{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,27]],"date-time":"2026-09-27T13:22:06Z","timestamp":1790515326577,"version":"4.1.0"},"reference-count":29,"publisher":"Springer Science and Business Media LLC","issue":"6625","license":[{"start":{"date-parts":[[1997,4,1]],"date-time":"1997-04-01T00:00:00Z","timestamp":859852800000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Nature"],"published-print":{"date-parts":[[1997,4]]},"DOI":"10.1038\/386616a0","type":"journal-article","created":{"date-parts":[[2003,8,12]],"date-time":"2003-08-12T02:26:50Z","timestamp":1060655210000},"page":"616-619","source":"Crossref","is-referenced-by-count":272,"title":["Release of gelatinase A during platelet activation mediates aggregation"],"prefix":"10.1038","volume":"386","author":[{"given":"Grzegorz","family":"Sawicki","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Eduardo","family":"Salas","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jesus","family":"Murat","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Helena","family":"Miszta-Lane","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marek W.","family":"Radomski","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","reference":[{"key":"BF386616a0_CR1","first-page":"58","volume":"69","author":"W Siess","year":"1989","unstructured":"Siess, W. Molecular mechanisms of platelet activation. Pharmacol. Rev. 69, 58\u2013178 (1989).","journal-title":"Pharmacol. Rev."},{"key":"BF386616a0_CR2","doi-asserted-by":"publisher","first-page":"1425","DOI":"10.1096\/fasebj.4.5.2407587","volume":"4","author":"RW Colman","year":"1990","unstructured":"Colman, R. W. Aggregin: a platelet ADP receptor that mediates activation. FASEB J. 4, 1425\u20131435 (1990).","journal-title":"FASEB J."},{"key":"BF386616a0_CR3","doi-asserted-by":"publisher","first-page":"395","DOI":"10.1016\/0163-7258(94)90019-1","volume":"64","author":"P Sargeant","year":"1994","unstructured":"Sargeant, P. & Sage, S. O. Calcium signaling in platelet and other non-exictable cells. Pharmac. Ther. 64, 395\u2013443 (1994).","journal-title":"Pharmac. Ther."},{"key":"BF386616a0_CR4","doi-asserted-by":"crossref","first-page":"2062","DOI":"10.1183\/09031936.94.07112062","volume":"7","author":"JM Ray","year":"1994","unstructured":"Ray, J. M. & Stetler-Stevenson, W. G. The role of matrix metalloproteases and their inhibitors in tumour invasion, metastasis and angiogenesis. Eur. Respir. J. 7, 2062\u20132072 (1994).","journal-title":"Eur. Respir. J."},{"key":"BF386616a0_CR5","first-page":"11","volume-title":"Inhibition of Matrix Metalloproteinases: Therapeutic Approach","author":"JF Woessner Jr","year":"1994","unstructured":"Woessner, J. F. Jr in Inhibition of Matrix Metalloproteinases: Therapeutic Approach (eds Greenwald, R. A. & Golub, L M.) Vol. 732, 11\u201321 (Ann. NYAcad. Sci., New York, 1994)."},{"key":"BF386616a0_CR6","doi-asserted-by":"publisher","first-page":"728","DOI":"10.1016\/0955-0674(95)80116-2","volume":"7","author":"H Birkedal-Hansen","year":"1995","unstructured":"Birkedal-Hansen, H. Proteolytic remodeling of extracellular matrix. Curr. Opin. Cell Biol. 7, 728\u2013735 (1995).","journal-title":"Curr. Opin. Cell Biol."},{"key":"BF386616a0_CR7","doi-asserted-by":"publisher","first-page":"2844","DOI":"10.1161\/01.CIR.91.11.2844","volume":"91","author":"P Libby","year":"1995","unstructured":"Libby, P. Molecular bases of the actue coronary syndromes. Circulation 91, 2844\u20132850 (1995).","journal-title":"Circulation"},{"key":"BF386616a0_CR8","first-page":"605","volume":"69","author":"PR Petrequin","year":"1987","unstructured":"Petrequin, P. R., Tod, R. F. Devall, L. J., Boxer, L. A. & Curnutte, J. T. Association between gelatinase release and increased plasma membrane expression of the Mol glycoprotein. Blood 69, 605\u2013610 (1987).","journal-title":"Blood"},{"key":"BF386616a0_CR9","doi-asserted-by":"publisher","first-page":"365","DOI":"10.1006\/excr.1994.1211","volume":"213","author":"JL Seltzer","year":"1994","unstructured":"Seltzer, J. L. et al. Activation of 72-kDa type IV collagenase\/gelatinase by normal fibroblasts in collagen lattices is mediated by integrin receptors but is not related to lattice contraction. Exp. Cell Res. 213, 365\u2013374 (1994).","journal-title":"Exp. Cell Res."