27]. In some other mammals, not only oocyte but also the follicle cells contribute to ZPC synthesis [28,29]. In the chicken, another major component, the 97-kDa glycoprotein (gp97), has not yet been characterized.…”

Section: Introductionmentioning

confidence: 99%

Morphological and Biochemical Changes of Isolated Chicken Egg-Envelope During Sperm Penetration: Degradation of the 97-Kilodalton Glycoprotein Is Involved in Sperm-Driven Hole Formation on the Egg-Envelope1

Takeuchi

Cho

Iwata

et al. 2001

Biology of Reproduction

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The chicken egg-envelope is made of two major glycoprotein components, which are designated as gp97 and gp42 (after their molecular masses). To elucidate how these two components are involved in macromolecular organization of the chicken egg-envelope, the isolated egg-envelope was characterized by immunochemical and biochemical methods. The gp97 was suggested to be a homologue of mouse ZPB based on the similarities of N-terminal and internal sequences. Immunoblotting using anti-gp97 monoclonal antibodies and two-dimensional gel electrophoresis with or without mercaptoethanol treatment revealed that gp97 formed a homodimer through disulfide bonds, whereas gp42 did not. Under indirect immunofluorescence microscopy, the anti-gp97 antibody visualized indistinct, small spots on the egg-envelope, whereas the anti-gp42 antibody showed a meshwork of blurry, fibrous structures. The hole formation on the egg-envelope by in vitro sperm penetration was completely inhibited by two anti-gp97 monoclonal antibodies. Interestingly, the anti-gp97 monoclonal antibodies blocked the proteolysis not only of gp97 but also of gp42 during incubation of the egg-envelope with either sperm or the crude chicken acrosin. Taken together, these results indicate that gp97 may play pivotal roles not only in constitution of the macromolecular organization of the egg-envelope but also in triggering hydrolysis of the egg-envelope during sperm penetration.

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Differential expression of ZPC in the bovine ovary, oocyte, and embryo

Cited by 31 publications

References 51 publications

Effects of Testosterone on Production of Perivitelline Membrane Glycoprotein ZPC by Granulosa Cells of Japanese Quail (Coturnix japonica)1

Effects of Testosterone on Production of Perivitelline Membrane Glycoprotein ZPC by Granulosa Cells of Japanese Quail (Coturnix japonica)1

Mammalian Fertilization Misread? Sperm Penetration of the Eutherian Zona Pellucida Is Unlikely to be a Lytic Event

Morphological and Biochemical Changes of Isolated Chicken Egg-Envelope During Sperm Penetration: Degradation of the 97-Kilodalton Glycoprotein Is Involved in Sperm-Driven Hole Formation on the Egg-Envelope1

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