Erratum to: Targeting MET kinase with the small-molecule inhibitor amuvatinib induces cytotoxicity in primary myeloma cells and cell lines
- Cornel Joseph Phillip†1, 6,
- Shadia Zaman†1,
- Shujun Shentu1,
- Kumudha Balakrishnan1, 6,
- Jiexin Zhang2,
- Veera Baladandayuthapani3, 6,
- Pietro Taverna7,
- Sanjeev Redkar7,
- Michael Wang5,
- Christine Marie Stellrecht†1, 6 and
- Varsha Gandhi†1, 4, 6Email author
© The Author(s). 2016
Received: 29 September 2016
Accepted: 29 September 2016
Published: 13 October 2016
The original article was published in Journal of Hematology & Oncology 2013 6:92
After the publication of this work , it was brought to our attention that two points needed to be explained further.
The revised Fig. 6c can be seen at the end of this Erratum with the corresponding and correct GAPDH image.
The interpretation of the results and findings of our investigations remain unchanged. As such, the results section that describes Fig. 6c remains the same. Also, correct images were used for quantification of the bands, and hence the quantitation figure (Fig. 6d) and associated text also do not change. Our findings remain valid and our inadvertent error did not affect our results, discussion, or the conclusions from this work, as the text refers to the correct values. We sincerely regret our error and apologize for any confusion this may have caused.
The second point was regarding similarity in the GAPDH and GSK-3β immunoblot (last 2 rows) in Fig. 7c. To generate this figure, protein lysates from each experiment were run on two different gels and transferred. The membranes from both gels were cut based on molecular marker, so that we would have a piece of the immunoblot containing proteins above ~80 kDa and a second piece containing proteins below ~80 kDa. The pieces of membranes above ~80 kDa were probed for Total and phospho-Met (quantitation of these blots were used in Fig. 6). Lower portions were used for Fig. 7c. One was used for phospho- and total-ERK and corresponding GAPDH. The other was used for phospho and total AKT (around 60 kDa) and phospho and total GSK-3β (around 40 kDa), along with GAPDH (around 37 kDa).
The lower 5 rows of the immunoblot were all from the same membrane and were probed as below. The membrane was first probed with a rabbit anti-phospho-AKT (S473) antibody followed by the secondary, which was a green fluorescent anti-rabbit antibody. Next, we probed with a mouse anti-total-AKT antibody followed by the secondary, which was a red fluorescent anti-mouse antibody. Next, we probed the blot with a rabbit anti-phospho-GSK-3β (S9) antibody followed by the secondary, which was a green fluorescent anti-rabbit antibody. Next, we probed with a mouse anti-total-GSK-3β antibody followed by the secondary, which was a red fluorescent anti-mouse antibody. Lastly, we probed with a mouse GAPDH antibody followed by the secondary red fluorescent anti-mouse antibody. We use a fluorescence based imaging system, LiCor Odyssey, to analyze immunoblots. With this system, our secondary antibodies against primary antibodies derived from different species are tagged with different fluorescence colors. The Odyssey software allows us to image each fluorescent channel separately as well and convert color image to grey scale image for publication. Because all 5 rows were from the same gel, and GSK3beta is fairly close to GAPDH, the shapes of each band in these two proteins appear similar. However, they are separate immunogenic reacted proteins as described above. This experiment was done in biological triplicate and quantitated using Odyssey Imaging software. The quantitated values were graphed in Fig. 7d, 7e, and 7f of the same published paper.
Because there were no errors in this figure, the published Fig. 7c is correct.
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