陈子江
博士研究生 教授
山东大学 生殖医学研究中心
主要从事妇产科生殖医学,生殖内分泌疾病及遗传优生、不孕不育症的诊治临床和研究。
个性化签名
- 姓名:陈子江
- 目前身份:在职研究人员
- 担任导师情况:
- 学位:
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学术头衔:
博士生导师, 中国科学院院士,
- 职称:高级-教授
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学科领域:
妇产科学
- 研究兴趣:主要从事妇产科生殖医学,生殖内分泌疾病及遗传优生、不孕不育症的诊治临床和研究。
陈子江,女,1959年10月出生,医学博士,教授,主任医师,博士生导师。国家“百千万人才工程一、二层次专家”、卫生部突出贡献中青年专家、世界生殖医学会理事会理事、国际奥委会(IOC)医学委员会专家组成员、“山东省医学领军人才”、“泰山学者”特聘教授。
1979年9月入山东医学院医疗系学习,获医学学士;1989年12月获医学博士学位(硕博连读);1989年12月任山东医科大学临床医学部讲师;1993年破格晋升教授,同时任山东省立医院妇科主任医师;2001年9月任山东省立医院妇产科主任、生殖医学中心主任;2002年2月任山东省立医院副院长;2006年12月起先后兼任山东大学医学院副院长,生殖内分泌教育部重点实验室主任,国家辅助生殖与优生工程技术研究中心主任;2013年5月任山东大学副校长;2015年7月兼任山东大学齐鲁医学部部长。
主要从事妇产科生殖医学、生殖内分泌及生殖遗传学的临床和相关基础研究。是国内最早开展人类辅助生殖技术的专家之一,擅长诊治输卵管不通、子宫内膜异位症、多囊卵巢综合症女性内分泌失调、闭经及男性少精、性功能异常所致不孕等影响人类生殖健康的各类复杂、疑难疾病。1992年,作为主要发明人创立“人类宫腔配子移植术(GIUT)”,诞生世界首例宫腔配子移植婴儿。2010年,组织完成了卫生部委托的本领域第一个行业标准—— “多囊卵巢综合征诊断”标准。担任国家重大科学研究计划(973项目)首席专家,主持“863”项目、国家自然科学基金、卫生公益性行业科研专项等课题30余项;获得国家发明奖、国家科技进步奖、中华医学科技奖、省部级奖等多项科研奖励。荣获“霍英东”研究奖、“吴阶平”医学研究奖、卫生部有突出贡献中青年专家、全国优秀科技工作者等多项荣誉。共发表学术论文280余篇,SCI收录50余篇,分别发表在American Journal of Human Genetics、Human Reproduction、Hypertension、Fertility and Sterility等杂志上。主编《多囊卵巢综合征——基础与临床》、《人类生殖与辅助生殖》等专业论著6部,参编论著20余部。
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成果数
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陈子江, Qun Lu a, Yueran Zhao a, Xuan Gao a, Yuan Li a, Shuiying Maa, Steve Mullen b, J.K. Critser b, Zi-Jiang Chen a, c, *
European Journal of Obstetrics & Gynecology and Reproductive Biology 126(2006)72-76,-0001,():
-1年11月30日
Objective: To determine whether oocyte activation using a combination of calcium ionophore A23187 (A23187) with puromycin could salvage human unfertilized oocytes after ICSI. Study Design: One hundred and thirteen discarded unfertilized oocytes 20–68 h after ICSI were assigned to four roups: ICSI 20-h group, ICSI 44-h group, ICSI 68-h group and control. All unfertilized oocytes were exposed to A23187 (5 mM) for 5 min and subsequently were incubated with puromycin (10 mg/ml) for 4 h. Sex chromosomal analysis was performed by dual color fluorescence in situ hybridization (FISH). Results: The combination of A23187 with puromycin could activate the unfertilized oocytes 20–68 h after ICSI. The best results were achieved in the ICSI 20-h group, which exhibited an activation rate of 91.2% (31/34), a cleavage rate of 64.7% (22/34) and 44.1% (15/34) high-quality embryos. The activation rate, cleavage rate and the number of high-quality embryos appeared to decrease with the cultured time of unfertilized oocytes after ICSI. FISH analysis showed six embryos with XX and seven embryos with XY in 16 embryos derived from 2PN2PB. Conclusions: The combination of calcium ionophore A23187 with puromycin could effectively salvage unfertilized oocytes within 20 h after ICSI.
