With the structural (c17-AA) alteration, the tablets will place a higher level of stress on the liver than the injectable. During longer or higher dosed cycles, liver values should therefore be watched closely through regular blood work. Such stress would of course be amplified when adding other c17-AA oral compounds to a cycle of stanozolol. When using such combinations, cautious users would make every effort to limit the length of the cycle not to be longer than a maximum of 6-8 weeks. It is also of note that stanozolol has been linked to strong adverse changes in the cholesterol levels. This side effect is common with anabolic steroid therapy, and obviously can become a health concern as the dose/duration of intake increase above normal. The oral version should have a greater impact on cholesterol values than the injectable due to the method of administration, and may therefore be the worse choice of the two for those concerned of this side effect. The oral use of stanozolol can also have a profound impact on levels of SHBG (sex hormone-binding globulin). This is characteristic of all anabolic/androgenic steroids, however its potency and form of administration makes oral stanozolol particularly noteworthy in this regard. Since plasma binding proteins such as SHBG act to temporarily constrain steroid hormones from exerting activity, this effect would provide a greater percentage of free (unbound) steroid hormone in the body. This may amount to an effective mechanism in which stanozolol could increase the potency of a concurrently used steroid. Proviron has an extremely high affinity for SHBG. This affinity may cause Proviron to displace other weaker substrates for SHBG, another mechanism in which the free hormone level may be increased. Adding stanozolol and Proviron to a testosterone cycle may therefore prove very useful, markedly enhancing the free state of this potent muscle building androgen.
The authors state that errors occurred during formatting of Fig 2B and Supplementary Fig 3C during the submission process of the original manuscript. The histogram of Fig 2B was mistakenly duplicated in Supplementary Fig S3C. The corrected histogram of Supplementary Fig S3C is shown below. In addition, Fig 2B contains two labeling errors of P‐values, originating from mistakes in the labeling during the graphical assembly of the figure: The P‐value for OSBPL3‐shRNA vs. scrambled shRNA should read instead of , and the P‐value for GJB3‐shRNA vs. scrambled shRNA should read instead of . The corrected Fig 2B is shown below. For the experiments shown in Fig 2B and Supplementary Fig S3C, a total number of 74–174 cells was analyzed in 3–14 vision fields per cell line.
Further, γH2AX staining of IMR90 cells mentioned in the results section (page 1373, last sentence “… telomerase‐negative BJ and IMR90 fibroblasts exhibited a strong accumulation of DNA damage (staining positive for both γH2AX and 53BP1) at early passage after shRNA transduction (Fig 2A, C and D, Supplementary Fig S3A and B)…” was not depicted in the paper, and the 53BP1 staining was performed only on the BJ cells. To correct for this mistake, the text and data presentation of the result section on the description of DNA damage foci (page 1373, last sentence, and page 1374, first paragraph) is specified as follows: “The experiments on IMR90 cells were conducted only for γH2AX staining. These results are now provided in Supplementary Fig S8”.
The description and presentation of Western blot results in Fig 1D (page 1372, first paragraph on the right column) is corrected as follows: The depicted analyses of p‐p53, p‐p38, and GAPDH in Fig 1D (see also the corresponding Source Data file in the original article) were all analyzed from the same blot. A repeat of the p‐p53 Western blot was run on a separate gel using the same protein lysates and loading buffer (see Source data for Figure 1D below).
The Western blot for p21 in Fig 1D and the corresponding beta‐actin control were run in parallel with the same protein lysates and the same loading on 2 separate gels; the gel probed for beta‐actin was not shown in the original source data file of Fig 1D. The gel was also used to repeat the analysis of p‐p38 expression (see Source data for Figure 1D below). Results of p21 induction were confirmed by immunofluorescence analysis (see Fig 1E and Supplementary Fig S2H–K of the original manuscript).
The corrections do not affect the original conclusions presented. The authors apologize for the mistakes and any inconvenience they might have caused.