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. 2018 Feb;17(2):2257-2262.
doi: 10.3892/mmr.2017.8147. Epub 2017 Nov 23.

Ran-binding protein M is associated with human spermatogenesis and oogenesis

Wen-Hao Tang  1 , Xin-Jie Zhuang  2 , Shi-De Song  3 , Han Wu  1 , Zhe Zhang  1 , Yu-Zhuo Yang  2 , Hong-Liang Zhang  2 , Jia-Ming Mao  2 , De-Feng Liu  2 , Lian-Ming Zhao  1 , Hao-Cheng Lin  1 , Kai Hong  1 , Lu-Lin Ma  1 , Jie Qiao  2 , Weibing Qin  4 , Yunge Tang  4 , Hui Jiang  1
Affiliations

Ran-binding protein M is associated with human spermatogenesis and oogenesis

Wen-Hao Tang et al. Mol Med Rep. 2018 Feb.

Abstract

The aim of the present study was to explore the underlying mechanism and diagnostic potential of Ran‑binding protein M (RanBPM) in human spermatogenesis and oogenesis. RanBPM expression in human testis and ovaries was analysed using polymerase chain reaction (PCR) and western blotting, and immunofluorescence was performed on testis and ovary tissue sections during different developmental stages of spermatogenesis and oogenesis using RanBPM antibodies. Interactions with a variety of functional proteins were also investigated. RanBPM mRNA and protein expression levels were determined by PCR and western blotting in the tissue sections. Results revealed that the mRNA expression levels were highest in the testis followed by the ovary. The RanBPM protein was predominantly localized in the nucleus of germ cells, and the expression levels were highest in pachytene spermatocytes and cells surrounding spermatids in testis tissue. In ovary cells, RanBPM was localized in the nucleus and cytoplasm. In conclusion, the results suggested that RanBPM may have multiple roles in the regulation of germ cell proliferation during human spermatogenesis and oogenesis. This research may provide a novel insight into the underlying molecular mechanism of RanBPM and may have implications for the clinical diagnosis and treatment of human infertility.

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Figures

Figure 1.
Figure 1.
Protein sequence of RanBPM and its structural domains. (A) RanBPM cDNA encodes 729 amino acids. (B) RanBPM is a member of the RAS superfamily and includes a CTLH domain, LisH domain, SPRY domain, pro-rich domain and a CRA domain. RanBPM, Ran-binding protein; LisH, lissencephaly type-1-like homology.
Figure 2.
Figure 2.
Human RanBPM was determined by PCR and western blotting. (A) PCR was performed on human tissues. RanBPM mRNA was expressed in the testis, ovary, kidney, heart and muscle tissues. (B) RanBPM was expressed in testis and ovary tissues (aged 25 weeks of fetal, 16 and 35 years of men) using western blotting. (C) RanBPM mRNA was different expression in 5 adult testis (aged 25–38 years). PCR, polymerase chain reaction; RanBPM, Ran-binding protein.
Figure 3.
Figure 3.
RanBPM expression was determined by immunostaining of testis sections. (A) The RanBPM was localized to the nucleus (red arrow shows) in human testis. (B) It was localized to the cytoplasm of testis cells (green arrow shows) too. RanBPM was present in both the nucleus and cytoplasm of testis cells, also expressed in the nucleus of primary spermatocytes, and is diffusely dispersed in the cytoplasm of round spermatids in testis of men aged 25–38 years. (C and D) Control testis tissues in men aged 25–38 years. RanBPM, Ran-binding protein.
Figure 4.
Figure 4.
Localization of RanBPM protein was detected in the developing female ovary. (A) The red arrow shows nuclear RanBPM expression and the green arrow shows cytoplasmic RanBPM expression. RanBPM was present in the nucleus and cytoplasm of ovary cells in women aged 15–28 years. (B) RanBPM was also evident in the nucleus of follicle cells, and was diffusely dispersed in the cytoplasm of granule cells. (C and D) Control ovary tissues in females aged 25–38 years. RanBPM, Ran-binding protein.
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