胎膜早破患者胎膜中EMMPRIN MMP-2的表达及意义
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摘要
目的:检测细胞外基质金属蛋白酶诱导因子(extracellular matrix metalloproteinase inducer, EMMPRIN)和基质金属蛋白酶-2(matrix metalloproteinase-2, MMP-2)在胎膜组织中的定位情况;探讨EMMPRIN及MMP-2在正常妊娠晚期胎膜组织中的表达及意义;研究EMMPRIN及MMP-2在胎膜早破中的相关性并分析二者在其发病机制中的作用。
方法:随机采集2006年9月至2007年7月在河北医科大学第二医院妇产科病房住院,临产前行剖宫产分娩的初产妇胎膜组织,其中足月胎膜早破者12例,足月前胎膜早破者10例和正常完好胎膜10例作对照组。所有受试对象排除有其他妊娠并发症、临床感染征象及近期抗生素应用史者。(1)应用半定量逆转录-多聚酶链反应(reverse transcription-polymerase chain reaction, RT-PCR)技术测定各组胎膜中EMMPRIN及MMP-2的mRNA表达水平并比较二者在各组间有无差异;在每一组中分析EMMPRIN mRNA与MMP-2 mRNA的相关性。(2)采用免疫组织化学SP方法检测各组胎膜组织中EMMPRIN和MMP-2的蛋白定位情况及表达水平;比较二者在各组间有无差异;在每一组中,分析二者的蛋白表达水平有无相关性。(3)依据常规苏木素-伊红(HE)染色后的组织学结果,将所有胎膜标本切片划分为绒毛膜羊膜炎组和非绒毛膜羊膜炎组,比较两组胎膜组织中EMMPRIN的蛋白表达水平有无差异。数据用SPSS 13.0软件作统计学处理,采用F检验、q检验、t检验及直线相关分析,P<0.05为差异有显著性意义。
结果:
1 EMMPRIN、MMP-2mRNA和蛋白在足月胎膜早破,足月前胎膜早破及正常妊娠晚期胎膜组织中均有表达。
2 EMMPRIN和MMP-2的蛋白表达部位:EMMPRIN主要表达于羊膜上皮细胞和绒毛膜滋养细胞的胞膜;MMP-2表达于羊膜上皮细胞和绒毛膜滋养细胞的胞浆。
3 MMP-2mRNA和蛋白的表达:对照组MMP-2mRNA的相对表达量为:[(63.50±9.53)×10-2],低于足月胎膜早破组[(80.75±7.02)×10-2](P<0.01)和足月前胎膜早破组[(77.30±6.31)×10-2](P<0.01),差异有统计学意义;对照组MMP-2的蛋白表达量为:[(20.01±1.83)×10-2],低于足月胎膜早破组[(23.33±2.81)×10-2](P<0.01)和足月前胎膜早破组[(22.60±2.99)×10-2](P<0.05),差异有统计学意义;但MMP-2mRNA和蛋白的表达在足月与足月前胎膜早破组之间差异无统计学意义(P>0.05)。
4 EMMPRIN mRNA和蛋白的表达:对照组EMMPRIN mRNA的相对表达量为:[(118.76±10.88)×10-2],低于足月胎膜早破组[(135.00±9.27)×10-2](P<0.01)和足月前胎膜早破组[(128.50±9.49)×10-2](P<0.05),差异有统计学意义;对照组EMMPRIN的蛋白表达量为:[(24.40±3.63)×10-2],低于足月胎膜早破组[(29.92±3. 23)×10-2](P<0.01)和足月前胎膜早破组[ (27.30±2.36)×10-2](P<0.05),差异有统计学意义。但EMMPRIN mRNA和蛋白的表达在足月与足月前胎膜早破组之间差异无统计学意义(P>0.05)。
5 EMMPRIN与MMP-2的mRNA相对表达量的相关性:在足月和足月前胎膜早破组中,二者存在显著正相关(r=0.639, P<0.05; r=0.645, P<0.05);在对照组中,相关性无统计学意义(r=0.178, P>0.05)。
6 EMMPRIN与MMP-2的蛋白表达量的相关性:在足月和足月前胎膜早破组中,二者存在显著正相关(r=0.585, P<0.05;r=0.681, P<0.05);在对照组中,相关性无统计学意义(r=0.268, P>0.05)。
7绒毛膜羊膜炎组EMMPRIN蛋白表达量为:([29.69±2.40)×10-2],高于非绒毛膜羊膜炎组[(26.00±3.74)×10-2],差异有统计学意义(P<0.01)。
结论:
1 EMMPRIN、MMP-2在足月胎膜早破,足月前胎膜早破及正常妊娠晚期胎膜组织中均有表达,EMMPRIN表达位置为羊膜上皮细胞及绒毛膜滋养细胞的胞膜。MMP-2表达于羊膜上皮细胞和绒毛膜滋养细胞的胞浆。
2正常妊娠晚期,EMMPRIN可能通过翻译后改变自身糖基化的程度,调节MMPs的水平参与妊娠的维持。
3在胎膜早破中,EMMPRIN在炎症等一种或几种因素的作用下,其转录水平被上调,并且可能通过诱导MMP-2而参与胎膜早破的病理过程。
Objective: To detect the locations of EMMPRIN and MMP-2 in fetal membranes;To study the expressions of EMMPRIN and EMMPRIN in fetal membranes of normal pregnancy , and to investigate the correlation between EMMPRIN and MMP-2, and evaluate their functions in the pathogenesis of premature rupture of fetal membranes.
