Journal of Cellular Physiology最新文献

Bertacchini J, Mediani L, Beretti F, et al. Clusterin enhances AKT2-mediated motility of normal and cancer prostate cells through a PTEN and PHLPP1 circuit. J Cell Physiol. 2019;234:11188–11199. https://doi.org/10.1002/jcp.27768

In the original version of this article, the authors mistakenly duplicated the panels showing AKT1 levels in Figure 1c and the panels showing clusterin (CLU) levels in Figure 3c.

In the correct Figure 1c below, the authors replaced the lower right panels (CLU cells transfected with scramble shRNA or shAkt2) with a replicate experiment showing the proper anti-Akt1 blot. Equal loading of CLU cell lysates was probed by anti-CLU.

In the correct Figure 3c below, the author replaced the panels showing CLU and ACTIN levels in the PC3 cell line with a replicate experiment.

This correction doesn't change the results and conclusions. The authors apologize for any confusion these errors may have caused.

Hawaiʻi's diverse population prime it to be an exemplary environment to study representation in science, technology, engineering, mathematics, and medicine (STEMM). In actuality, Hawaiʻi has low STEMM enrollment and therefore, low representation in STEMM. What primarily inhibits Hawaiʻi from having a strong STEMM workforce is the lack of education in STEMM, resources allocated to STEMM, and mentorship to succeed in STEMM. Other factors such as cultural values, high costs of living, and geographical barriers also contribute to Hawaiʻi's low STEMM enrollment. To combat these issues, I offer suggestions to encourage STEMM enrollment, such as directing funds toward after-school education. I also suggest combatting the lack of resources by providing more online opportunities for students and workers. As for Hawaiʻi's low mentorship, I suggest that more programs be created within communities and universities to create a platform for mentors and mentees to network. This manuscript seeks to highlight these areas of improvement and recognize lessons to be learned from Hawaiʻi, thus serving as a resource for individuals internationally.

Retraction: S. Mukherjee, S. Manna, D. Pal, P. Mukherjee, C. K. Panda, Sequential loss of cell cycle checkpoint control contributes to malignant transformation of murine embryonic fibroblasts induced by 20-methylcholanthrene, Journal of Cellular Physiology 224, no. 1 (2010): 49-58, https://doi.org/10.1002/jcp.22089. The above article, published online on 23 April 2010 in Wiley Online Library (wileyonlinelibrary.com), has been retracted by agreement between journal Editor in Chief, Alexander Hutchison; and Wiley Periodicals LLC. Concerns were raised by a third party regarding image manipulation and duplication in the above article. An investigation by the publisher has confirmed the following image-related concerns: duplication and splicing of western blots in Figure 3B(i); rotation, resizing, and duplication of cellular sections in Figure 4; duplication of cellular sections between Figure 4 and Figure 6 C; duplication of western blots in Figure 5B; duplication of western blots in Figure 6 A; and duplication of cellular sections in Figure 6 C. Because the evidence of image manipulation is extensive and impacts several figures, the journal has determined that the results are fundamentally compromised, and so the journal must retract the article. The authors disagree with the retraction.

Huang, H., Wu, Q., Guo, X., Huang, T., Xie, X., Wang, L., Liu, Y., Shi, L., Li, W., Zhang, J., & Liu, Y. (2021). O-GlcNAcylation promotes the migratory ability of hepatocellular carcinoma cells via regulating FOXA2 stability and transcriptional activity. J Cell Physiol, 236, 7491–7503. https://doi.org/10.1002/jcp.30385

In the first published version of this manuscript, a transwell migration microscope image presented in Figure 6b of the HepG2 Mock group was accidentally misused during the assembly of the figures, resulting in image duplication. In the corrected Figure 6b below, the photo corresponding to HepG2 Mock group has been replaced with the original and accurate one.

The authors regret the initial mistake in manuscript preparation. This error does not affect the scientific validity of the conclusions of this study. The authors apologize for any confusion they may have caused.

