Please provide a high-quality Persian translation of the following text, tailored for PhD graduates in medical sciences. You are absolutely free to change the sentence structure, vocabulary, and grammar as you wish for the best translation fit. Please adhere to the following guidelines:

1. Accuracy: Ensure grammatical precision and technical accuracy, particularly regarding medical terminology.

2. Fluency: Aim for natural language flow that sounds authentic to native Persian speakers in academic medical contexts.

3. Register: Maintain a formal academic tone appropriate for postgraduate-level medical professionals.

4. Clarity: Prioritize unambiguous communication of complex medical concepts.

5. Cultural adaptation:
   o Adapt any culture-specific references or idioms to Persian equivalents where appropriate.
   o Note any cultural nuances relevant to the Iranian medical context.

6. Restructuring: If necessary, rephrase or reorder sentences to enhance coherence and logical flow in Persian.

7. Annotations:
   o Briefly explain your choices for particularly challenging or nuanced passages.
   o Suggest alternative phrasings where multiple valid options exist.
   o Highlight any terms or concepts that may require additional explanation for the target audience.

8. Consistency: Maintain consistent terminology and style throughout the translation.

9. To improve the translation, you can use literary patterns and vocabulary found in Persian scientific literature.

10. References: If the original text includes citations or references, ensure they are formatted according to Persian academic conventions.

Your expertise in both the Persian language and medical sciences is crucial for this task. The goal is a translation that conveys the original meaning accurately and reads as if it were originally written in Persian for an advanced medical audience. Feel free to modify the language structure, vocabulary, and grammar as needed to achieve the most natural and effective translation in Persian.

"Our study demonstrates that overexpression of TSGA10 induces autophagy and apoptosis in HeLa cells, suggesting a potential tumor suppressive function of TSGA10. Specifically, we observed increased expression of autophagy-related genes, accumulation of acidic vesicles indicative of autophagic flux, upregulation of pro-apoptotic proteins, and a reduction in cell viability upon TSGA10 overexpression. Although these results provide valuable insights, several limitations require cautious interpretation and highlight the need for further investigation.
First, our experimental approach focused exclusively on overexpression of TSGA10 without complementary loss-of-function studies. To fully elucidate the role of TSGA10 in the regulation of autophagy and apoptosis, it is important to evaluate the effects of TSGA10 knockdown or knockout. Such studies would determine whether suppression of TSGA10 has opposite effects, thereby strengthening the causal relationship between TSGA10 expression and the observed cellular outcomes. Unfortunately, due to budget constraints, we were unable to perform knockdown experiments in the current study.
Second, we found that TSGA10 expression levels were not significantly different between normoxic and hypoxic conditions. This observation suggests that TSGA10 may not be directly regulated by hypoxia-inducible factors or that its overexpression through a strong promoter overrides any physiological regulation by oxygen levels. Previous studies have shown that hypoxia can modulate gene expression through HIF-1α-dependent and -independent pathways (28). Therefore, further studies are required to clarify the regulation of TSGA10 under different oxygen tensions and its interaction with hypoxia-responsive elements.
Third, although we observed a decrease in BCL-2 expression and an increase in the BAX/BCL-2 ratio in TSGA10-overexpressing cells, the mechanistic relationship between TSGA10 and BCL-2 remains unclear. Our molecular docking simulations suggested a possible interaction between TSGA10 and the BH2 domain of BCL-2, which is crucial for its anti-apoptotic function (29). However, computational predictions alone cannot confirm protein-protein interactions. To support this proposed interaction, experimental validation using techniques such as co-immunoprecipitation or proximity ligation assays is required. Furthermore, the reduction in BCL-2 levels could be due to indirect effects of TSGA10 overexpression on upstream signaling pathways rather than direct binding.
Moreover, our assessment of autophagy-related gene expression was limited to a select group of genes, including Beclin1, BNIP3, NIX, ATG5, LC3I, and LC3II. While these markers indicate autophagic activity, a more comprehensive analysis using transcriptomic approaches would allow a more comprehensive understanding of the molecular changes induced by TSGA10 overexpression. High-throughput RNA sequencing could identify additional genes and pathways involved in autophagy regulation and reveal potential compensatory mechanisms.
The connection between autophagy induction and reduced cell viability in TSGA10-overexpressing cells also requires further investigation. Autophagy can play a dual and context-dependent role in cancer, either promoting cell survival under stressful conditions or facilitating cell death when excessively activated (30). To determine whether the autophagy observed in our study contributes to cell death or represents a protective response, experiments with autophagy inhibitors (e.g. 3-methyladenine, bafilomycin A1) or genetic silencing of key autophagy genes (e.g. ATG5, Beclin1) insightful.
Furthermore, our studies were limited to the HeLa cell line, which may limit the generalizability of our results. HeLa cells possess unique characteristics, including high proliferation and genetic instability, which may influence their response to TSGA10 overexpression [4]. Expanding our studies to additional cancer cell lines of different origins as well as normal epithelial cells would allow a more comprehensive assessment of the role of TSGA10 in cellular homeostasis and tumorigenesis.
We also acknowledge that, although our molecular docking studies provide evidence for possible interactions between TSGA10 and BCL-2, they cannot replace experimental validation. The energy calculations indicating favorable binding provide a rationale for further investigation but do not confirm a direct interaction. Empirical evidence is needed to establish the biological relevance of this predicted interaction.
Our previous work has shown that TSGA10 can inhibit the activity of hypoxia-inducible factor 1-alpha (HIF-1α) by preventing its nuclear localization and transcriptional activity [5]. Since HIF-1α regulates genes involved in autophagy and apoptosis [6], it is plausible that TSGA10 indirectly modulates these pathways through HIF-1α inhibition. The interplay between the TSGA10, HIF-1α, and BCL-2 family proteins remains to be elucidated and represents an important avenue for future research.
Budget constraints limited our ability to conduct additional experiments that could answer these critical questions. Despite these limitations, our study provides preliminary evidence for the role of TSGA10 in promoting autophagy and apoptosis in cancer cells. These results contribute to the understanding of TSGA10 as a potential tumor suppressor and highlight its importance in cancer biology."