Methods: The amniochorion (fetal membranes) samples were collected from 32 nulliparous women: 12 cases of term premature rupture of membranes (tPROM), 10 cases of preterm premature rupture of membranes (pPROM) and 10 cases of term intact membranes as controls. The caesarean sections were operated on all the patients before the urinary constriction in the Obstetrics of the Second Hospital of HeBei Medical University from September 2006 to July 2007. We excluded women with other pregnancy complication, clinical infections and/or undergoing antibiotic treatment. (1) The reverse transcription-polymerase chain reaction (RT-PCR) was performed to assay the mRNA levels of EMMPRIN and MMP-2 in fetal membrane samples in order to show whether there are differences among their concentrations of each group, and in order to study the relationship between EMMPRIN mRNA and MMP-2 mRNA in every group; (2) The protein levels of EMMPRIN and MMP-2 in fetal membranes were documented with s-p immunohistochemistry, and were compared among the three groups, respectively. Their correlation in every group was studied also. (3) The hematoryline and eosin (HE) staining was used to divide all fetal membranes samples into two groups: with chorioamnionitis and without chorioamnionitis, and the protein level of EMMPRIN was compared between them. Results were analyzed with use of F test、q test、t test、and linear correlation; For these analyses, P<0.05 was considered statistically significant.
Results:
1 EMMPRIN and MMP-2, not only their mRNA, but also their protein, were expressed in all of the three groups.
2 The localization of EMMPRIN and MMP-2 proteins: EMMPRIN-positive staining was found in the amniotic epithelial cells and chorionic cytotrophoblast cells, and which all presenced on cell membranes. MMP-2-positive staining was found in the amniotic epithelial cells and chorionic cytotrophoblast cells, and all presenced in cell plasma.
3 The mRNA and protein levels of MMP-2: The mRNA level of MMP-2 in control was: [(63.50±9.53)×10-2], significantly lower than tPROM [(80.75±7.02)×10-2](P<0.01) and pPROM[(77.30±6.31)×10-2](P<0.01). The protein level of MMP-2 in controls was: [(20.01±1.83)×10-2], significantly lower than tPROM[(23.33±2.81)×10-2](P<0.01) and pPROM[(22.60±2.99)×10-2](P<0.05). The expression of MMP-2 mRNA and protein in tPROM and pPROM has no statistically significant difference (P>0.05).
4 The mRNA and protein levels of EMMPRIN: The mRNA level of EMMPRIN in controls was:[(118.76±10.88)×10-2], significantly lower than tPROM[(135.00±9.27)×10-2](P<0.01) and pPROM [(128.50±9.49)×10-2](P<0.05); The protein level of EMMPRIN in controls was:[(24.40±3.6)×10-2], significantly lower than tPROM[(29.92±3. 23)×10-2](P<0.01) and pPROM [(27.30±2.36)×10-2] (P<0.05). The expression of EMMPRIN mRNA and protein in tPROM and pPROM has no statistically significant difference (P>0.05).
5 The relationship between EMMPRIN mRNA and MMP-2 mRNA: EMMPRIN mRNA and MMP-2 mRNA was positively correlated in term and preterm premature rupture of fetal membranes (r=0.639, P <0.05; r=0.645, P <0.05), whereas no significant differences between them in control group(r=0.178, P>0.05).
6 The relationship between the EMMPRIN protein and MMP-2 protein: EMMPRIN protein and MMP-2 protein was positively correlated in term and preterm premature rupture of fetal membranes (r=0.585, P <0.05; r=0.681, P <0.05), whereas no significant differences between them in control group (r=0.268, P>0.05).
7 The levels of EMMPRIN protein in the group with chorioamnionitis was [(29.69±2.40)×10-2], significantly higher than that of the group without chorioamnionitis [(26.00±3.74)×10-2] (P<0.01).
Conclusion:
1 EMMPRIN and MMP-2 expressed in all of the three groups, and EMMPRIN appeared mainly on cell membranes of the amniotic epithelial cells and chorionic cytotrophoblast cells, and MMP-2 localized in cell plasma of the same cells.
2 EMMPRIN may regulate MMPs by altering its level of glycosylation during normal pregnancy, and which may be helpful for pregnancy.
