{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T13:50:08Z","timestamp":1791208208656,"version":"4.1.0"},"reference-count":35,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2012,1,20]],"date-time":"2012-01-20T00:00:00Z","timestamp":1327017600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["J of Cellular Biochemistry"],"published-print":{"date-parts":[[2012,3]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>MT1\u2010MMP (membrane type 1\u2010matrix metalloproteinase) plays important roles in cell growth and tumor invasion via mediating cleavage of MMP2\/gelatinase A and a variety of substrates including type I collagen. BST\u20102 (bone marrow stromal cell antigen 2) is a membrane tetherin whose expression dramatically reduces the release of a broad range of enveloped viruses including HIV from infected cells. In this study, we provided evidence that both transient and IFN\u2010\u03b1 induced BST\u20102 could decrease the activity of MMP2 via binding to cellular MT1\u2010MMP on its C\u2010terminus and inhibiting its proteolytic activity; and finally block cell growth and migration. Zymography gel and Western blot experiments demonstrated that BST\u20102 decreased MMP2 activity, but no effect on the expression of MMP2 and MT1\u2010MMP genes. Confocal and immunoprecipitation data showed that BST\u20102 co\u2010localized and interacted with MT1\u2010MMP. This interaction inhibited the proteolytic enzyme activity of MT1\u2010MMP, and blocked the activation of proMMP2. Experimental results of C\u2010terminus deletion mutant of MT1\u2010MMP showed that activity of MMP2 was no change and also no interaction existed between the mutant and BST\u20102 after co\u2010transfection with the mutant and BST\u20102. It meant that C\u2010terminus of MT1\u2010MMP played a key role in the interaction with BST\u20102. In addition, cell growth in 3D type I collagen gel lattice and cell migration were all inhibited by BST\u20102. Taken together, BST\u20102, as a membrane protein and a tetherin of enveloped viruses, was a novel inhibitor of MT1\u2010MMP and could be considerable as an inhibitor of cancer cell growth and migration on clinic. J. Cell. Biochem. 113: 1013\u20131021, 2012. \u00a9 2011 Wiley Periodicals, Inc.<\/jats:p>","DOI":"10.1002\/jcb.23433","type":"journal-article","created":{"date-parts":[[2011,11,7]],"date-time":"2011-11-07T13:13:11Z","timestamp":1320671591000},"page":"1013-1021","source":"Crossref","is-referenced-by-count":19,"title":["BST\u20102 binding with cellular MT1\u2010MMP blocks cell growth and migration via decreasing MMP2 activity"],"prefix":"10.1002","volume":"113","author":[{"given":"Gongping","family":"Gu","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dejian","family":"Zhao","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ziming","family":"Yin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ping","family":"Liu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2012,1,20]]},"reference":[{"key":"e_1_2_6_2_1","first-page":"3610","article-title":"Tissue inhibitor of metalloproteinases\u20104 inhibits but does not support the activation of gelatinase A via efficient inhibition of membrane type 1\u2010matrix metalloproteinase","volume":"61","author":"Bigg HF","year":"2001","journal-title":"Cancer Res"},{"key":"e_1_2_6_3_1","doi-asserted-by":"publisher","DOI":"10.1038\/sj.emboj.7601606"},{"key":"e_1_2_6_4_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1432-1033.1997.00751.x"},{"key":"e_1_2_6_5_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.tim.2010.06.010"},{"key":"e_1_2_6_6_1","doi-asserted-by":"publisher","DOI":"10.1091\/mbc.E03-07-0516"},{"key":"e_1_2_6_7_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0092-8674(00)81768-7"},{"key":"e_1_2_6_8_1","doi-asserted-by":"publisher","DOI":"10.1002\/ijc.11522"},{"key":"e_1_2_6_9_1","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.149.6.1309"},{"key":"e_1_2_6_10_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M306618200"},{"key":"e_1_2_6_11_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.241293698"},{"key":"e_1_2_6_12_1","doi-asserted-by":"publisher","DOI":"10.1096\/fj.00-0269com"},{"key":"e_1_2_6_13_1","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.148.3.615"},{"key":"e_1_2_6_14_1","doi-asserted-by":"publisher","DOI":"10.1034\/j.1600-0854.2003.00129.x"},{"key":"e_1_2_6_15_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M109128200"},{"key":"e_1_2_6_16_1","doi-asserted-by":"publisher","DOI":"10.1002\/jcp.22292"},{"key":"e_1_2_6_17_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M109.005124"},{"key":"e_1_2_6_18_1","doi-asserted-by":"publisher","DOI":"10.1152\/ajpcell.90638.2007"},{"key":"e_1_2_6_19_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0002-9440(10)63692-9"},{"key":"e_1_2_6_20_1","doi-asserted-by":"publisher","DOI":"10.1038\/nature06553"},{"key":"e_1_2_6_21_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M608045200"},{"key":"e_1_2_6_22_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.272.4.2446"},{"key":"e_1_2_6_23_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.274.13.8925"},{"key":"e_1_2_6_24_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.271.15.9135"},{"key":"e_1_2_6_25_1","doi-asserted-by":"publisher","DOI":"10.1242\/jcs.00710"},{"key":"e_1_2_6_26_1","doi-asserted-by":"publisher","DOI":"10.1242\/jcs.003343"},{"key":"e_1_2_6_27_1","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.200804154"},{"key":"e_1_2_6_28_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0955-0674(02)00363-0"},{"key":"e_1_2_6_29_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0304-3835(02)00699-7"},{"key":"e_1_2_6_30_1","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.200108112"},{"key":"e_1_2_6_31_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.chom.2008.03.001"},{"key":"e_1_2_6_32_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.yexmp.2011.04.012"},{"key":"e_1_2_6_33_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M409074200"},{"key":"e_1_2_6_34_1","doi-asserted-by":"publisher","DOI":"10.1007\/s00262-008-0612-4"},{"key":"e_1_2_6_35_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.271.29.17119"},{"key":"e_1_2_6_36_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.060037197"}],"container-title":["Journal of Cellular Biochemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.wiley.com\/onlinelibrary\/tdm\/v1\/articles\/10.1002%2Fjcb.23433","content-type":"unspecified","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/pdf\/10.1002\/jcb.23433","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,10,10]],"date-time":"2023-10-10T09:13:39Z","timestamp":1696929219000},"score":1,"resource":{"primary":{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/10.1002\/jcb.23433"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2012,1,20]]},"references-count":35,"journal-issue":{"issue":"3","published-print":{"date-parts":[[2012,3]]}},"alternative-id":["10.1002\/jcb.23433"],"URL":"https:\/\/doi.org\/10.1002\/jcb.23433","archive":["Portico"],"relation":{},"ISSN":["0730-2312","1097-4644"],"issn-type":[{"value":"0730-2312","type":"print"},{"value":"1097-4644","type":"electronic"}],"subject":[],"published":{"date-parts":[[2012,1,20]]}}}