scholarly journals Presence, processing, and localization of mouse ADAM15 during sperm maturation and the role of its disintegrin domain during sperm–egg binding

Reproduction ◽  
2008 ◽  
Vol 136 (1) ◽  
pp. 41-51 ◽  
Author(s):  
Karina Pastén-Hidalgo ◽  
Rosaura Hernández-Rivas ◽  
Ana Lilia Roa-Espitia ◽  
Manuel Sánchez-Gutiérrez ◽  
Francisco Martínez-Pérez ◽  
...  
Keyword(s):  
Acrosome Reaction ◽  
Sperm Maturation ◽  
Epididymal Sperm ◽  
Male And Female ◽  
Antigen Present ◽  
Epididymal Maturation ◽  
Disintegrin Domain ◽  
35 Kda Protein ◽  
Proteolytic Product

Successful fertilization requires gametes to complete several stages, beginning with maturation and transport along the male and female reproductive tracts and ending with the interaction between the sperm and the egg. This last step involves sperm–egg adhesion and membrane fusion. ADAMs (disintegrin and metalloprotease domain proteins) are a family of membrane-anchored glycoproteins that are thought to play diverse roles in cell–cell adhesion through their interaction with integrins. This study analyzes the presence, location, processing, and possible role of ADAM15 in mouse sperm. The presence of ADAM15 in mouse spermatozoa was detected by Western blotting, which revealed that ADAM15 is post-translationally processed, during epididymal sperm maturation and the acrosome reaction. The 35 kDa antigen present in the acrosome-reacted sperm is the last proteolytic product of the 110/75 kDa ADAM15 found in non-capacitated sperm. This 35 kDa protein contains the disintegrin domain. By indirect immunofluorescence, ADAM15 was identified in the acrosomal region and along the flagellum of mouse spermatozoa. In acrosome-reacted sperm, ADAM15 was lost from the acrosomal region, but remained diffusely distributed throughout the head and flagellum. Furthermore, the ADAM15 disintegrin domain (RPPTDDCDLPEF) partially inhibited fusion and almost completely inhibited sperm–oolemma adhesion. In conclusion, our data indicate that ADAM15 is present in the testis and in spermatozoa from the caput, corpus, and cauda epididymis, as well as in non-capacitated and acrosome-reacted gametes. Results also indicate that ADAM15 is processed during epididymal maturation and acrosome reaction and that it may play a role during sperm–egg binding.

Observations on the Reproductive-Biology and Anatomy of Rhinolophus-Megaphyllus (Chiroptera, Rhinolophidae) in Eastern Australia

1992 ◽  
Vol 40 (5) ◽  
pp. 533 ◽  
Author(s):  
PH Krutzsch ◽  
RA Young ◽  
EG Crichton
Keyword(s):  
Corpus Luteum ◽  
Late Summer ◽  
Sperm Storage ◽  
Epididymal Sperm ◽  
Male And Female ◽  
Vaginal Plug ◽  
Eastern Australia ◽  
Accessory Sex Organs ◽  
Reproductive Events

The anatomy and chronology of reproductive events in male and female Rhinolophus megaphyllus from eastern Australia (27-32-degrees-S.) is discussed. Rhinolophus megaphyllus was monoestrous and monotocous. A delay of several months occurs between the delivery of spermatozoa to the caudae epididymides (late summer/early autumn) and copulation/ovulation/conception (winter), which occur towards the termination of the spermatogenic cycle. There is no storage of sperm in female tracts prior to ovulation but epididymal sperm storage persists beyond the time of birth (late spring). Male, but not female, readiness to initiate reproduction prior to the onset of winter, places this species in an 'intermediate' position with features of both temperate and tropical chiropteran reproductive cycle patterns. The presence of an extroverted corpus luteum in the female and of a complement of accessory sex organs in the male are normal glandular features for members of this chiropteran family. The role of the urethral gland is unknown; however, since there is no vaginal plug, its products apparently do not coagulate in the vagina in this species following insemination.

scholarly journals Role of WNT signaling in epididymal sperm maturation

2017 ◽  
Vol 35 (2) ◽  
pp. 229-236 ◽  
Author(s):  
Jin-Mei Cheng ◽  
Ji-Xin Tang ◽  
Jian Li ◽  
Yu-Qian Wang ◽  
Xiu-Xia Wang ◽  
...  
Keyword(s):  
Wnt Signaling ◽  
Sperm Maturation ◽  
Epididymal Sperm

scholarly journals Caput Ligation Renders Immature Mouse Sperm Motile and Capable to Undergo cAMP-Dependent Phosphorylation

