Withdrawal: Identification of human aminopeptidase O, a novel metalloprotease with structural similarity to aminopeptidase B and leukotriene A4 hydrolase

Open AccessPublished:January 25, 2019DOI:
      VOLUME 280 (2005) PAGES 14310–14317
      This article has been withdrawn by the authors upon request from the Journal. The Journal raised questions regarding Fig. 4, A and B. The authors were able to locate the original autoradiographs corresponding to Fig. 4A, detecting two duplicated GAPDH control bands. In Fig. 4B, an actin lane appears to be duplicated. Since the original data for the experiment shown in Fig. 4B, performed 13 years ago, could not be found, the authors state that a new experiment was performed using RNA from mouse testis from different ages (10–74 days). The authors state that the AP-O expression results concur with an RNA-seq–based transcriptomic analysis reported independently by other researchers (Margolin et al. (2014) BMC Genomics 15, 39). The authors assert that all of the results reported in this article are valid.

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      • Identification of Human Aminopeptidase O, a Novel Metalloprotease with Structural Similarity to Aminopeptidase B and Leukotriene A4 Hydrolase
        Journal of Biological ChemistryVol. 280Issue 14
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          We have cloned and characterized a human brain cDNA encoding a new metalloprotease that has been called aminopeptidase O (AP-O). AP-O exhibits a series of structural features characteristic of aminopeptidases, including a conserved catalytic domain with a zinc-binding site (HEXXHX18E) that allows its classification in the M1 family of metallopeptidases or gluzincins. The structural complexity of AP-O is further increased by the presence of an additional C-terminal domain 170 residues long, which is predicted to have an ARM repeat fold originally identified in the Drosophila segment polarity gene product Armadillo.
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