Retraction Watch

Tracking retractions as a window into the scientific process

Three expressions of concern added to cancer researcher’s notice list

with 12 comments

3.coverQuestions about data and conclusions in papers by a cancer researcher at the University of Maryland have led to three expressions of concern in the Journal of Biological Chemistry.

The notices follow four retractions — two for image duplications and two for unknown reasons — for Anil K. Jaiswal. The three papers under notice are all on mechanisms that regulate gene expression; PubPeer commenters have raised questions about some of the figures in the papers.

The expression of concern on all three papers reads, in full:

The publisher of the Journal of Biological Chemistry is issuing this Expression of Concern to notify readers that questions have been raised with the corresponding author’s institution regarding some of the data and the conclusions in the articles listed above. This Expression of Concern is solely intended to notify readers for informational purposes. It is not a statement regarding the validity of the data. The Journal of Biological Chemistry will provide additional information as it becomes available.

The papers that bear this notice are:

The first author on two of those papers is Suryakant K. Niture, who shares three retractions with Jaiswal; we couldn’t find contact info for him. Abhinav K. Jain is the first author on one paper, and co-author on another.

Bruce Jarrell, Chief Academic and Research Officer and UMB, told us that these EOCs and Jaiswal’s retractions are

all part of the same investigation. It’s been going on for at least two years, maybe longer.

We asked if he could provide details regarding which aspects of Jaiswal’s work were being investigated:

I can’t. That’s one of the restrictions I’m under.

We also reached out to Jaiswal and JBC. We’ll update this post with anything else we learn.

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Comments
  • fernandopessoa January 20, 2016 at 11:17 am

    The 4th retraction you covered was of a paper published at Baylor College of Medicine, and was without Suryakant K. Niture.
    http://retractionwatch.com/2015/02/06/fourth-retraction-appears-cancer-researcher-anil-jaiswal/

    Retraction Notice.
    http://cancerres.aacrjournals.org/content/67/11/5380

  • fernandopessoa January 21, 2016 at 1:10 pm

    Eur J Biochem. 1994 Nov 15;226(1):31-9.
    Human antioxidant-response-element-mediated regulation of type 1 NAD(P)H:quinone oxidoreductase gene expression. Effect of sulfhydryl modifying agents.
    Li Y1, Jaiswal AK.
    Author information
    1Department of Pharmacology, Fox Chase Cancer Center, Philadelphia, PA 19111.

    http://medschool.umaryland.edu/FACULTYRESEARCHPROFILE/viewprofile.aspx?id=9727

    “He joined as Assistant Professor at NYU Medical Center, New York followed by Associate Member in Fox Chase Cancer Center, Philadelphia. He moved to Baylor College of Medicine Houston, TX as Associate Professor in 1997 and was promoted to Full Professor in 2004. He joined the Department of Pharmacology and Experimental Therapeutics, University of Maryland, Baltimore, Maryland as Full Professor in 2007.”

    Pubpeer comment: https://pubpeer.com/publications/7957257

    Figure 5.
    http://imgur.com/x8BK74b

  • fernandopessoa June 23, 2016 at 5:53 am

    Paper same first author first two papers mentioned in post.

    Carcinogenesis. 2007 Feb;28(2):378-89. Epub 2006 Aug 31.
    Increased expression of the MGMT repair protein mediated by cysteine prodrugs and chemopreventative natural products in human lymphocytes and tumor cell lines.
    Niture SK1, Velu CS, Smith QR, Bhat GJ, Srivenugopal KS.
    Author information
    1Anticancer Resistance Research Group, Department of Pharmaceutical Sciences, Texas Tech University Health Sciences Center 1400 Wallace Boulevard, Amarillo, TX 79106, USA.

    https://pubpeer.com/publications/16950796

  • fernandopessoa June 23, 2016 at 7:30 am

    Paper where SK Niture (first author first two papers mentioned in post) is second author.

    Biochemistry. 2007 Jul 3;46(26):7765-80. Epub 2007 Jun 8.
    Human p53 is inhibited by glutathionylation of cysteines present in the proximal DNA-binding domain during oxidative stress.
    Velu CS1, Niture SK, Doneanu CE, Pattabiraman N, Srivenugopal KS.
    Author information
    1Anticancer Resistance Research Group, Department of Pharmaceutical Sciences, Texas Tech University Health Sciences Center, Amarillo, Texas 79106, USA.

    https://pubpeer.com/publications/336810EECD04F0B8DFD99E56559FC3#fb53154

    Figure 6.
    http://i.imgur.com/0bQrhLx.jpg

  • fernandopessoa February 3, 2017 at 6:38 am

    J Biol Chem. 2005 Aug 12;280(32):29158-68. Epub 2005 May 17.
    Nuclear import and export signals in control of Nrf2.
    Jain AK1, Bloom DA, Jaiswal AK.
    Author information
    1Department of Pharmacology, Baylor College of Medicine, Houston, TX 77030, USA.