3 In premature rupture of membranes, EMMPRIN may have changed in transcriptional level, influenced by one or several factors, such as inflammation and so on, and it may participate in the pathogenesis of premature rupture of fetal membranes by stimulating MMP-2.
方法:随机采集2006年9月至2007年7月在河北医科大学第二医院妇产科病房住院,临产前行剖宫产分娩的初产妇胎膜组织,其中足月胎膜早破者12例,足月前胎膜早破者10例和正常完好胎膜10例作对照组。所有受试对象排除有其他妊娠并发症、临床感染征象及近期抗生素应用史者。(1)应用半定量逆转录-多聚酶链反应(reverse transcription-polymerase chain reaction, RT-PCR)技术测定各组胎膜中EMMPRIN及MMP-2的mRNA表达水平并比较二者在各组间有无差异;在每一组中分析EMMPRIN mRNA与MMP-2 mRNA的相关性。(2)采用免疫组织化学SP方法检测各组胎膜组织中EMMPRIN和MMP-2的蛋白定位情况及表达水平;比较二者在各组间有无差异;在每一组中,分析二者的蛋白表达水平有无相关性。(3)依据常规苏木素-伊红(HE)染色后的组织学结果,将所有胎膜标本切片划分为绒毛膜羊膜炎组和非绒毛膜羊膜炎组,比较两组胎膜组织中EMMPRIN的蛋白表达水平有无差异。数据用SPSS 13.0软件作统计学处理,采用F检验、q检验、t检验及直线相关分析,P<0.05为差异有显著性意义。
结果:
1 EMMPRIN、MMP-2mRNA和蛋白在足月胎膜早破,足月前胎膜早破及正常妊娠晚期胎膜组织中均有表达。
2 EMMPRIN和MMP-2的蛋白表达部位:EMMPRIN主要表达于羊膜上皮细胞和绒毛膜滋养细胞的胞膜;MMP-2表达于羊膜上皮细胞和绒毛膜滋养细胞的胞浆。
3 MMP-2mRNA和蛋白的表达:对照组MMP-2mRNA的相对表达量为:[(63.50±9.53)×10-2],低于足月胎膜早破组[(80.75±7.02)×10-2](P<0.01)和足月前胎膜早破组[(77.30±6.31)×10-2](P<0.01),差异有统计学意义;对照组MMP-2的蛋白表达量为:[(20.01±1.83)×10-2],低于足月胎膜早破组[(23.33±2.81)×10-2](P<0.01)和足月前胎膜早破组[(22.60±2.99)×10-2](P<0.05),差异有统计学意义;但MMP-2mRNA和蛋白的表达在足月与足月前胎膜早破组之间差异无统计学意义(P>0.05)。
4 EMMPRIN mRNA和蛋白的表达:对照组EMMPRIN mRNA的相对表达量为:[(118.76±10.88)×10-2],低于足月胎膜早破组[(135.00±9.27)×10-2](P<0.01)和足月前胎膜早破组[(128.50±9.49)×10-2](P<0.05),差异有统计学意义;对照组EMMPRIN的蛋白表达量为:[(24.40±3.63)×10-2],低于足月胎膜早破组[(29.92±3. 23)×10-2](P<0.01)和足月前胎膜早破组[ (27.30±2.36)×10-2](P<0.05),差异有统计学意义。但EMMPRIN mRNA和蛋白的表达在足月与足月前胎膜早破组之间差异无统计学意义(P>0.05)。
5 EMMPRIN与MMP-2的mRNA相对表达量的相关性:在足月和足月前胎膜早破组中,二者存在显著正相关(r=0.639, P<0.05; r=0.645, P<0.05);在对照组中,相关性无统计学意义(r=0.178, P>0.05)。
6 EMMPRIN与MMP-2的蛋白表达量的相关性:在足月和足月前胎膜早破组中,二者存在显著正相关(r=0.585, P<0.05;r=0.681, P<0.05);在对照组中,相关性无统计学意义(r=0.268, P>0.05)。
7绒毛膜羊膜炎组EMMPRIN蛋白表达量为:([29.69±2.40)×10-2],高于非绒毛膜羊膜炎组[(26.00±3.74)×10-2],差异有统计学意义(P<0.01)。
结论:
1 EMMPRIN、MMP-2在足月胎膜早破,足月前胎膜早破及正常妊娠晚期胎膜组织中均有表达,EMMPRIN表达位置为羊膜上皮细胞及绒毛膜滋养细胞的胞膜。MMP-2表达于羊膜上皮细胞和绒毛膜滋养细胞的胞浆。
2正常妊娠晚期,EMMPRIN可能通过翻译后改变自身糖基化的程度,调节MMPs的水平参与妊娠的维持。
3在胎膜早破中,EMMPRIN在炎症等一种或几种因素的作用下,其转录水平被上调,并且可能通过诱导MMP-2而参与胎膜早破的病理过程。
Objective: To detect the locations of EMMPRIN and MMP-2 in fetal membranes;To study the expressions of EMMPRIN and EMMPRIN in fetal membranes of normal pregnancy , and to investigate the correlation between EMMPRIN and MMP-2, and evaluate their functions in the pathogenesis of premature rupture of fetal membranes.
