Corrigendum for 398441“Hypidone hydrochloride (YL-0919) produces a fast-onset reversal of the behavioral and Synaptic Deficits Caused by Chronic Stress Exposure”

Yuhua Ran Zengliang Jin Xiaofei Chen Nan Zhao Xinxin Fang Zhang Liming Youzhi Zhang Yunfeng Li ^*

• Beijing Key Laboratory of Neuropsychopharmacology, Beijing Institute of Pharmacology and Toxicology, Beijing, China

Corrigendum for 398441Error in Figure/Table LegendIn the published article, there was an error in the legend for [[Figure 4] as published. [(C) Levels of pmTOR were quantified with mTOR]. The corrected legend appears below. [ (C) Levels of pmTOR were quantified with each β-actin and mTOR were quantified with each β-actin respectively, then the ratio of pmTOR/mTOR were show]The authors apologize for this error and state that this does not change the scientific conclusions of the article in any way. The original article has been updated.Missing Disscusion and citaionIn the published article [①Bauer DE, Haroutunian V, McCullumsmith RE, Meador-Woodruff JH. Expression of four housekeeping proteins in elderly patients with schizophrenia. J Neural Transm. 2009; 116(4):487–491. [PubMed: 19139805]. ②Ferguson RE, Carroll HP, Harris A, Maher ER, Selby PJ, Banks RE. Housekeeping proteins: a preliminary study illustrating some limitations as useful references in protein expression studies.Proteomics. 2005; 5(2):566–571. [PubMed: 15627964]. ③Eaton, S. L., Roche, S. L., Llavero Hurtado, M., Oldknow, K. J.et al., Total protein analysis as a reliable loading control for quantitative fluorescent Western blotting. PLoS One 2013, 8,e72457. [PubMed: 24023619]. ④Dittmer, A., Dittmer, J., Beta-actin is not a reliable loading control in Western blot analysis. Electrophoresis 2006, 27, 2844–2845.[PubMed: 16688701].] was not cited in the article. The citation has now been inserted in [Disscusion], [Paragraph 6, 7] and should read:In Figure 4, normalizationβ-actin is recognized as an internal reference. For most tissues and cells, its expression is abundant and stable. 42kd, not suitable for detecting 38-48 target proteins. In response to this issue, I think it is necessary to explore the rationality of b-actin as an internal reference. First of all, the actin family includes 6 proteins. The homology between different actins is as high as 90%. There are 4 muscle tissue-specific β-actin, and the other two are expressed in non-muscle tissues. The sample in this study is brain tissue, not muscle tissue. So specificity is not a problem. According to the following literature reports, there are three cases of β-actin changes. 1). In mouse spinal cord injury or muscle atrophy models, as well as some neurodegenerative diseases, the expression of actin will change (Ferguson 2005; Bauer 2009 ); 2). Changes in expression levels in different tissues of the same species. Studies have analyzed that the expression levels of actin in muscle, heart, bone, and fat of mice are different (Eaton, SL, 2013). 3). Changes in the expression of actin in different parts of the same tissue. In the sciatic nerve tissue of mice, the expression of actin is higher in the proximal tissue than in the distal tissue. Same as above 4, effective linear range of β- actin. An ideal internal control should have a wide linear interval to accommodate samples with different protein expression levels. Eaton et al.'s thermal study found that in brain homogenate, the linearity of β- actin was better when the total protein loading amount was between 10-30ug, and the band signal above 30ug tended to be saturated. However, the experiment ( Dittmer A ,2006)found that 2ug was saturated. This difference may be related to the experimental sample and the sensitivity of fluorescence chromatography. Of course, we know that the sensitivity of fluorescence chromatography is much higher than that of ECL luminescence method. Based on the above research onβ- actin as internal reference combined with the wb results in Fig.4 of our article, we unanimously agree and recognize that the quantitative method of WB mentioned by experts is the most correct and accurate, but in our experiment, it did not involve factors that cause actin to change. Any factor, therefore, we adopted an approach also adopted by many other colleagues to compare target proteins. This is of course not as accurate as the quantitative method mentioned by experts, but our method simplifies the steps. Although the process is not precise, it does not affect the final result. Biomedicine is developing rapidly, and western blot, as a protein semi-quantitative technology, is also undergoing innovation.For the experiments we completed ten years ago, the laboratory conditions at that time could only provide chemi-luminescence method for development. Nowadays, more sensitive fluorescence quantification is also very popular. We certainly believe that more and better technologies will appear in the future. Experimental technology that supports precise and in-depth biomedical research. However, although the chemiluminescence development method has limitations, it does not affect the reliability of the experimental results.The authors apologize for this error and state that this does not change the scientific conclusions of the article in any way. The original article has been updated.