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Withdrawal: Matriptase-2, a membrane-bound mosaic serine proteinase predominantly expressed in human liver and showing degrading activity against extracellular matrix proteins

Open AccessPublished:January 25, 2019DOI:https://doi.org/10.1074/jbc.W118.007324
      VOLUME 277 (2002) PAGES 37637–37646
      This article has been withdrawn by the authors upon request from the Journal. In Fig. 6, a duplicated image of the lane corresponding to untreated fibrinogen was used in the PMSF-inactivated Matriptase-2 lane. In Fig. 8, actin panels were reused from previous publications of the group using the same commercial membranes, and the actin panel for the Northern blot containing spleen, thymus, prostate, testis, ovary, intestine, colon, and leukocyte samples was rotated 180 degrees. The liver-specific expression of Matriptase-2/TMPRSS6 shown in Fig. 8 can be compared to independent global RNA-seq studies (GTEx portal, https://www.gtexportal.org/home/gene/TMPRSS6). The authors assert that all of the results reported in this article are valid.

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      • Matriptase-2, a Membrane-bound Mosaic Serine Proteinase Predominantly Expressed in Human Liver and Showing Degrading Activity against Extracellular Matrix Proteins
        Journal of Biological ChemistryVol. 277Issue 40
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          We have identified and cloned a fetal liver cDNA encoding a new serine proteinase that has been called matriptase-2. This protein exhibits a domain organization similar to other members of an emerging family of membrane-bound serine proteinases known as type II transmembrane serine proteinases. Matriptase-2 contains a short cytoplasmic domain, a type II transmembrane sequence, a central region with several modular structural domains including two CUB (complement factor C1s/C1r, urchin embryonic growth factor,bone morphogenetic protein) domains and three low density lipoprotein receptor tandem repeats, and finally, a C-terminal catalytic domain with all typical features of serine proteinases.
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