Methods: The amniochorion (fetal membranes) samples were collected from 32 nulliparous women: 12 cases of term premature rupture of membranes (tPROM), 10 cases of preterm premature rupture of membranes (pPROM) and 10 cases of term intact membranes as controls. The caesarean sections were operated on all the patients before the urinary constriction in the Obstetrics of the Second Hospital of HeBei Medical University from September 2006 to July 2007. We excluded women with other pregnancy complication, clinical infections and/or undergoing antibiotic treatment. (1) The reverse transcription-polymerase chain reaction (RT-PCR) was performed to assay the mRNA levels of EMMPRIN and MMP-2 in fetal membrane samples in order to show whether there are differences among their concentrations of each group, and in order to study the relationship between EMMPRIN mRNA and MMP-2 mRNA in every group; (2) The protein levels of EMMPRIN and MMP-2 in fetal membranes were documented with s-p immunohistochemistry, and were compared among the three groups, respectively. Their correlation in every group was studied also. (3) The hematoryline and eosin (HE) staining was used to divide all fetal membranes samples into two groups: with chorioamnionitis and without chorioamnionitis, and the protein level of EMMPRIN was compared between them. Results were analyzed with use of F test、q test、t test、and linear correlation; For these analyses, P<0.05 was considered statistically significant.
Results:
1 EMMPRIN and MMP-2, not only their mRNA, but also their protein, were expressed in all of the three groups.
2 The localization of EMMPRIN and MMP-2 proteins: EMMPRIN-positive staining was found in the amniotic epithelial cells and chorionic cytotrophoblast cells, and which all presenced on cell membranes. MMP-2-positive staining was found in the amniotic epithelial cells and chorionic cytotrophoblast cells, and all presenced in cell plasma.
3 The mRNA and protein levels of MMP-2: The mRNA level of MMP-2 in control was: [(63.50±9.53)×10-2], significantly lower than tPROM [(80.75±7.02)×10-2](P<0.01) and pPROM[(77.30±6.31)×10-2](P<0.01). The protein level of MMP-2 in controls was: [(20.01±1.83)×10-2], significantly lower than tPROM[(23.33±2.81)×10-2](P<0.01) and pPROM[(22.60±2.99)×10-2](P<0.05). The expression of MMP-2 mRNA and protein in tPROM and pPROM has no statistically significant difference (P>0.05).
4 The mRNA and protein levels of EMMPRIN: The mRNA level of EMMPRIN in controls was:[(118.76±10.88)×10-2], significantly lower than tPROM[(135.00±9.27)×10-2](P<0.01) and pPROM [(128.50±9.49)×10-2](P<0.05); The protein level of EMMPRIN in controls was:[(24.40±3.6)×10-2], significantly lower than tPROM[(29.92±3. 23)×10-2](P<0.01) and pPROM [(27.30±2.36)×10-2] (P<0.05). The expression of EMMPRIN mRNA and protein in tPROM and pPROM has no statistically significant difference (P>0.05).
5 The relationship between EMMPRIN mRNA and MMP-2 mRNA: EMMPRIN mRNA and MMP-2 mRNA was positively correlated in term and preterm premature rupture of fetal membranes (r=0.639, P <0.05; r=0.645, P <0.05), whereas no significant differences between them in control group(r=0.178, P>0.05).
6 The relationship between the EMMPRIN protein and MMP-2 protein: EMMPRIN protein and MMP-2 protein was positively correlated in term and preterm premature rupture of fetal membranes (r=0.585, P <0.05; r=0.681, P <0.05), whereas no significant differences between them in control group (r=0.268, P>0.05).
7 The levels of EMMPRIN protein in the group with chorioamnionitis was [(29.69±2.40)×10-2], significantly higher than that of the group without chorioamnionitis [(26.00±3.74)×10-2] (P<0.01).
Conclusion:
1 EMMPRIN and MMP-2 expressed in all of the three groups, and EMMPRIN appeared mainly on cell membranes of the amniotic epithelial cells and chorionic cytotrophoblast cells, and MMP-2 localized in cell plasma of the same cells.
2 EMMPRIN may regulate MMPs by altering its level of glycosylation during normal pregnancy, and which may be helpful for pregnancy.
3 In premature rupture of membranes, EMMPRIN may have changed in transcriptional level, influenced by one or several factors, such as inflammation and so on, and it may participate in the pathogenesis of premature rupture of fetal membranes by stimulating MMP-2.