Calcium ionophore A23187, Fluorescence in situ hybridization, Human oocyte, Oocyte activation, Puromycin
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【期刊论文】Cyclophilin A Functions as an Endogenous Inhibitor for Membrane-Bound Guanylate Cyclase-A
陈子江, Zi-Jiang Chen, Michael Vetter, Geen-Dong Chang, Shiguo Liu, Danian Che, Yaxian Ding, Sung Soo Kim, Chung-Ho Chang
Hypertension 2004; 44; 963-968,-0001,():
-1年11月30日
Cyclophilin A (CypA), a receptor for the immunosuppressive agent cyclosporin A, is a cis-trans–peptidyl-prolyl isomerase (PPIase). It accelerates the cis-trans isomerization of prolyl-peptide bonds. CypA binds and regulates the activity of a variety of proteins. Atrial natriuretic factor (ANF) and its receptor membrane-bound guanylate cyclase-A (GC-A) are involved in the regulation of blood pressure. We examined whether CypA affects the activation of GC-A by ANF. The results showed that CypA associated with GC-A. Interestingly, binding of ANF to GC-A released CypA. Transfection of CypA inhibited ANF-stimulated GC-A activity, indicating that CypA functions as an endogenous inhibitor for GC-A activation. CypA also inhibits the activity of guanylate cyclase-C (GC-c), the catalytic domain of GC-A, indicating that CypA interacts with the catalytic domain of GC-A. In contrast, transfection of CypA R55A, a CypA mutant expressing low PPIase activity, did not significantly attenuate the activity of GC-c and the activation of GC-A. Inhibition of PPIase activity of CypA with cyclosporin A also blocks the inhibitory effect of CypA on GC-c activity. These results demonstrate that PPIase activity is required for CypA to inhibit GC-c activity and GC-A activation by ANF. Furthermore, mutation of Pro 822, 902, or 958 in GC-c abolished its activity. Therefore, it is likely that CypA binds to GC-A and catalyzes the cis-trans isomerization of Pro 822, 902, or 958, which keeps GC-A in the inactive state, and that binding of ANF to GC-A alters the conformation of the catalytic domain that releases CypA from GC-A leading to enzyme activation.
cyclosporin, cyclic GMP
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陈子江, Z.J.Chen, , M.Li, Y.Li, L.X.Zhao, R.Tang, Y.Sheng, X.Gao, C.H.Chang and H.L.Feng
Human Reproduction Vol. 19, No.10 pp. 2345-2349, 2004,-0001,():
-1年11月30日
Success of human oocyte cryopreservation depends on multiple cryobiological factors that could influence the developmental potential of the oocytes. The objective of this study was to examine the effects of different sucrose concentrations on the developmental potential of human frozen–thawed oocytes at different maturity stages. METHODS: A total of 355 oocytes collected from small follicles were randomly divided into three groups and two groups (B and C) were cryopreserved using slow-freezing method. Group A included 131 oocytes at different maturity stages without freezing. Another 119 oocytes in Group B were cryopreserved with 0.1M sucrose and 105 oocytes in Group C with 0.2M sucrose concentration. RESULTS: The post-thaw survival rate of the oocytes and the cleavage rate in Group C were significantly higher than that of Group B (P<0.05). For immature metaphase I (MI) stage oocytes, a significant difference was found in the maturation rate between Group C and Group B (P<0.05). The maturation rate for the GV oocytes in Groups A and C was significantly higher than Group B (P<0.01). CONCLUSIONS: The results suggested that sucrose concentration of 0.2M in the cryoprotectant solution is more suitable for human oocyte cryopreservation.
cryopreservation/, embryo/, human fertilization in vitro/, ooctyes
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陈子江, Zi-Jiang Chen a, b, Danian Che a, Michael Vetter a, Shiguo Liu a, Chung-Ho Chang a, *
Journal of Steroid Biochemistry & Molecular Biology 78(2001)451-458,-0001,():
-1年11月30日
Besides its involvement in reproductive functions, estrogen protects against the development of cardiovascular diseases. The guanylate cyclase/cGMP system is known to exert potent effects on the regulation of blood pressure and electrolyte balance. We examined whether 17β-estradiol can affect soluble guanylate cyclase in PC12 cells. The results indicate that 17β-estradiol decreases cGMP levels in PC12 cells. 17β-Estradiol decreases sodium nitroprusside (SNP)-stimulated, but not atrial natriuretic factor-stimulated cGMP formation in PC12 cells, indicating that 17β-estradiol decreases cGMP levels by inhibiting the activity of soluble guanylate cyclase. 17β-Estradiol also stimulates protein tyrosine phosphatase activities in PC12 cells and dephosphorylates at least three proteins. Addition of sodium vanadate, a protein tyrosine phosphatase inhibitor, blocks the in ibitory effects of 17β-estradiol on soluble guanylate cyclase activity in PC12 cells. Furthermore, transfection of SHP-1, a protein tyrosine phosphatase, into PC12 cells inhibits both basal and SNP-stimulated guanylate cyclase activity. Amino acid analysis also reveals that the 70-kDa subunit of soluble guanylate cyclase contains the SHP-1 substrate consensus sequence. These results suggest that 17β-estradiol inhibits soluble guanylate cyclase activity through SHP-1.
17β-estradiol, Guanylate cyclase activity, Protein tyrosine phosphatase
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