Human sperm head morphometric distribution and its influence on human fertility

1998 ◽  
Vol 70 (5) ◽  
pp. 883-891 ◽  
Author(s):  
Nabil Aziz ◽  
Simon Fear ◽  
Clare Taylor ◽  
Charles R Kingsland ◽  
D.Iwan Lewis-Jones
2020 ◽  
Vol 22 (4) ◽  
pp. 401
Author(s):  
MaríaPaz Herráez ◽  
Silvia González-Rojo ◽  
Cristina Fernández-Díez ◽  
Marta Lombó

2021 ◽  
pp. 177-191
Author(s):  
Natalia V. Revollo ◽  
G. Noelia Revollo Sarmiento ◽  
Claudio Delrieux ◽  
Marcela Herrera ◽  
Rolando González-José

2012 ◽  
Vol 98 (2) ◽  
pp. 315-320 ◽  
Author(s):  
Atsushi Tanaka ◽  
Motoi Nagayoshi ◽  
Izumi Tanaka ◽  
Hiroshi Kusunoki

2017 ◽  
Vol 84 ◽  
pp. 205-216 ◽  
Author(s):  
Violeta Chang ◽  
Laurent Heutte ◽  
Caroline Petitjean ◽  
Steffen Härtel ◽  
Nancy Hitschfeld

Author(s):  
Tongguang Ni ◽  
Yan Ding ◽  
Jing Xue ◽  
Kaijian Xia ◽  
Xiaoqing Gu ◽  
...  

Morphological classification of human sperm heads is a key technology for diagnosing male infertility. Due to its sparse representation and learning capability, dictionary learning has shown remarkable performance in human sperm head classification. To promote the discriminability of the classification model, a novel local constraint and label embedding multi-layer dictionary learning model called LCLM-MDL is proposed in this study. Based on the multi-layer dictionary learning framework, two dictionaries are built on the basis of Laplacian regularized constraint and label embedding term in each layer, and the two dictionaries are approximated to each other as much as possible, so as to well exploit the nonlinear structure and discriminability features of the morphology of human sperm heads. In addition, to promote the robustness of the model, the asymmetric Huber loss is adopted in the last layer of LCLM-MDL, which approximates the misclassification error by using the absolute error function. Finally, the experimental results on HuSHeM dataset demonstrate the validity of the LCLM-MDL.


Andrologia ◽  
2009 ◽  
Vol 25 (2) ◽  
pp. 67-70 ◽  
Author(s):  
M. C. Ou ◽  
H. T. Ng ◽  
B. N. Chiang ◽  
C. Y. Hong ◽  
C. T. Hsu

Zygote ◽  
2012 ◽  
Vol 21 (4) ◽  
pp. 330-336 ◽  
Author(s):  
Adriana Fortunato ◽  
Rita Leo ◽  
Francesca Liguori

SummaryThe integrity of sperm chromatin structure has proven to be of great importance for human fertility. In this study, we investigated whether sperm cryopreservation has an effect on nuclear DNA tertiary structure, (i.e. condensation), measured by aniline blue staining, in 103 male patients who required consultation for hypo-fertility. Sperm DNA damage was significantly higher in patients showing oligospermia and severe morphological abnormalities than in native sperm populations. Furthermore we observed that chromatin decondensation was related to the cryostorage technique and to the duration of storage. This increase in decondensation was highly significant (P < 0.01) immediately after cryopreservation and from 90 days of cryostorage onwards. The possible mechanisms involved in sperm chromatin cryoinjury and the need to incorporate new methods for testing sperm nuclear structure alteration into the routine spermiogram are discussed.


1995 ◽  
Vol 43 (4) ◽  
pp. 439-445 ◽  
Author(s):  
M Kalina ◽  
R Socher ◽  
R Rotem ◽  
Z Naor

We localized protein kinase C (PKC) in human sperm cells at the ultrastructural level by the immunogold technique. The sperm head PKC was localized in the acrosome, equatorial segment, and post-acrosomal region. In the flagellum, PKC was associated with the segmented column of the neck and was distributed along the mid, principal, and end pieces. Immunoreactive sites were observed in patches along the axoneme and outer dense fibers and were evenly distributed between these regions. Pre-absorption of the antibody used with rat brain PKC (alpha and beta) eliminated gold labeling of the sperm head but only reduced labeling of the sperm tail. The co-localization of PKC with various cytoskeletal and other structural elements suggests that the proteins involved are potential substrates for sperm PKC subspecies. The localization of PKC in distinct structures of the human sperm (head, neck, and tail) strongly suggests a role for this enzyme in various aspects of sperm physiology.


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