},{"key":"BF386616a0_CR10","first-page":"83","volume-title":"Proteolytic Enzymes: a Practical Approach","author":"G Salvesen","year":"1989","unstructured":"Salvesen, G. & Nagase, H. in Proteolytic Enzymes: a Practical Approach (eds Beynon, R. L. & Bond,}. S.) 83\u2013104 (IRL, Oxford University Press, Oxford, New York and Tokyo, 1989)."},{"key":"BF386616a0_CR11","doi-asserted-by":"publisher","first-page":"631","DOI":"10.1111\/j.1476-5381.1990.tb15858.x","volume":"100","author":"SC Cruwys","year":"1990","unstructured":"Cruwys, S. C., Davies, D. E. & Pettipher, E. R. Co-operation between interleukin-1 and the fibrinolytic system in the degradation of collagen by articular chondrocytes. Br. J. Pharmacol. 100, 631\u2013635 (1990).","journal-title":"Br. J. Pharmacol."},{"key":"BF386616a0_CR12","doi-asserted-by":"publisher","first-page":"61","DOI":"10.1038\/370061a0","volume":"370","author":"H Sato","year":"1994","unstructured":"Sato, H. et al. A matrix metalloproteinase expressed on the surface of invasive tumour cells. Nature 370, 61\u201365 (1994).","journal-title":"Nature"},{"key":"BF386616a0_CR13","doi-asserted-by":"publisher","first-page":"1647","DOI":"10.1172\/JCI107715","volume":"53","author":"CM Chesney","year":"1974","unstructured":"Chesney, C. M., Harper, E. & Colman, R. W. Human platelet collagenase. j. Clin Invest. 53, 1647\u20131654 (1974).","journal-title":"j. Clin Invest."},{"key":"BF386616a0_CR14","first-page":"743","volume":"18","author":"RM Leven","year":"1990","unstructured":"Leven, R. M. & Yee, T. Collagenase production by guinea pig megakaryocytes in vitro. Exp. Hematol. 18, 743\u2013747 (1990).","journal-title":"Exp. Hematol."},{"key":"BF386616a0_CR15","doi-asserted-by":"publisher","first-page":"485","DOI":"10.1016\/0049-3848(89)90203-X","volume":"53","author":"R Joseph","year":"1989","unstructured":"Joseph, R., Welch, K. M. A., D'Andrea, G. & Riddle, J. M. Evidence for the presence of red and white cells within \u2018platelet\u2019 aggregates formed in whole-blood. Thromb. Res. 53, 485\u2013491 (1989).","journal-title":"Thromb. Res."},{"key":"BF386616a0_CR16","doi-asserted-by":"crossref","first-page":"17374","DOI":"10.1016\/S0021-9258(18)71503-2","volume":"264","author":"WG Stetler-Stevenson","year":"1989","unstructured":"Stetler-Stevenson, W. G., Krutzsch, H. C. & Liotta, L. A. Tissue inhibitor of metalloproteinase (TIMP-2). A new member of the metalloproteinase inhibitor family. J. Biol. Chem. 264, 17374\u201317379 (1989).","journal-title":"J. Biol. Chem."},{"key":"BF386616a0_CR17","doi-asserted-by":"publisher","first-page":"8207","DOI":"10.1073\/pnas.86.21.8207","volume":"86","author":"GI Goldberg","year":"1989","unstructured":"Goldberg, G. I. et al. Human 72-kilodalton type IV collagenase forms a complex with a tissue inhibitor of metalloproteases designated TIMP-2. Proc. Natl Acad. Sci. USA 86, 8207\u20138211 (1989).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BF386616a0_CR18","doi-asserted-by":"publisher","first-page":"232","DOI":"10.1038\/newbio231232a0","volume":"231","author":"JR Vane","year":"1971","unstructured":"Vane, J. R. Inhibition of prostaglandin synthesis as a mechanism of action for aspirin-like drugs. Nature (New Biol.) 231, 232\u2013235 (1971).","journal-title":"Nature (New Biol.)"},{"key":"BF386616a0_CR19","doi-asserted-by":"publisher","first-page":"233","DOI":"10.1016\/0167-4889(95)00135-2","volume":"1310","author":"M Komoszynski","year":"1996","unstructured":"Komoszynski, M. & Wojtczak, A. Apyrases (ATP diphosphohydrolases, EC 3.6.1.5): function and relationship to ATPases. Biochim. Biophys. Acta 1310, 233\u2013241 (1996).","journal-title":"Biochim. Biophys. Acta"},{"key":"BF386616a0_CR20","doi-asserted-by":"crossref","first-page":"2810","DOI":"10.1016\/S0021-9258(17)35859-3","volume":"261","author":"GS Herron","year":"1986","unstructured":"Herron, G. S., Werb, Z., Dwer, K. & Banda, M. J. Secretion of metalloproteinases by stimulated capillary endothelial cells. I. Production of procollagenase and prostromelysin exceeds expression of proteolytic activity. J. Biol. Chem. 261, 2810\u20132813 (1986).","journal-title":"J. Biol. Chem."