Jianchao Huo - Academia.edu (original) (raw)
Papers by Jianchao Huo
Histochemistry and cell biology, Mar 26, 2024
Biologia, 2019
Myosin heavy chain 11 (MYH11), a member of the myosin family, is an actin-based cytoskeletal moto... more Myosin heavy chain 11 (MYH11), a member of the myosin family, is an actin-based cytoskeletal motor protein. Limited previous studies have revealed that the Myh11 gene is expressed in cumulus cells, cumulus-oocyte complexes, and ovarian theca cells. However, its expression profiles in mouse tissues, oocytes and preimplantation embryos are largely unknown. Here, we found that the MYH11 protein was expressed in multiple mouse tissues. In the ovary, the MYH11 protein was highly expressed in oocytes and smooth muscle fiber cells. After ovulation and fertilization, Myh11 mRNA expression had sharply declined in zygotes and could not be detected from 8-cell to blastocyst stages, while the protein persisted until the blastocyst stage. Furthermore, the MYH11 protein was localized in the cytoplasm of oocytes and preimplantation embryos. These results provide the first evidence that MYH11 is enriched in oocytes and early embryos and might play a key role in oogenesis and early embryogenesis of mice.
Theriogenology, 2019
Ribosomal protein S3 (RpS3), a member of the ribosome 40S subunit, has conventional ribosomal fun... more Ribosomal protein S3 (RpS3), a member of the ribosome 40S subunit, has conventional ribosomal function and additional extraribosomal functions. The aim of the present study was to analyze the expression and localization of RpS3 and its function in early embryogenesis in mice. RpS3 mRNA and protein were expressed in multiple mouse tissues. In the ovary, RpS3 protein was ubiquitously and highly expressed in oocytes and granulosa cells. After ovulation and fertilization, RpS3 mRNA and protein were detected in oocytes and preimplantation embryos. Furthermore, RpS3 protein was localized in the cytoplasm of oocytes and preimplantation embryos. Moreover, knockdown of RpS3 in zygotes led to a significantly decreased rate of blastocyst formation. These results provide the first evidence for a novel function of RpS3 in regulating early embryonic development in mice.
Asian-Australasian Journal of Animal Sciences, 2019
Objective: Uncoupling protein 3 gene (UCP3) is a candidate gene associated with the meat quality ... more Objective: Uncoupling protein 3 gene (UCP3) is a candidate gene associated with the meat quality of pigs. The aim of this study was to explore the regulation mechanism of UCP3 expres sion and provide a theoretical basis for the research of the function of porcine UCP3 gene in meat quality. Methods: Bisulfite sequencing polymerase chain reaction (PCR) and quantitative realtime PCR (QPCR) were used to analyze the methylation of UCP3 5′flanking region and UCP3 mRNA expression in the adipose tissue or skeletal muscle of three pig breeds at different ages (1, 90, 210dayold Putian Black pig; 90dayold Duroc; and 90dayold Dupu). Results: Results showed that two cytosineguanine dinucleotide (CpG) islands are present in the promoter region of porcine UCP3 gene. The second CpG island located in the core promoter region contained 9 CpG sites. The methylation level of CpG island 2 was lower in the adipose tissue and skeletal muscle of 90dayold Putian Black pigs compared with 1day old and 210dayold Putian Black pigs, and the difference also existed in the skeletal muscle among the three 90dayold pig breeds. Furthermore, the obvious changing difference of UCP3 mRNA expression was observed in the skeletal muscle of different groups. However, the difference of methylation status and expression level of UCP3 gene was not significant in the adipose tissue. Conclusion: Our data indicate that UCP3 mRNA expression level was associated with the methylation status of UCP3 promoter in the skeletal muscle of pigs.
Biology of Reproduction, 2018
Valosin-containing protein (VCP) is a member of the highly conserved AAA (ATPase associated with ... more Valosin-containing protein (VCP) is a member of the highly conserved AAA (ATPase associated with a variety of cellular activities) superfamily. A previous study has shown that targeted deletion of Vcp in mice results in early embryonic lethality. The aim of the present study was to analyze the expression and localization of VCP and its function in meiotic arrest of mouse oocytes. Vcp mRNA and protein were expressed in multiple mouse tissues. In the ovary, VCP protein was mainly expressed in oocytes and granulosa cells. After ovulation and fertilization, Vcp mRNA and protein were detected in oocytes and preimplantation embryos. Furthermore, VCP protein was localized in both the cytoplasm and nucleus of germinal vesicle (GV)-stage oocytes and preimplantation embryos. Moreover, knockdown of Vcp in GV-stage oocytes led to a significantly increased rate of germinal vesicle breakdown (GVBD). In addition, inhibition of VCP protein improved the GVBD rate in mouse GV-stage oocytes. When VCP inhibition was reversed, the final GVBD rate returned to normal. These results provide the first evidence for a novel function of VCP in meiotic arrest of mouse oocytes.