引文
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22 Lim M, Martinez T, Jablons D, et al.Tumor-derived EMMPRIN (extracellular matrix metalloproteinase inducer) stimulates collagenase transcription through MAPK p38[J]. FEBS Lett, 1998, 441:88~92
23 Taylor PM, Woodfield RJ, Hodgkin MN, et al. Breast cancercell-derived EMMPRIN stimulates fibroblast MMP2 release through a phospholipase A(2) and 5-lipoxygenase catalyzed pathway. Oncogene, 2002, 21:5765~5772
24 Tang Y, Kesavan L, Nakada MT, et al. Tumor-stroma interaction: positive feedback regulation of extracellular matrix metalloproteinase inducer(EMMPRIN) expression and matrix metalloproteinase-dependent generation of soluble EMMPRIN. Mol Cancer Res, 2004, 2:73~80
25 Menashi S, Serova M, Ma L, et al. Regulation of extracellular matrix metalloproteinase inducer and matrix metalloproteinase expression by amphiregulin in transformed human breast epithelial cells. Cancer Res, 2003, 63: 7575~7580
26 Papadopoulos N, Simopoulos C, Polihronidis A, et al. Expression of fibrillar proteins and vimentin in developing chorionic villi is related to fetal maturation[J ]. Clin Exp Obstet Gynecol , 2001, 28:171 ~172
27 Menon R, Fortunato SJ. The role of matrix degrading enzymes and apoptosis in rupture of membranes[J]. J Soc Gynecol Investig, 2004, 11:427~437
28 Li W, Alfaidy N, Challis JR. Expression of extracellular matrix metalloproteinase inducer in human placenta and fetal membranes at term labor[J]. J Clin Endocrinol Metab, 2004, 89(6):2897~2904
29 满冬梅, 孔灵玲. 基质金属蛋白酶 2 和 9 与自发性胎膜早破关系的研究[J]. 实用诊断与治疗杂志,2006,20(12) :866~867
30 丁依玲,李婵娟. 基质金属蛋白酶 2 ,9 在胎膜早破产妇胎膜的表达变化[J]. 实用妇产科杂志, 2005, 21(3): 174~176
31 Fortanato SJ, Menon R, Jombardi Sj. Presence of four tissue inhibitors of matrix metalloproteinases ( TIMP - 1 ,2 ,3 ,4) in human fetal membranes. Am JReprodImmunol, 1998, 40:195
32 张玲. MMP - 2 、MT1 - MMP、TIMP - 2 在胎膜早破的作用[J ]. 中国优生与遗传杂志, 2005, 13(12):27~29
33 卢丹,王志学,王晓玲,等.基质金属蛋白酶9及其组织抑物1的水平变化与胎膜早破发病的关系[J].中华妇产科杂志, 2006,41(1):20~24
34 YoshidaS, Shibata M, yamamoto S, et al. Homo-oligomer formation by basigin,an immunoglobulin superfamily member,via its N-terminal immunoglobulin domain. Eub.J.Biochem, 2000, 267(10):4372~4380
35 Kanekura.T, Chen T, Kanzaki T. Basigin (CD 147) is expressed on melanoma cells and induces tumor cell invasion by stimulating production of matrix metalloproteinases by fibroblasts. Int. J. Cancer, 2002, 99:520~528
36 Bordador LC, Li K, Toole B, et al. Expression of EMMPRIN by oral squamous cell carcinoma. Int J Cancer, 2000, 85: 347~352
37 Kameda K, Matsunaga T, Okumura K, et al. C-reactive protein-induced upregulation of extracellular matrix metalloproteinase inducer in macrophages: inhibitory effect of fluvastatin[J]. Life Sci, 2006, 78(9):1021~1028
1 Biswas C, Zhang Y, Decastro R, et al. The human tumor cell - derived collagenase stimulatory factor ( Renamed EMMPR IN ) is a member of the immunoglobulin [ J ]. Cancer Res, 1995, 55: 434～439
2 Guo H, Majmudar G, Jensen T C, et al. Characterization of the human EMMPR IN, a tumor cell surface inducer of matrix metallop roteinases[J]. Gene, 1998, 220 (122) : 99～108
3 Noguchi Y, Sato T, Hirata M, et al. Identification and characterization of extracellular matrix metalloproteinase inducer in human endometrium during the menstrual cycle in vivo and in vitro[J].J Clin Endocrinol Metab,2003, 88(12):6063~6072
4 Braundmeier A G, Fazleabas A T, Lessey B A, et al. Extracellular matrix metalloproteinase inducer regulates metalloproteinases in human uterine endometrium[J].J Clin Endocrinol Metab,2006, 91(6):2358~2365
5 Chang H, Ni H, Ma X H, et al. Basigin expression and regulation in mouse ovary during the sexual maturation and development of corpus luteum[J].Mol Reprod Dev,2004, 68(2):135~141
6 Smedts A M, Curry T E. Expression of basigin, an inducer of matrix metalloproteinases, in the rat ovary[J].Jr Biol Reprod,2005,73(1):80~87
7 Jo M, Thomas L E, Wheeler S E, et al. Membrane type 1-matrix metalloproteinase (MMP)-associated MMP-2 activation increases in the rat ovary in response to an ovulatory dose of human chorionic gonadotropin[J].Biol Reprod,2004,70:1024~1032