    2017 retraction notice.
    http://www.jbc.org/content/292/5/2052.short
    This article has been retracted by the publisher. An investigation at the University of Maryland, Baltimore determined that contrast and brightness were enhanced to selectively conceal LDH and Lamin B bands in Fig. 4. This drastically reduced the apparent presence of Lamin B in the cytosol fraction and of LDH in the nuclear fraction, thereby artificially increasing the difference in the proteins compared to that in the other fraction examined.

    © 2017 by The American Society for Biochemistry and Molecular Biology, Inc.

  • fernandopessoa February 3, 2017 at 6:40 am

    J Biol Chem. 2006 Apr 28;281(17):12132-42. Epub 2006 Mar 2.
    Phosphorylation of tyrosine 568 controls nuclear export of Nrf2.
    Jain AK1, Jaiswal AK.
    Author information
    1Department of Pharmacology, Baylor College of Medicine, Houston, Texas 77030, USA.

    2017 retraction notice.
    http://www.jbc.org/content/292/5/2051.short
    This article has been retracted by the publisher. An investigation at the University of Maryland, Baltimore determined in both the submitted but unpublished and in the published versions of Fig. 2, empty lanes were purported to depict absence of labeling in pcDNA. Examining the unedited version shows that the image was obtained from a region outside of the gel, where no labeling can occur. The figure does not support that there is no labeling after transfection with the empty pcDNA vector and the claim that transfection with the active constructs had a specific effect. The investigation also determined that in Fig. 6, in the versions submitted to EMBO, JBC (first submission), and to Mol. Cell. Biol., images of transfected Hepa-1 cells were obtained from a single sample, captured from a single microscope field, and then presented as if they originated from different samples. Whereas in the originally submitted versions, the treatment is described as “LMB,” in the published version, the same data are purported to show effects of PP2.

    © 2017 by The American Society for Biochemistry and Molecular Biology, Inc.

  • fernandopessoa February 3, 2017 at 6:42 am

    J Biol Chem. 2008 Jun 20;283(25):17712-20. doi: 10.1074/jbc.M709854200. Epub 2008 Apr 23.
    Phosphorylation and dephosphorylation of tyrosine 141 regulate stability and degradation of INrf2: a novel mechanism in Nrf2 activation.
    Jain AK1, Mahajan S, Jaiswal AK.
    Author information
    1Department of Pharmacology and Experimental Therapeutics, University of Maryland School of Medicine, Baltimore, Maryland 21201, USA.

    2017 retraction notice.
    http://www.jbc.org/content/292/5/2050.short

    This article has been retracted by the publisher. In Fig. 3C, cytosol panels, lanes 5 and 6 were duplicated in the INrf2-V5 immunoblot. Additionally, lanes 5 and 6 were duplicated in the INrf2-Y141A-V5 immunoblot. In Fig. 3C, nucleus panels, lanes 1 and 2 of the INrf2-V5 immunoblot were duplicated. Additionally, the Lamin B immunoblot was duplicated in the top and bottom panels.

    © 2017 by The American Society for Biochemistry and Molecular Biology, Inc.

  • fernandopessoa February 3, 2017 at 7:19 am

    J Biol Chem. 2009 May 15;284(20):13856-68. doi: 10.1074/jbc.M808084200. Epub 2009 Mar 11.
    Prothymosin-alpha mediates nuclear import of the INrf2/Cul3 Rbx1 complex to degrade nuclear Nrf2.
    Niture SK1, Jaiswal AK.
    Author information
    1Department of Pharmacology and Experimental Therapeutics, University of Maryland School of Medicine, Baltimore, Maryland 21201.

    2017 retraction notice.
    http://www.jbc.org/content/292/5/2049.short
    This article has been retracted by the publisher. An investigation at the University of Maryland, Baltimore determined that there is evidence of duplication in Fig. 2B. The investigation also determined that in Fig. 3, data in Cul3, INrf2, and Rbx1 show clear evidence of manipulations in which individual blots were spliced and rearranged. In Fig. 5A, duplication of bands is apparent. In addition, the journal determined that in Fig. 1B, left panel, lanes 6 and 9 were duplicated. The Lamin B immunoblot from Fig. 5D was reused as Lamin B in Fig. 5E. Also in Fig. 5E, the INrf2 immunoblot from 25 nM and 50 nM PTMα siRNA were duplicated. In Fig. 9B, lanes 5 and 6 of the PTMα immunoblot were duplicated.

    © 2017 by The American Society for Biochemistry and Molecular Biology, Inc.

  • fernandopessoa February 3, 2017 at 7:21 am

    J Biol Chem. 2011 Aug 19;286(33):28821-32. doi: 10.1074/jbc.M111.255042. Epub 2011 Jun 20.
    Src subfamily kinases regulate nuclear export and degradation of transcription factor Nrf2 to switch off Nrf2-mediated antioxidant activation of cytoprotective gene expression.
    Niture SK1, Jain AK, Shelton PM, Jaiswal AK.
    Author information
    1Department of Pharmacology and Experimental Therapeutics, University of Maryland School of Medicine, 655 West Baltimore Street, Baltimore, Maryland 21201, USA.