This study delved into the role of delta-like noncanonical notch ligand 2 (DLK2) in the cell cycle, proliferation, apoptosis, and differentiation of myoblasts, as well as its interaction with the classical Wnt/β-catenin signaling pathway in regulating myoblast function. The research revealed that upregulation of DLK2 in myoblasts during the proliferation phase enhanced myoblast proliferation, facilitated cell cycle progression, and reduced apoptosis. Conversely, downregulation of DLK2 expression using siRNA during the differentiation phase promoted myoblast hypertrophy and fusion, suppressed the expression of muscle fiber degradation factors, and expedited the differentiation process. DLK2 regulates myoblasts function by influencing the expression of various factors associated with the Wnt/β-catenin signaling pathway, including CTNNB1, FZD1, FZD6, RSPO1, RSPO4, WNT4, WNT5A, and adenomatous polyposis coli. In essence, DLK2, with the involvement of the Wnt/β-catenin signaling pathway, plays a crucial regulatory role in the cell cycle, proliferation, apoptosis, and differentiation of myoblasts.

M. Ghasemi-Chaleshtari, S. H. Kiaie, M. Irandoust, H. Karami, M. N. Afjadi, S. Ghani, N. A. Vanda, M. J. Ghaderi Sede, A. Ahmadi, A. Masjedi, H. Hassannia, F. Atyabi, M. Hojjat-Farsangi, A. Namdar, G. Ghalamfarsa, F. Jadidi-Niaragh, “Concomitant blockade of A2AR and CTLA-4 by siRNA-loaded polyethylene glycol-chitosan-alginate nanoparticles synergistically enhances antitumor T-cell responses,” Journal of Cellular Physiology 235, no. 12 (2020): 10068-10080, https://doi.org/10.1002/jcp.29822.

In the original version of this article, the authors mistakenly duplicated the panels showing the β-actin bands across Figure 2b, 2f and Figure 4e. While Figure 2b and 2f share the same cellular origin and treatment, the β-actin bands in Figure 4e have been mistakenly used. The corrected Figure 4e is shown below.

This correction doesn't change the results and conclusions. The authors apologize for any confusion these errors may have caused.

Previously we showed hyperosmotic solution caused TRPV1-dependent NKCC1 activation in the lens by a mechanism that involved ERK1/2 signaling. In various tissues, integrins and the cytoskeletal network play a role in responses to osmotic stress. Here, we examined the association between integrins and TRPV1-dependent activation of NKCC1 in mouse lens epithelium. Wild-type (WT) lenses exposed to the integrin agonist leukadherin-1 (LA-1) for 10 min displayed a ~33% increase in the bumetanide-sensitive rate of Rb uptake indicating NKCC activation. Paclitaxel, a microtubule stabilizing agent, abolished the Rb uptake response. In primary cultured lens epithelium LA-1 caused a robust ERK1/2 activation response that was almost fully suppressed by paclitaxel. The TRPV1 agonist capsaicin caused a similar ERK1/2 activation response. Consistent with an association between integrins and TRPV1, the TRPV1 antagonist A889425 prevented the Rb uptake response to LA-1 as did the ERK inhibitor U0126. LA-1 did not increase Rb uptake by lenses from TRPV1 knockout mice. In cells exposed to a hyperosmotic stimulus, both the ERK1/2 activation and Rb uptake responses were prevented by paclitaxel. Taken together, the findings suggest TRPV1 activation is associated with integrins and the tubulin cytoskeleton. This aligned with the observation that LA-1 elicited a robust cytoplasmic calcium rise in cells from WT lenses but failed to increase calcium in cells from TRPV1 knockout lenses. The results are consistent with the notion that integrin activation by LA-1, or a hyperosmotic stimulus, causes TRPV1 channel opening and the consequent downstream activation of the ERK1/2 and NKCC1 responses.