8 Smedts A M, Lele S M, Modesitt S C, et al. Expression of an extracellular matrix metalloproteinase inducer (basigin) in the human ovary and ovarian endometriosis[J].Fertil Steril,2006, 86(3):535~542
9 Pilka R, Kudela M, Procházka M. Matrix metalloproteinases, embryo implantation and tumor invasion[J].Ceska Gynekol,2003, 68(3):179~185
10 Xiao LJ, Diao HL, Ma XH, et al. Basigin expression and hormonal regulation in the rat uterus during the peri-implantation period. Reproduction, 2002, (12)4:219~225
11 Hen L, Nakai M, Belton RJ, et al. Expression of extracellular matrix metalloproteinase inducer and matrix metalloproteinases during mouse embryonic development[J].Reproduction,2007,133(2):405~414
12 Weiss A, Goldman S, Shalev E. The matrix metalloproteinases (MMPs) in the decidua and fetal membranes[J].Front Biosci, 2007, 12:649~659
13 Settle P, Mynett K, Speake P, et al. Polarized lactate transporter activity and expression in the syncytiotrophoblast of the term human placenta[J].Placenta, 2004, 25(6):496~504
14 Li W, Alfaidy N, Challis J R. Expression of extracellular matrix metalloproteinase inducer in human placenta and fetal membranes at term labor[J].J Clin Endocrinol Metab, 2004, 89(6):2897~2904
15 Sun JX, Hemler ME, Regulation of MMP-1 and MMP-2 production through CD147/extracellar matrix metalloproteinase inducer interactions. Cancer Res , 2001, 61:2276~2281
16 Yuasa J, Toyama Y, Miyauchi T, et al. Specific localization of the basigin protein in human testes from normal adults, normal juveniles and patients with azoospermia[J]. Andrologia, 2001, 33(5):293~299
17 Toyama Y, Maekawa M, Kadomatsu K, et al. Histological characterization of defective spermatogenesis in mice lacking the basigin gene[J].Anat Histol Embryol, 1999, 28(3):205~213
18 Saxena DK, Oh-Oka T, Kadomatsu K, et al. Behaviour of a sperm surface transmembrane glycoprotein basigin during epididymal maturation and its role in fertilization in mice[J]. Reproduction, 2002, 12(3):435~444
19 Saxena D K, Toshimori K. Molecular modifications of MC31/CE9, a sperm surface molecule, during sperm capacitation and the acrosome reaction in the rat: Is MC31/CE9 required for fertilization[J].Biol Reprod,2004, 70(4):993~1000
2 王永清,李俊,尚涛,等.细胞外基质金属蛋白酶诱导因子在绒毛和胎盘组织中的表达[J].中华妇产科杂志,2005, 40 (7):457~459
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5 Biswas C, zhang Y, DeCastro R, et al. The human tumor cell derived collagenase stimulatory factor (renamed EMMPRIN)is a member of the immunoglobulin super family[J]. Cancer Res, 1995, 55(2):434
6 Fossum S,Mallett S,Bsrclay AN et al. The MRC OX-47 antigen is a member of the immunoglobulin superfamily with an unusual transmembrane sequence. Eur-J-Immunol[J], 1991, 21(3): 671~679
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8 Ellis SM, Nabeshima K, Biswas C. Monoclonal preparationan purification of a tumor cell collagenase stimulatory factor[J]. Cancer Res, 1989, 49: 3385~3391
9 Menashi S, Serova M, Ma L, et al. Regulation ofextracellular matrix metalloproteinase inducer and matrix metalloproteinase expression by amphiregulin in transformed human breast epithelial cells [J]. Cancer Res, 2003, 63:7575
10 Li R, Huang L, Guo H, et al. Basigin(murine EMMPRIN) stimulates matrix metalloproteinase production by fibroblasts [J]. J Cell Physiol, 2001, 186:371
11 Braundmeier AG, Fazleabas AT, Lessey BA, et al. Extracellular matrix metalloproteinase inducer regulates metalloproteinases in human uterine endometrium[J]. J Clin Endocrinol Metab, 2006, 91(6):2358~2365
12 王永清,李俊,王雁玲,等. 细胞外基质金属蛋白酶诱导因子对细胞滋养细胞分泌基质金属蛋白酶的调节 [J].中华妇产科杂志, 2006, 41(8):560~562
13 Berditchevski F, Chang S, Bodorova J et al. Generation of monoclonal antibodies to integrin-associated proteins.Evidence that alpha3beta1 complexes with EMMPRIN/basigin/OX47/M6[J].J-Biol-Chem,1997,272(46): 29174~29180
14 Yurchenko V, Zybarth G, O'Connor M, et al. Active site residues of cyclophilin A are crucial for its signaling activity via CD147[J]. J Biol Chem.2002 , 277(25):22959~22965.
