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

2018 ◽  
Vol 24 (3) ◽  
pp. 111-122 ◽  
Author(s):  
Jinghua Hu ◽  
D Jo Merriner ◽  
Anne E O’Connor ◽  
Brendan J Houston ◽  
Luc Furic ◽  
...  

2015 ◽  
Vol 113 ◽  
pp. 226-243 ◽  
Author(s):  
Valérie Labas ◽  
Lucie Spina ◽  
Clémence Belleannee ◽  
Ana-Paula Teixeira-Gomes ◽  
Audrey Gargaros ◽  
...  

1994 ◽  
Vol 17 (5) ◽  
pp. 256-261 ◽  
Author(s):  
R. WEISSENBERG ◽  
S. YOSSEFI ◽  
Y. OSCHRY ◽  
I. MADGAR ◽  
L. M. LEWIN

Reproduction ◽  
2009 ◽  
Vol 137 (3) ◽  
pp. 379-389 ◽  
Author(s):  
P Sipilä ◽  
J Jalkanen ◽  
I T Huhtaniemi ◽  
M Poutanen

Apart from condoms and vasectomy, modern contraceptive methods for men are still not available. Besides hormonal approaches to stop testicular sperm production, the post-meiotic blockage of epididymal sperm maturation carries lots of promise. Microarray and proteomics techniques and libraries of expressed sequence tags, in combination with digital differential display tools and publicly available gene expression databases, are being currently used to identify and characterize novel epididymal proteins as putative targets for male contraception. The data reported indicate that these technologies provide complementary information for the identification of novel highly expressed genes in the epididymis. Deleting the gene of interest by targeted ablation technology in mice or using immunization against the cognate protein are the two preferred methods to functionally validate the function of novel genesin vivo. In this review, we summarize the current knowledge of several epididymal proteins shown eitherin vivoorin vitroto be involved in the epididymal sperm maturation. These proteins include CRISP1, SPAG11e, DEFB126, carbonyl reductase P34H, CD52, and GPR64. In addition, we introduce novel proteinases and protease inhibitor gene families with potentially important roles in regulating the sperm maturation process. Furthermore, potential contraceptive strategies as well as delivery methods will be discussed. Despite the progress made in recent years, further studies are needed to reveal further details in the epididymal sperm maturation process and the factors involved, in order to facilitate the development of new epididymal contraceptives.


2010 ◽  
Vol 340 (3) ◽  
pp. 569-581 ◽  
Author(s):  
Kelly Moore ◽  
Kyle Lovercamp ◽  
Dongyan Feng ◽  
Jennifer Antelman ◽  
Miriam Sutovsky ◽  
...  

2011 ◽  
Vol 32 (6) ◽  
pp. 665-671 ◽  
Author(s):  
B. Nixon ◽  
H. W. Ecroyd ◽  
J.-L. Dacheux ◽  
R. C. Jones

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 ◽  
...  

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.


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