2021 ◽  
Vol 22 (19) ◽  
pp. 10241
Author(s):  
Darya A. Tourzani ◽  
Maria A. Battistone ◽  
Ana M. Salicioni ◽  
Sylvie Breton ◽  
Pablo E. Visconti ◽  
...  
Keyword(s):  
Reproductive Tract ◽  
Female Reproductive Tract ◽  
Sperm Maturation ◽  
Molecular Pathways ◽  
Epididymal Sperm ◽  
Mammalian Sperm ◽  
Maturation In Vitro ◽  
Epididymal Maturation ◽  
Immature Mouse

Mammalian sperm must undergo two post-testicular processes to become fertilization-competent: maturation in the male epididymis and capacitation in the female reproductive tract. While caput epididymal sperm are unable to move and have not yet acquired fertilization potential, sperm in the cauda epididymis have completed their maturation, can move actively, and have gained the ability to undergo capacitation in the female tract or in vitro. Due to the impossibility of mimicking sperm maturation in vitro, the molecular pathways underlying this process remain largely unknown. We aimed to investigate the use of caput epididymal ligation as a tool for the study of sperm maturation in mice. Our results indicate that after seven days of ligation, caput sperm gained motility and underwent molecular changes comparable with those observed for cauda mature sperm. Moreover, ligated caput sperm were able to activate pathways related to sperm capacitation. Despite these changes, ligated caput sperm were unable to fertilize in vitro. Our results suggest that transit through the epididymis is not required for the acquisition of motility and some capacitation-associated signaling but is essential for full epididymal maturation. Caput epididymal ligation is a useful tool for the study of the molecular pathways involved in the acquisition of sperm motility during maturation.

scholarly journals Proteomic Analyses Reveal a Role of Cytoplasmic Droplets as an Energy Source during Epididymal Sperm Maturation

PLoS ONE ◽  
2013 ◽  
Vol 8 (10) ◽  
pp. e77466 ◽  
Author(s):  
Shuiqiao Yuan ◽  
Huili Zheng ◽  
Zhihong Zheng ◽  
Wei Yan
Keyword(s):  
Energy Source ◽  
Sperm Maturation ◽  
Epididymal Sperm ◽  
Proteomic Analyses

scholarly journals NCOA5 Haplo-insufficiency Results in Male Mouse Infertility through Increased IL-6 Expression in the Epididymis

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Shenglan Gao ◽  
Yueqi Zhang ◽  
Chengfeng Yang ◽  
Gloria I. Perez ◽  
Hua Xiao
Keyword(s):  
Male Infertility ◽  
Physiological Role ◽  
Sperm Maturation ◽  
Male Mice ◽  
Heterozygous Deletion ◽  
Epididymal Sperm ◽  
Nuclear Receptor Coactivator ◽  
Spermatozoa Motility ◽  
Morphological Defects

Abstract Male infertility might be caused by genetic and/or environmental factors that impair spermatogenesis and epididymal sperm maturation. Here we report that heterozygous deletion of the nuclear receptor coactivator-5 (Ncoa5) gene resulted in decreased motility and progression of spermatozoa in the cauda epididymis, leading to infertility in male mice. Light microscopic and ultrastructural analysis revealed morphological defects in the spermatozoa collected from the cauda epididymis of Ncoa5+/− mice. Immunohistochemistry showed that interleukin-6 (IL-6) expression in epithelial cells of Ncoa5+/− epididymis was higher than wild type counterparts. Furthermore, heterozygous deletion of Il-6 gene in Ncoa5+/− male mice partially improved spermatozoa motility and moderately rescued infertility phenotype. Our results uncover a previously unknown physiological role of NCOA5 in the regulation of epididymal sperm maturation and suggest that NCOA5 deficiency could cause male infertility through increased IL-6 expression in epididymis.

Deficiency for Lcn8 causes epididymal sperm maturation defects in mice

2021 ◽  
Vol 548 ◽  
pp. 7-13
Author(s):  
Zongzhuang Wen ◽  
Dongyue Liu ◽  
Haixia Zhu ◽  
Xiaoyang Sun ◽  
Yu Xiao ◽  
...  
Keyword(s):  
Sperm Maturation ◽  
Epididymal Sperm
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