15 Arora K, Gwinn WM, Bower MA,et al Extracellular cyclophilins contribute to the regulation of inflammatory responses[J]. J Immunol, 2005,175(1):517~522
16 Marbaix E. Role of matrix metalloproteinases in theendometrium in normal and pathologic menstruation. Bull Mem Acad R Med Belg, 2005, 160: 232~238
17 Liu Q, Zhang X, Lin H, et al. Effects of E-cadherin on mouse embryo implantation and expression of matrix metalloproteinase-2 and -9. Biochem Biophys Res Commun, 2006, 343: 832~838
18 Baek KH, Choi BC, Lee JH, et al. Comparison of gene expression at the feto-maternal interface between normal and recurrent pregnancy loss patients. Reprod Fertil Dev, 2002, 14: 235~240
19 Sun J, Hemler ME. Regulation of MMP-1 and MMP-2 production through CD147/extracellular matrix metalloproteinase inducer interactions, Cancer Res,2001,61:2276~2281
20 Zucker S, Hymowitz M, Rollo EE, et al. Tumorigenic potential of extracellular matrix metalloproteinase inducer, Am[J]. J. Pathol, 2001,158 :1921~1928
21 Sun JX, Hemler ME. Regulation of MMP-1 and MMP-2 production through CD147/extracellar matrix metalloproteinase inducer interactions[J]. Cancer Res, 2001,61:2276~2281
22 Lim M, Martinez T, Jablons D, et al.Tumor-derived EMMPRIN (extracellular matrix metalloproteinase inducer) stimulates collagenase transcription through MAPK p38[J]. FEBS Lett, 1998, 441:88~92
23 Taylor PM, Woodfield RJ, Hodgkin MN, et al. Breast cancercell-derived EMMPRIN stimulates fibroblast MMP2 release through a phospholipase A(2) and 5-lipoxygenase catalyzed pathway. Oncogene, 2002, 21:5765~5772
24 Tang Y, Kesavan L, Nakada MT, et al. Tumor-stroma interaction: positive feedback regulation of extracellular matrix metalloproteinase inducer(EMMPRIN) expression and matrix metalloproteinase-dependent generation of soluble EMMPRIN. Mol Cancer Res, 2004, 2:73~80
25 Menashi S, Serova M, Ma L, et al. Regulation of extracellular matrix metalloproteinase inducer and matrix metalloproteinase expression by amphiregulin in transformed human breast epithelial cells. Cancer Res, 2003, 63: 7575~7580
26 Papadopoulos N, Simopoulos C, Polihronidis A, et al. Expression of fibrillar proteins and vimentin in developing chorionic villi is related to fetal maturation[J ]. Clin Exp Obstet Gynecol , 2001, 28:171 ~172
27 Menon R, Fortunato SJ. The role of matrix degrading enzymes and apoptosis in rupture of membranes[J]. J Soc Gynecol Investig, 2004, 11:427~437
28 Li W, Alfaidy N, Challis JR. Expression of extracellular matrix metalloproteinase inducer in human placenta and fetal membranes at term labor[J]. J Clin Endocrinol Metab, 2004, 89(6):2897~2904
29 满冬梅, 孔灵玲. 基质金属蛋白酶 2 和 9 与自发性胎膜早破关系的研究[J]. 实用诊断与治疗杂志,2006,20(12) :866~867
30 丁依玲,李婵娟. 基质金属蛋白酶 2 ,9 在胎膜早破产妇胎膜的表达变化[J]. 实用妇产科杂志, 2005, 21(3): 174~176
31 Fortanato SJ, Menon R, Jombardi Sj. Presence of four tissue inhibitors of matrix metalloproteinases ( TIMP - 1 ,2 ,3 ,4) in human fetal membranes. Am JReprodImmunol, 1998, 40:195
32 张玲. MMP - 2 、MT1 - MMP、TIMP - 2 在胎膜早破的作用[J ]. 中国优生与遗传杂志, 2005, 13(12):27~29
33 卢丹,王志学,王晓玲,等.基质金属蛋白酶9及其组织抑物1的水平变化与胎膜早破发病的关系[J].中华妇产科杂志, 2006,41(1):20~24
34 YoshidaS, Shibata M, yamamoto S, et al. Homo-oligomer formation by basigin,an immunoglobulin superfamily member,via its N-terminal immunoglobulin domain. Eub.J.Biochem, 2000, 267(10):4372~4380
35 Kanekura.T, Chen T, Kanzaki T. Basigin (CD 147) is expressed on melanoma cells and induces tumor cell invasion by stimulating production of matrix metalloproteinases by fibroblasts. Int. J. Cancer, 2002, 99:520~528
36 Bordador LC, Li K, Toole B, et al. Expression of EMMPRIN by oral squamous cell carcinoma. Int J Cancer, 2000, 85: 347~352