    2017 retraction.
    http://www.jbc.org/content/292/5/2048.short

    This article has been retracted by the publisher. Phillip M. Shelton agrees with the retraction. An investigation at the University of Maryland, Baltimore determined that bands depicted in several figures were digitally altered as follows.

    In Fig. 2, the LaminB immunoblot from “Src siRNA” was digitally mirrored and duplicated as LDH in the “YES siRNA” panel. Bands 4, 5, and 6 in the LDH panels of the Fyn and Lyn panels were duplicated.

    In Fig. 4A, in the Nrf2-V5 panel, bands 1 and 2 and bands 4 and 5 are identical. Similarly, in the IP:pTyr lane, bands 5 and 6 are identical. In Fig 4B, there is evidence of splicing in the Nrf2-V5 panel. In addition, in the FLAG panel, bands 1 and 2 and bands 4 and 7 are identical.

    In Fig. 5A, there is evidence of splicing in the Nrf2 panel. In addition, bands 1 and 2 in the Src panel are identical. In Fig. 5C, in the Nrf2 panel, lanes 1 and 2 and lanes 5 and 8 are identical. Similarly, in the Fyn panel, lanes 1 and 2 are identical. In addition, lanes 4 and 5 were duplicated and presented as mirror images of each other. In Fig. 5E, lanes 4 and 5 from the IP:V5 WB:pTyr panel were duplicated in Fig. 7A, right panel LDH, lanes 4 and 5.

    In Fig. 7A, the left Lyn panel and the right Yes panel were duplicated after resizing. In Fig. 7B, the left and right GSKβ panels were duplicated after resizing.

    In Fig. 8A, in the NQO1 panel, bands 2 and 6 are identical. In the HO-1 panel, bands 2 and 6 were resized and duplicated. In the GCLC panel, bands 1 and 6 were duplicated.

    In addition, the journal determined that lanes 2–4 of the HO-1 immunoblot from the “Yes siRNA” panel from Fig. 1A was flipped horizontally and reused in lanes 2–4 of the Lyn immunoblot from the “Lyn siRNA” panel of the same figure. In Fig. 2, lanes 3 and 6 of the Src immunoblot from the “Src siRNA” panel were duplicated. In Fig. 5D, lanes 2 and 5 of the IP:V5 WB:pSer immunoblot from the right panels were duplicated. In Fig. 6D, lanes 1–4 of the Lamin B immunoblot from SYF+/+ MEFs were duplicated in the LDH immunoblot from Fig. 7B, right panel. The LDH immunoblot from Fig. 7A, left panel, was duplicated as LDH in Fig. 7B, left panel. The right Fyn panel and the right Src panel were duplicated in Fig. 7A. In Fig. 7B, lanes 3 and 5 of the GSKβpY216 immunoblot, right panel, were duplicated.

    © 2017 by The American Society for Biochemistry and Molecular Biology, Inc.

  • fernandopessoa February 3, 2017 at 7:22 am

    J Biol Chem. 2012 Dec 7;287(50):41608-18. doi: 10.1074/jbc.M112.387738. Epub 2012 Oct 18.
    NAD(P)H:quinone oxidoreductase 1 (NQO1) competes with 20S proteasome for binding with C/EBPα leading to its stabilization and protection against radiation-induced myeloproliferative disease.
    Xu J1, Jaiswal AK.
    Author information
    1Department of Pharmacology and Experimental Therapeutics, University of Maryland School of Medicine, Baltimore, Maryland 21201, USA.

    2017 retraction.
    http://www.jbc.org/content/292/5/2047.short

    This article has been retracted by the publisher. An investigation at the University of Maryland, Baltimore determined that the data shown in Fig. 2A are unreliable and do not support the hypothesis of this work.

    © 2017 by The American Society for Biochemistry and Molecular Biology, Inc.

  • fernandopessoa February 3, 2017 at 7:51 am
  • fernandopessoa February 3, 2017 at 7:59 am

    http://data.baltimoresun.com/salaries/state/cy2015/?showvals=true&NullVariableName=&sortby=first-name&sortdirection=DESC&page=11342

    First Name ANIL
    Middle initial K
    Last name JAISWAL
    Suffix
    Pay system (CT, RG or UM)† UM
    Agency number 360221
    Organization UNIVERSITY OF MARYLAND
    Organization subtitle 360221-UMB
    Classification code 1212
    Salary/pay scale* $265,000.00
    Actual regular wages earned $274,000.00
    Date of hire (EOD) 2007-06-03
    Overtime earnings $0.00
    Other earnings $0.00
    YTD gross compensation** $274,000.00
    Pay type (hourly, annually or daily) A
    Termination date

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