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Published on: August 23, 2014
Expression and function of HSP110 family in mouse testis after vasectomy
Zhen-Ning Du1, Cheng-Ting Rong1,2, Shi Hui1
1Department of Medicine, Yantai University, Yantai 264005, China.
Abstract:
HSP110 functions to protect cells, tissues, and organs from noxious conditions. Vasectomy induces apoptosis in the testis; however, little is known about the reason leading to this outcome. The aim of the present study was to evaluate the expression and function of HSP110 in mouse testis after vasectomy. Following bilateral vasectomy, we used fluorescent Terminal deoxynucleotidyl transferase dUTP nick end labeling (TUNEL) to detect apoptosis, Western blotting and immunohistochemistry to examine HSP110 expression and localization. Serum antisperm antibody (AsAb) and testosterone were measured by Enzyme-linked immunosorbent assay (ELISA) and radioimmunoassay, respectively. Expression of endoplasmic reticulum stress (ERS) sensors and downstream signaling components was measured by Reverse Transcription-Polymerase Chain Reaction (RT-PCR), and the phosphorylation of eIF2α and JNK was detected by Western blotting. Vasectomy induced morphologic changes, increased apoptosis in the testis, increased serum AsAb, and decreased testosterone levels. After vasectomy, ORP150 mRNA level was increased first and then decreased, Bcl-2 was decreased, and the expression of HSPA4l, GRP78, GADD153, PERK, ATF6, IRE-1, XBP-1s, Bax, Bak, and caspases and the phosphorylation of eIF2α and JNK were increased. We present that an ER stress-mediated pathway is activated and involved in apoptosis in the testis after vasectomy. HSPA4l and ORP150 may play important roles in maintaining the normal structure and function of testis.
Insights
Vasectomy triggers testicular apoptosis via endoplasmic reticulum stress (ERS). Heat shock protein 110 (HSP110) and related proteins may protect testicular cells from this damage.
Area of Science:
- Reproductive biology
- Cellular stress response
- Molecular mechanisms of apoptosis
Background:
- Heat shock proteins (HSPs) protect cells from various stressors.
- Vasectomy is known to induce testicular apoptosis, but the underlying mechanisms are not fully understood.
- Understanding HSP110's role in post-vasectomy testicular changes is crucial.
Purpose of the Study:
- To investigate the expression and function of HSP110 in mouse testes following vasectomy.
- To elucidate the role of endoplasmic reticulum stress (ERS) in vasectomy-induced testicular apoptosis.
- To identify potential protective factors against testicular damage after vasectomy.
Main Methods:
- Bilateral vasectomy in mice.
- Assessment of apoptosis using fluorescent Terminal deoxynucleotidyl transferase dUTP nick end labeling (TUNEL).
- Analysis of HSP110 expression via Western blotting and immunohistochemistry.
- Measurement of serum antisperm antibodies (AsAb) and testosterone levels (ELISA, radioimmunoassay).
- Evaluation of ERS markers (mRNA and protein phosphorylation) using RT-PCR and Western blotting.
Main Results:
- Vasectomy led to testicular morphological changes, increased apoptosis, elevated serum AsAb, and reduced testosterone levels.
- HSP110 expression and markers of ERS (e.g., GRP78, GADD153, PERK, ATF6, IRE-1, XBP-1s) were significantly upregulated post-vasectomy.
- Pro-apoptotic proteins (Bax, Bak, caspases) and phosphorylated eIF2α and JNK increased, while anti-apoptotic Bcl-2 decreased.
- ORP150 mRNA levels initially increased then decreased; HSPA4l expression was elevated.
Conclusions:
- An ER stress-mediated pathway is activated and contributes to testicular apoptosis after vasectomy.
- HSPA4l and ORP150 may play significant roles in preserving testicular structure and function following vasectomy.
- HSP110 and its related proteins warrant further investigation for their protective potential against vasectomy-induced testicular damage.
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