37 Kameda K, Matsunaga T, Okumura K, et al. C-reactive protein-induced upregulation of extracellular matrix metalloproteinase inducer in macrophages: inhibitory effect of fluvastatin[J]. Life Sci, 2006, 78(9):1021~1028
1 Biswas C, Zhang Y, Decastro R, et al. The human tumor cell - derived collagenase stimulatory factor ( Renamed EMMPR IN ) is a member of the immunoglobulin [ J ]. Cancer Res, 1995, 55: 434～439
2 Guo H, Majmudar G, Jensen T C, et al. Characterization of the human EMMPR IN, a tumor cell surface inducer of matrix metallop roteinases[J]. Gene, 1998, 220 (122) : 99～108
3 Noguchi Y, Sato T, Hirata M, et al. Identification and characterization of extracellular matrix metalloproteinase inducer in human endometrium during the menstrual cycle in vivo and in vitro[J].J Clin Endocrinol Metab,2003, 88(12):6063~6072
4 Braundmeier A G, Fazleabas A T, Lessey B A, et al. Extracellular matrix metalloproteinase inducer regulates metalloproteinases in human uterine endometrium[J].J Clin Endocrinol Metab,2006, 91(6):2358~2365
5 Chang H, Ni H, Ma X H, et al. Basigin expression and regulation in mouse ovary during the sexual maturation and development of corpus luteum[J].Mol Reprod Dev,2004, 68(2):135~141
6 Smedts A M, Curry T E. Expression of basigin, an inducer of matrix metalloproteinases, in the rat ovary[J].Jr Biol Reprod,2005,73(1):80~87
7 Jo M, Thomas L E, Wheeler S E, et al. Membrane type 1-matrix metalloproteinase (MMP)-associated MMP-2 activation increases in the rat ovary in response to an ovulatory dose of human chorionic gonadotropin[J].Biol Reprod,2004,70:1024~1032
8 Smedts A M, Lele S M, Modesitt S C, et al. Expression of an extracellular matrix metalloproteinase inducer (basigin) in the human ovary and ovarian endometriosis[J].Fertil Steril,2006, 86(3):535~542
9 Pilka R, Kudela M, Procházka M. Matrix metalloproteinases, embryo implantation and tumor invasion[J].Ceska Gynekol,2003, 68(3):179~185
10 Xiao LJ, Diao HL, Ma XH, et al. Basigin expression and hormonal regulation in the rat uterus during the peri-implantation period. Reproduction, 2002, (12)4:219~225
11 Hen L, Nakai M, Belton RJ, et al. Expression of extracellular matrix metalloproteinase inducer and matrix metalloproteinases during mouse embryonic development[J].Reproduction,2007,133(2):405~414
12 Weiss A, Goldman S, Shalev E. The matrix metalloproteinases (MMPs) in the decidua and fetal membranes[J].Front Biosci, 2007, 12:649~659
13 Settle P, Mynett K, Speake P, et al. Polarized lactate transporter activity and expression in the syncytiotrophoblast of the term human placenta[J].Placenta, 2004, 25(6):496~504
14 Li W, Alfaidy N, Challis J R. Expression of extracellular matrix metalloproteinase inducer in human placenta and fetal membranes at term labor[J].J Clin Endocrinol Metab, 2004, 89(6):2897~2904
15 Sun JX, Hemler ME, Regulation of MMP-1 and MMP-2 production through CD147/extracellar matrix metalloproteinase inducer interactions. Cancer Res , 2001, 61:2276~2281
16 Yuasa J, Toyama Y, Miyauchi T, et al. Specific localization of the basigin protein in human testes from normal adults, normal juveniles and patients with azoospermia[J]. Andrologia, 2001, 33(5):293~299
17 Toyama Y, Maekawa M, Kadomatsu K, et al. Histological characterization of defective spermatogenesis in mice lacking the basigin gene[J].Anat Histol Embryol, 1999, 28(3):205~213
18 Saxena DK, Oh-Oka T, Kadomatsu K, et al. Behaviour of a sperm surface transmembrane glycoprotein basigin during epididymal maturation and its role in fertilization in mice[J]. Reproduction, 2002, 12(3):435~444
19 Saxena D K, Toshimori K. Molecular modifications of MC31/CE9, a sperm surface molecule, during sperm capacitation and the acrosome reaction in the rat: Is MC31/CE9 required for fertilization[J].Biol Reprod,2004, 70(4):993~1000