The Journal of reproduction and development, Jan 9, 2018
Fas-associated protein factor 1 (FAF1) is a Fas-associated protein that functions in multiple cel... more Fas-associated protein factor 1 (FAF1) is a Fas-associated protein that functions in multiple cellular processes. Previous research showed that mutations in Faf1 led to the lethality of cleavage stage embryos in a mouse model. The aim of the present study was to analyze the expression pattern, localization, and function of FAF1 in meiotic resumption of mouse oocytes. FAF1 was exclusively expressed in oocytes at various follicular stages within the ovary and was predominantly localized in the cytoplasm of growing oocytes. Furthermore, Faf1 mRNA and protein were persistently present during oocyte maturation and Faf1 mRNA levels were similar in the germinal vesicle (GV), GV breakdown (GVBD), and metaphase II (MII) stages of oocytes. Moreover, knockdown of Faf1 in GV-stage oocytes led to a significantly decreased rate of GVBD. To our knowledge, these results provide the first evidence regarding a novel function of FAF1 in meiotic resumption in mouse oocytes.
Reproduction (Cambridge, England), Sep 19, 2017
Nlrp2 is a maternal effect gene specifically expressed by mouse ovaries; deletion of this gene fr... more Nlrp2 is a maternal effect gene specifically expressed by mouse ovaries; deletion of this gene from zygotes is known to result in early embryonic arrest. In the present study, we identified FAF1 protein as a specific binding partner of the NLRP2 protein in both mouse oocytes and preimplantation embryos. In addition to early embryos, both Faf1 mRNA and protein were detected in multiple tissues. NLRP2 and FAF1 proteins were co-localized to both the cytoplasm and nucleus during the development of oocytes and preimplantation embryos. Co-immunoprecipitation assays were used to confirm the specific interaction between NLRP2 and FAF1 proteins. Knockdown of the Nlrp2 or Faf1 gene in zygotes interfered with the formation of a NLRP2-FAF1 complex and led to developmental arrest during early embryogenesis. We therefore conclude that NLRP2 interacts with FAF1 under normal physiological conditions and that this interaction is probably essential for the successful development of cleavage-stage mou...
Histochemistry and cell biology, Mar 26, 2024
Biologia, 2019
Myosin heavy chain 11 (MYH11), a member of the myosin family, is an actin-based cytoskeletal moto... more Myosin heavy chain 11 (MYH11), a member of the myosin family, is an actin-based cytoskeletal motor protein. Limited previous studies have revealed that the Myh11 gene is expressed in cumulus cells, cumulus-oocyte complexes, and ovarian theca cells. However, its expression profiles in mouse tissues, oocytes and preimplantation embryos are largely unknown. Here, we found that the MYH11 protein was expressed in multiple mouse tissues. In the ovary, the MYH11 protein was highly expressed in oocytes and smooth muscle fiber cells. After ovulation and fertilization, Myh11 mRNA expression had sharply declined in zygotes and could not be detected from 8-cell to blastocyst stages, while the protein persisted until the blastocyst stage. Furthermore, the MYH11 protein was localized in the cytoplasm of oocytes and preimplantation embryos. These results provide the first evidence that MYH11 is enriched in oocytes and early embryos and might play a key role in oogenesis and early embryogenesis of mice.
Theriogenology, 2019
Ribosomal protein S3 (RpS3), a member of the ribosome 40S subunit, has conventional ribosomal fun... more Ribosomal protein S3 (RpS3), a member of the ribosome 40S subunit, has conventional ribosomal function and additional extraribosomal functions. The aim of the present study was to analyze the expression and localization of RpS3 and its function in early embryogenesis in mice. RpS3 mRNA and protein were expressed in multiple mouse tissues. In the ovary, RpS3 protein was ubiquitously and highly expressed in oocytes and granulosa cells. After ovulation and fertilization, RpS3 mRNA and protein were detected in oocytes and preimplantation embryos. Furthermore, RpS3 protein was localized in the cytoplasm of oocytes and preimplantation embryos. Moreover, knockdown of RpS3 in zygotes led to a significantly decreased rate of blastocyst formation. These results provide the first evidence for a novel function of RpS3 in regulating early embryonic development in mice.
