Open AccessPRSS55 plays an important role in the structural differentiation and energy metabolism of sperm and is required for male fertility in mice
Author(s) -
Zhu Feng,
Li Wen,
Zhou Xinli,
Chen Xu,
Zheng Meimei,
Cui Yiqiang,
Liu Xiaofei,
Guo Xuejiang,
Zhu Hui
Publication year - 2021
Publication title -
journal of cellular and molecular medicine
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.44
H-Index - 130
eISSN - 1582-4934
pISSN - 1582-1838
DOI - 10.1111/jcmm.16116
Subject(s) - sperm , biology , andrology , sperm motility , microbiology and biotechnology , spermatogenesis , motility , zona pellucida , sertoli cell , knockout mouse , sterility , proteases , genetics , endocrinology , oocyte , embryo , gene , medicine , biochemistry , enzyme
Abstract Orderly and stage‐specifically expressed proteins are essential for spermatogenesis, and proteases play a key role in protein activation and function. The present study aimed to investigate serine protease 55 (PRSS55), which was reported to play a role in sperm‐uterotubal junction (UTJ) migration and sperm‐zona pellucida (ZP) binding. We found that PRSS55 was specifically expressed in testicular spermatids and epididymal spermatozoa. By constructing knockout mice targeting all transcripts of Prss55 , we demonstrated that deletion of Prss55 resulted in a serious decline of male fertility, with significantly increased sperm malformation and decreased sperm motility. In Prss55 −/− mice, increased structural abnormality, including deficient “9 + 2” microtubules, damaged peripheral dense fibre, and defective mitochondrial cristae, were found in sperm. In addition, sperm showed decreased expression of electron transfer chain molecules and lower ATP contents. These could be the potential causes of the astheno/teratozoospermia phenotype of the Prss55 −/− mice, and provided new evidence for the previously reported impaired sperm‐UTJ migration. Moreover, preliminary studies allowed us to speculate that PRSS55 might function by activating type II muscle myosin in the testis, which is involved in many processes requiring motivation and cytoskeleton translocation. Thus, PRSS55 is essential for the structural differentiation and energy metabolism of sperm, and might be a potential pathogenic factor in astheno/teratozoospermia. Our results provide an additional explanation for the male sterility of Prss55 −/− mice, and further reveal the role of PRSS55.