},{"key":"BF386616a0_CR21","doi-asserted-by":"publisher","first-page":"93","DOI":"10.1042\/bj2880093","volume":"288","author":"KM Southgate","year":"1992","unstructured":"Southgate, K. M., Davies, M., Booth, R. F. & Newby, A. C. Involvement of extracellular-matrix-degrading metalloproteinases in rabbit aortic smooth-muscle cell proliferation. Biochem. J. 288, 93\u201399 (1992).","journal-title":"Biochem. J."},{"key":"BF386616a0_CR22","doi-asserted-by":"publisher","first-page":"8154","DOI":"10.1073\/pnas.88.18.8154","volume":"88","author":"AM Henney","year":"1991","unstructured":"Henney, A. M. et al. Localization of stromelysin gene expression in atherosclerotic plaques by in situ hybridization. Proc. Natl Acad. Sci. USA 88, 8154\u20138158 (1991).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BF386616a0_CR23","doi-asserted-by":"publisher","first-page":"80","DOI":"10.1055\/s-0038-1646376","volume":"66","author":"R McEver","year":"1991","unstructured":"McEver, R. Leukocyte interactions mediated by selectins. Thromb. Haemost. 66, 80\u201387 (1991).","journal-title":"Thromb. Haemost."},{"key":"BF386616a0_CR24","first-page":"43","volume-title":"Nitric Oxide: a Modulator of Cell-Cell Interations in the Micro-circulation","author":"MW Radomski","year":"1995","unstructured":"Radomski, M. W. & Salas, E. in Nitric Oxide: a Modulator of Cell-Cell Interations in the Micro-circulation (ed. Kubes, P.) 43\u201374 (Springer, New York, 1995)."},{"key":"BF386616a0_CR25","doi-asserted-by":"publisher","first-page":"383","DOI":"10.1016\/0049-3848(83)90230-X","volume":"30","author":"MW Radomski","year":"1983","unstructured":"Radomski, M. W. & Moncada, S. An improved method for washing of human platelets with prostacyclin. Thromb. Res. 30, 383\u2013389 (1983).","journal-title":"Thromb. Res."},{"key":"BF386616a0_CR26","doi-asserted-by":"publisher","first-page":"196","DOI":"10.1016\/0003-2697(80)90338-3","volume":"102","author":"C Heussen","year":"1980","unstructured":"Heussen, C. & Dowdle, E. B. Electrophoretic analysis of plasminogen activators in polyacrylamide gels containing sodium dodecyl sulfate and copolymerized substrates. Analyt. Biochem. 102, 196\u2013202 (1980).","journal-title":"Analyt. Biochem."},{"key":"BF386616a0_CR27","doi-asserted-by":"publisher","first-page":"1688","DOI":"10.1172\/JCI118211","volume":"96","author":"A Zembowicz","year":"1995","unstructured":"Zembowicz, A., Jones, S. L. & Wu, K. W. Induction of cyclooxygenase-2 in human umbilical vein endothelial cells by lysophosphatidylcholine. J. Clin. Invest. 96, 1688\u20131692 (1995).","journal-title":"J. Clin. Invest."},{"key":"BF386616a0_CR28","doi-asserted-by":"crossref","first-page":"1","DOI":"10.4049\/jimmunol.156.1.1","volume":"156","author":"EJ Goetzl","year":"1996","unstructured":"Goetzl, E. J., Banda, M. J. & Leppert, D. Matrix metalloproteinases in immunity. J. Immunol. 156, 1\u20134 (1996).","journal-title":"J. Immunol."},{"key":"BF386616a0_CR29","doi-asserted-by":"publisher","first-page":"429","DOI":"10.1016\/B978-0-12-455555-6.50050-3","volume-title":"Platelets: Physiology and Pharmacology","author":"RD Feinman","year":"1985","unstructured":"Feinman, R. D., Detwiler, T. C. & Ingerman-Wojenski, C. in Platelets: Physiology and Pharmacology (ed. Longenecker, G. L.) 429\u2013440 (Academic, New York, 1985)."}],"container-title":["Nature"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/www.nature.com\/articles\/386616a0","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/386616a0.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/386616a0.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,5,17]],"date-time":"2023-05-17T03:11:02Z","timestamp":1684293062000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/386616a0"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1997,4]]},"references-count":29,"journal-issue":{"issue":"6625","published-print":{"date-parts":[[1997,4]]}},"alternative-id":["BF386616a0"],"URL":"https:\/\/doi.org\/10.1038\/386616a0","relation":{},"ISSN":["0028-0836","1476-4687"],"issn-type":[{"value":"0028-0836","type":"print"},{"value":"1476-4687","type":"electronic"}],"subject":[],"published":{"date-parts":[[1997,4]]}}}