{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,29]],"date-time":"2025-10-29T03:09:26Z","timestamp":1761707366253},"reference-count":56,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2002,4,25]],"date-time":"2002-04-25T00:00:00Z","timestamp":1019692800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecular Reproduction Devel"],"published-print":{"date-parts":[[2002,6]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Zymography and in situ hybridizition were used to investigate matrix metalloproteinase\u20102, \u20109 (MMP\u20102, \u20109) activities, and expression of mRNAs for MMP\u20102, \u20109 and tissue inhibitors of matrix metalloproteinases (TIMP\u20101, \u20102, \u20103) in the rat uterus during early pregnancy (day 1\u20137). The zymography results showed two forms of MMP\u20102 (64 and 67 kDa) in the rat uteri during early pregnancy. The 64\u2010kDa MMP\u20102 activity was the highest on day 2 (<jats:italic>P<\/jats:italic>\u2009&lt;\u20090.01) and higher on day 5 and 6 (<jats:italic>P<\/jats:italic>\u2009&lt;\u20090.05). The 67\u2010kDa MMP\u20102 activity reached the highest on day 5 and 6 (<jats:italic>P<\/jats:italic>\u2009&lt;\u20090.01). The 64\u2010kDa MMP\u20102 activity at the implantation sites was higher than those at interimplantation sites (<jats:italic>P<\/jats:italic>\u2009&lt;\u20090.05). Furthermore, the 67 kDa MMP\u20102 can be converted to 64 kDa forms by incubation with <jats:italic>p<\/jats:italic>\u2010aminophenylmercuric acetate (APMA) and trypsin in vitro. The 92\u2010kDa MMP\u20109 activity was only detected on day 5 and 6 of pregnancy (<jats:italic>P<\/jats:italic>\u2009&lt;\u20090.01). In situ hybridization showed that on day 1\u20134 of pregnancy, both MMP\u20102 and TIMP\u20102 mRNAs were evidently localized in the basal stromal cells. On day 5, MMP\u20102 mRNA signals were decreased in the basal stromal cells and mRNA for TIMP\u20102 was expressed in the epithelial cells and subepithelial stromal cells. The mRNAs for MMP\u20109, TIMP\u20101, and \u20103 were mainly expressed in epithelial cells on day 1\u20135. At the implantation site on day 6, the mRNAs for MMP\u20102, \u20109, TIMP\u20101, \u20102, and \u20103 were highly expressed in the primary decidual zone surrounding the implanting embryo, and in the whole decidualized stromal cells (the primary and secondary decidual zones) at the implantation site on day 7. The intensities of mRNAs for the TIMPs in decidualized stromal cells at the implantation site on day 6 and 7 were stronger than those for the MMPs. The weak mRNAs for MMP\u20102, \u20109, TIMP\u20101, and \u20103 but not TIMP\u20102 were also observed in the ectoplacental cone\/trophoblastic cells of the implanting embryos. However, at the interimplantation sites on day 6 and 7, MMP\u20102, \u20109, TIMP\u20101, \u20102, and \u20103 mRNAs were weakly expressed in the epithelial cells, subepithelial stromal cells, and myometrium. The results suggested that the implanting rat embryo strongly induced MMP\u20102 and \u20109 proteins and gene expression for decidulization and embryo invasion, which were strictly controlled and balanced by the simultaneous expression of TIMP\u20101, \u20102 and \u20103. Mol. Reprod. Dev. 62: 149\u2013158, 2002. \u00a9 2002 Wiley\u2010Liss, Inc.<\/jats:p>","DOI":"10.1002\/mrd.10123","type":"journal-article","created":{"date-parts":[[2002,8,25]],"date-time":"2002-08-25T23:24:15Z","timestamp":1030317855000},"page":"149-158","source":"Crossref","is-referenced-by-count":24,"title":["Expression of matrix metalloproteinase \u20102, \u20109 and tissue inhibitors of metalloproteinase \u20101, \u20102, \u20103 mRNAs in rat uterus during early pregnancy"],"prefix":"10.1002","volume":"62","author":[{"given":"Yun\u2010Ge","family":"Zhao","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ai\u2010Zhen","family":"Xiao","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Xiu\u2010Mei","family":"Cao","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Cheng","family":"Zhu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2002,4,25]]},"reference":[{"key":"e_1_2_1_2_1","doi-asserted-by":"publisher","DOI":"10.1002\/jez.1402660610"},{"key":"e_1_2_1_3_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.270.11.5872"},{"key":"e_1_2_1_4_1","doi-asserted-by":"crossref","first-page":"1723","DOI":"10.1242\/dev.122.6.1723","article-title":"Expression and function of matrix metalloproteinases and their inhibitors at the maternal\u2010embryonic boundary during mouse embryo implantation","volume":"122","author":"Alexander CM","year":"1996","journal-title":"Development"},{"key":"e_1_2_1_5_1","doi-asserted-by":"publisher","DOI":"10.1053\/beog.2000.0120"},{"key":"e_1_2_1_6_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0092-8674(00)81235-0"},{"key":"e_1_2_1_7_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0092-8674(00)80931-9"},{"key":"e_1_2_1_8_1","doi-asserted-by":"publisher","DOI":"10.1002\/ar.1092370103"},{"key":"e_1_2_1_9_1","first-page":"295","article-title":"Matrix metalloproteinases and metastatic cancer","volume":"63","author":"Cockett MI","year":"1998","journal-title":"Biochem Soc Symp"},{"key":"e_1_2_1_10_1","doi-asserted-by":"publisher","DOI":"10.1095\/biolreprod61.5.1309"},{"key":"e_1_2_1_11_1","doi-asserted-by":"publisher","DOI":"10.1159\/000468613"},{"key":"e_1_2_1_12_1","doi-asserted-by":"publisher","DOI":"10.1095\/biolreprod46.2.256"},{"key":"e_1_2_1_13_1","doi-asserted-by":"publisher","DOI":"10.1002\/(SICI)1520-6408(1997)21:1<44::AID-DVG5>3.0.CO;2-8"},{"key":"e_1_2_1_14_1","doi-asserted-by":"publisher","DOI":"10.1016\/0014-5793(95)00345-A"},{"key":"e_1_2_1_15_1","doi-asserted-by":"publisher","DOI":"10.1095\/biolreprod56.2.348"},{"key":"e_1_2_1_16_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1432-0436.1987.tb00161.x"},{"key":"e_1_2_1_17_1","doi-asserted-by":"publisher","DOI":"10.1016\/0014-5793(95)01435-7"},{"key":"e_1_2_1_18_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.86.21.8207"},{"key":"e_1_2_1_19_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(18)42873-6"},{"key":"e_1_2_1_20_1","first-page":"199","volume-title":"Collagen. 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