{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,3]],"date-time":"2026-10-03T06:50:54Z","timestamp":1791010254231,"version":"4.1.0"},"reference-count":41,"publisher":"Oxford University Press (OUP)","issue":"2","license":[{"start":{"date-parts":[[2006,10,31]],"date-time":"2006-10-31T00:00:00Z","timestamp":1162252800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/pages\/standard-publication-reuse-rights"}],"funder":[{"DOI":"10.13039\/501100004359","name":"Swedish Research Council","doi-asserted-by":"publisher","award":["2002-6479"],"award-info":[{"award-number":["2002-6479"]}],"id":[{"id":"10.13039\/501100004359","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004359","name":"Swedish Research Council","doi-asserted-by":"publisher","award":["71X-15152"],"award-info":[{"award-number":["71X-15152"]}],"id":[{"id":"10.13039\/501100004359","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004359","name":"Swedish Research Council","doi-asserted-by":"publisher","award":["73X-09487"],"award-info":[{"award-number":["73X-09487"]}],"id":[{"id":"10.13039\/501100004359","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003173","name":"Crafoord Foundation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100003173","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100006075","name":"Greta and Johan Kock Foundation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100006075","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100005753","name":"Kungliga Fysiografiska S\u00e4llskapet","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100005753","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Thelma Zo\u00e9ga Foundation"},{"name":"Magn Bergvalls Foundation"},{"name":"\u00c5ke Wibergs Foundation"},{"name":"Alfred \u00d6sterlund Foundation"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2007,2,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Proteinase 3 (PR3) is found in granules of all neutrophils but also on the plasma membrane of a subset of neutrophils (mPR3). CD177, another neutrophil protein, also displays a bimodal surface expression. In this study, we have investigated the coexpression of these two molecules, as well as the effect of cell activation on their surface expression. We can show that CD177 is expressed on the same subset of neutrophils as mPR3. Experiments show that the expression of mPR3 and CD177 on the plasma membrane is increased or decreased in parallel during cell stimulation or spontaneous apoptosis. Furthermore, we observed a rapid internalization and recirculation of mPR3 and plasma membrane CD177, where all mPR3 is replaced within 30 min. Our findings suggest that the PR3 found on the plasma membrane has its origin in the same intracellular storage as CD177, i.e., secondary granules and secretory vesicles and not primary granules. PR3- and CD177-expressing neutrophils constitute a subpopulation of neutrophils with an unknown role in the innate immune system, which may play an important role in diseases such as Wegener\u2019s granulomatosis and polycythemia vera.<\/jats:p>","DOI":"10.1189\/jlb.0806514","type":"journal-article","created":{"date-parts":[[2006,10,31]],"date-time":"2006-10-31T23:33:27Z","timestamp":1162337607000},"page":"458-464","source":"Crossref","is-referenced-by-count":111,"title":["Proteinase 3 and CD177 are expressed on the plasma membrane of the same subset of neutrophils"],"prefix":"10.1093","volume":"81","author":[{"given":"Susanne","family":"Bauer","sequence":"first","affiliation":[{"name":"Department of Clinical Sciences, Section for Clinical and Experimental Infection Medicine, Lund University , Lund , Sweden"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mohamed","family":"Abdgawad","sequence":"additional","affiliation":[{"name":"Department of Nephrology, Clinical Sciences in Lund, Lund University , Lund , Sweden"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lena","family":"Gunnarsson","sequence":"additional","affiliation":[{"name":"Department of Nephrology, Clinical Sciences in Lund, Lund University , Lund , Sweden"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"M\u00e5rten","family":"Segelmark","sequence":"additional","affiliation":[{"name":"Department of Nephrology, Clinical Sciences in Lund, Lund University , Lund , Sweden"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hans","family":"Tapper","sequence":"additional","affiliation":[{"name":"Department of Clinical Sciences, Section for Clinical and Experimental Infection Medicine, Lund University , Lund , Sweden"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thomas","family":"Hellmark","sequence":"additional","affiliation":[{"name":"Department of Nephrology, Clinical Sciences in Lund, Lund University , Lund , Sweden"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2006,10,31]]},"reference":[{"key":"2023033007022622700_","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1111\/j.1432-1033.1973.tb02932.x","article-title":"The neutral proteases of human granulocytes. Isolation and partial characterization of two granulocyte collagenases.","volume":"36","author":"Ohlsson","year":"1973","journal-title":"Eur. J. Biochem."},{"key":"2023033007022622700_","doi-asserted-by":"crossref","first-page":"3503","DOI":"10.1182\/blood.V89.10.3503","article-title":"Granules of the human neutrophilic polymorphonuclear leukocyte.","volume":"89","author":"Borregaard","year":"1997","journal-title":"Blood"},{"key":"2023033007022622700_","doi-asserted-by":"crossref","first-page":"2487","DOI":"10.1182\/blood.V94.7.2487.419k07_2487_2496","article-title":"Presence of proteinase 3 in secretory vesicles: evidence of a novel, highly mobilizable intracellular pool distinct from azurophil granules.","volume":"94","author":"Witko-Sarsat","year":"1999","journal-title":"Blood"},{"key":"2023033007022622700_","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/0014-5793(95)01073-N","article-title":"Bimodal distribution of proteinase 3 (PR3) surface expression reflects a constitutive heterogeneity in the polymorphonuclear neutrophil pool.","volume":"374","author":"Halbwachs-Mecarelli","year":"1995","journal-title":"FEBS Lett."},{"key":"2023033007022622700_","doi-asserted-by":"crossref","first-page":"659","DOI":"10.1515\/bchm3.1994.375.10.659","article-title":"Comparison of properties of membrane bound versus soluble forms of human leukocytic elastase and cathepsin G.","volume":"375","author":"Bangalore","year":"1994","journal-title":"Biol. 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Immunol."},{"key":"2023033007022622700_","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1016\/0014-5793(94)00952-X","article-title":"Interleukin-8 processing by neutrophil elastase, cathepsin G and proteinase-3.","volume":"352","author":"Padrines","year":"1994","journal-title":"FEBS Lett."},{"key":"2023033007022622700_","doi-asserted-by":"crossref","first-page":"694","DOI":"10.1681\/ASN.V75694","article-title":"Proteinase 3, the major autoantigen of Wegener\u2019s granulomatosis, enhances IL-8 production by endothelial cells in vitro.","volume":"7","author":"Berger","year":"1996","journal-title":"J. Am. Soc. Nephrol."},{"key":"2023033007022622700_","doi-asserted-by":"crossref","first-page":"4612","DOI":"10.4049\/jimmunol.152.9.4612","article-title":"Proteinase 3. A neutrophil proteinase with activity on platelets.","volume":"152","author":"Renesto","year":"1994","journal-title":"J. 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