TMEM95

Last update 08 May 2025

Basic Info

Synonyms

MGC129793, Sperm-egg fusion protein TMEM95, TMEM95

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Introduction

Sperm protein required for fusion of sperm with the egg membrane during fertilization.

100 Clinical Results associated with TMEM95

100 Translational Medicine associated with TMEM95

0 Patents (Medical) associated with TMEM95

Literatures (Medical) associated with TMEM95

01 Aug 2025·Theriogenology

Transmembrane protein 95 as a promising molecular marker of ram sperm functionality

Article

Author: Riesco, Marta F ; de Paz, Paulino ; Alvarez, Mercedes ; Anel, Luis ; Palacin-Martinez, Cristina ; Montes-Garrido, Rafael ; Soriano-Úbeda, Cristina ; Anel-Lopez, Luis ; Neila-Montero, Marta

The optimization of preservation protocols (refrigeration and freezing) in ovine species is necessary for a wider diffusion of artificial insemination in this species. Besides the ram sperm quality assays, the characterization of novel proteins could be crucial for improving these protocols employing biomarkers. The protein transmembrane 95 (TMEM95) is a sperm membrane protein associated with oocyte-sperm fusion previously described in bull or mouse. However, this protein has not yet been characterized in the ram until now. In this work, different experimental groups based on sperm functionality: capacitated, refrigerated at different times (5 °C 24 h, 5 °C 48 h, and 5 °C 72 h), and frozen-thawed sperm samples were analyzed and compared to initial sperm quality samples (15 °C 3 h) to characterize the expression of this novel protein and its relationship with other sperm quality markers (motility, kinetic parameters, viability, apoptosis-like events, mitochondrial function, acrosome-reacted, zinc content as marker of capacitation). In addition, capacitation status was tested by Fluozin-3, a novel fluorescent probe measuring zinc content used for the first time in ram sperm. After capacitation induction, as expected, acrosome reactive spermatozoa and zinc signature 2 and 3 were significantly increased, while linearity was significantly (P < 0.05) decreased compared to non-capacitated samples. Concerning TMEM95, its profile was significantly (P < 0.05) increased after the capacitation process, confirming its relationship with this spermatozoa status. Attending to preservation processes, as expected, semen quality decreased progressively during liquid storage, and a significant (P < 0.05) decrease was observed at 24 h according to fast progressive motility and linearity. TMEM95 profile showed the same decrease tendency, showing a significant reduction (P < 0.05) at 48 h with respect to the control samples. Finally, after the cryopreservation process, the semen quality of the thawed samples suffered a detrimental effect compared to the initial control sample, concerting all studied parameters accomplished by a significant (P < 0.05) decrease in TMEM95 profile compared to initial control samples. When we analyzed the TMEM95 correlation with other sperm quality markers, the highest positive correlations observed were with low sperm quality parameters in capacitated samples, such as apoptosis-like changes and acrosome-reaction. On the other hand, the highest positive correlations observed between TMEM95 and sperm quality parameters in preservation process samples were observed with suitable sperm quality parameters (motility, viability, and mitochondrial functionality). According to our results, this novel protein could be considered a predictor of early damage in ram sperm preservation protocols (cooling and freezing), considering its relationship with capacitation and membrane integrity status.

01 Apr 2025·Cell Reports

Noncanonical phagocytosis-like SEAL establishes mammalian fertilization

Article

Author: Inoue, Naokazu ; Wada, Ikuo ; Saito, Takako

In many forms of sexual reproduction, only the most robust spermatozoa, which overcome multiple physiological challenges, reach the oocyte. However, the exact mechanisms of gamete recognition and fusion are unknown. In the present study, we demonstrated that with the onset of gamete recognition, oocyte microvilli form lamellipodium-like structures, activate actin polymerization, and subsequently engulf spermatozoa to initiate gamete fusion. Gamete fusion occurred via a phagocytosis-like process we termed "sperm engulfment activated by IZUMO1-JUNO linkage and gamete fusion-related factors" (SEAL). Gamete adhesion was strictly regulated by binding of sperm IZUMO1 to oocyte JUNO, while SEAL was primarily mediated by sperm DCST1/2, SPACA6, TMEM95, FIMP, and TMEM81, the essential factors for gamete fusion. Interestingly, JUNO was almost depleted from oocyte surfaces in the region where SEAL enveloped spermatozoa by microvilli without actin polymerization. SEAL formation was recapitulated using JUNO-expressing K562 lymphocytic cells rather than oocytes. Together, these findings suggest that dynamic rearrangement of membrane components facilitates SEAL prior to successful fertilization.

01 Jan 2025·FUKUSHIMA JOURNAL OF MEDICAL SCIENCE

Molecular mechanisms leading to gamete fusion

Article

Author: Inoue, Naokazu

The fusion between spermatozoon and oocyte represents the final stage of fertilization in mammals.　Since only one of the extremely large number of spermatozoa fertilizes the oocyte, there should be a strictly regulated molecular mechanism in gamete fusion.　Oocyte CD9 was first identified as a key factor for gamete fusion, followed by sperm IZUMO1 and oocyte IZUMO1 receptor JUNO. Since 2020, with the recent emergence of genome editing technologies, new gamete fusion sperm factors, SPACA6, TMEM95, FIMP, SOF1, DCST1, and DCST2, have been reported one after another.　In this review, I would like to give an overview of mammalian gamete fusion based on the latest findings on these factors.

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TMEM95

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