Asian-Australasian Journal of Animal Sciences, 2019
Objective: Uncoupling protein 3 gene (UCP3) is a candidate gene associated with the meat quality ... more Objective: Uncoupling protein 3 gene (UCP3) is a candidate gene associated with the meat quality of pigs. The aim of this study was to explore the regulation mechanism of UCP3 expres sion and provide a theoretical basis for the research of the function of porcine UCP3 gene in meat quality. Methods: Bisulfite sequencing polymerase chain reaction (PCR) and quantitative realtime PCR (QPCR) were used to analyze the methylation of UCP3 5′flanking region and UCP3 mRNA expression in the adipose tissue or skeletal muscle of three pig breeds at different ages (1, 90, 210dayold Putian Black pig; 90dayold Duroc; and 90dayold Dupu). Results: Results showed that two cytosineguanine dinucleotide (CpG) islands are present in the promoter region of porcine UCP3 gene. The second CpG island located in the core promoter region contained 9 CpG sites. The methylation level of CpG island 2 was lower in the adipose tissue and skeletal muscle of 90dayold Putian Black pigs compared with 1day old and 210dayold Putian Black pigs, and the difference also existed in the skeletal muscle among the three 90dayold pig breeds. Furthermore, the obvious changing difference of UCP3 mRNA expression was observed in the skeletal muscle of different groups. However, the difference of methylation status and expression level of UCP3 gene was not significant in the adipose tissue. Conclusion: Our data indicate that UCP3 mRNA expression level was associated with the methylation status of UCP3 promoter in the skeletal muscle of pigs.
Biology of Reproduction, 2018
Valosin-containing protein (VCP) is a member of the highly conserved AAA (ATPase associated with ... more Valosin-containing protein (VCP) is a member of the highly conserved AAA (ATPase associated with a variety of cellular activities) superfamily. A previous study has shown that targeted deletion of Vcp in mice results in early embryonic lethality. The aim of the present study was to analyze the expression and localization of VCP and its function in meiotic arrest of mouse oocytes. Vcp mRNA and protein were expressed in multiple mouse tissues. In the ovary, VCP protein was mainly expressed in oocytes and granulosa cells. After ovulation and fertilization, Vcp mRNA and protein were detected in oocytes and preimplantation embryos. Furthermore, VCP protein was localized in both the cytoplasm and nucleus of germinal vesicle (GV)-stage oocytes and preimplantation embryos. Moreover, knockdown of Vcp in GV-stage oocytes led to a significantly increased rate of germinal vesicle breakdown (GVBD). In addition, inhibition of VCP protein improved the GVBD rate in mouse GV-stage oocytes. When VCP inhibition was reversed, the final GVBD rate returned to normal. These results provide the first evidence for a novel function of VCP in meiotic arrest of mouse oocytes.
The Journal of reproduction and development, Jan 9, 2018
Fas-associated protein factor 1 (FAF1) is a Fas-associated protein that functions in multiple cel... more Fas-associated protein factor 1 (FAF1) is a Fas-associated protein that functions in multiple cellular processes. Previous research showed that mutations in Faf1 led to the lethality of cleavage stage embryos in a mouse model. The aim of the present study was to analyze the expression pattern, localization, and function of FAF1 in meiotic resumption of mouse oocytes. FAF1 was exclusively expressed in oocytes at various follicular stages within the ovary and was predominantly localized in the cytoplasm of growing oocytes. Furthermore, Faf1 mRNA and protein were persistently present during oocyte maturation and Faf1 mRNA levels were similar in the germinal vesicle (GV), GV breakdown (GVBD), and metaphase II (MII) stages of oocytes. Moreover, knockdown of Faf1 in GV-stage oocytes led to a significantly decreased rate of GVBD. To our knowledge, these results provide the first evidence regarding a novel function of FAF1 in meiotic resumption in mouse oocytes.
Reproduction (Cambridge, England), Sep 19, 2017
Nlrp2 is a maternal effect gene specifically expressed by mouse ovaries; deletion of this gene fr... more Nlrp2 is a maternal effect gene specifically expressed by mouse ovaries; deletion of this gene from zygotes is known to result in early embryonic arrest. In the present study, we identified FAF1 protein as a specific binding partner of the NLRP2 protein in both mouse oocytes and preimplantation embryos. In addition to early embryos, both Faf1 mRNA and protein were detected in multiple tissues. NLRP2 and FAF1 proteins were co-localized to both the cytoplasm and nucleus during the development of oocytes and preimplantation embryos. Co-immunoprecipitation assays were used to confirm the specific interaction between NLRP2 and FAF1 proteins. Knockdown of the Nlrp2 or Faf1 gene in zygotes interfered with the formation of a NLRP2-FAF1 complex and led to developmental arrest during early embryogenesis. We therefore conclude that NLRP2 interacts with FAF1 under normal physiological conditions and that this interaction is probably essential for the successful development of cleavage-stage mou...