Human sperm chaperone HSPA2 distribution during in vitro capacitation

Huerta-Retamal, Natalia; Sáez‐Espinosa, Paula; Robles-Gómez, Laura; Avilés, Manuel; Romero, Alejandro; Aizpurúa, Jon; Gómez‐Torres, María José

doi:10.1016/j.jri.2020.103246

Cited by 12 publications

(15 citation statements)

References 52 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…To the best of our knowledge, this is the first time that HSPA2 has been localized in sperm with globozoospermia. Due to the importance of the chaperone during egg-sperm recognition, the HSPA2 location has been recently described during in vitro capacitation [40]. In our study, we identified positive labeling for this protein around the head in only 15% of sperm from a globozoospermic patient.…”

Section: Discussionsupporting

confidence: 46%

Immunofluorescence and High-Resolution Microscopy Reveal New Insights in Human Globozoospermia

Sáez‐Espinosa

Robles-Gómez

Ortega-López

et al. 2022

IJMS

Self Cite

View full text Add to dashboard Cite

Globozoospermia is a rare and severe type of teratozoospermia characterized by the presence of round-headed, acrosomeless spermatozoa with cytoskeleton defects. Current data support a negative relationship between globozoospermia and intracytoplasmic sperm injection (ICSI) outcomes, revealing the need to perform exhaustive studies on this type of sperm disorder. The aim of this study was to evaluate different structural, functional and molecular sperm biomarkers in total globozoospermia with proper embryo development after ICSI. The combination of field-emission scanning electron microscopy (FE-SEM) and transmission electron microscopy (TEM) allowed us to identify and correlate eight morphological patterns with both types of microscopy. Additionally, results reported a high percentage of coiled forms, with cytoplasmic retentions around the head and midpiece. By fluorescent microscopy, we detected that most of the sperm showed tubulin in the terminal piece of the flagellum and less than 1% displayed tyrosine phosphorylation in the flagellum. Moreover, we did not detect chaperone Heat shock-related 70 kDa protein 2 (HSPA2) in 85% of the cells. Overall, these findings provide new insights into globozoospermia, which could have potential implications in improving sperm selection methods for assisted reproductive techniques.

show abstract

Section: Discussionsupporting

confidence: 46%

Immunofluorescence and High-Resolution Microscopy Reveal New Insights in Human Globozoospermia

Sáez‐Espinosa

Robles-Gómez

Ortega-López

et al. 2022

IJMS

Self Cite

View full text Add to dashboard Cite

show abstract

“…Several studies have shown the importance of chaperone proteins in this process [ 75 , 76 , 77 , 78 , 79 , 80 ]. Among them, HSP70 has been the focus of several studies in different mammalian species [ 20 , 26 , 27 , 29 , 81 , 82 , 83 , 84 ]. However, these studies either referred to “HSP70”, neglecting the existence of multiple isoforms in this chaperone family, or focused only on one specific isoform.…”

Section: Discussionmentioning

confidence: 99%

“…However, these studies either referred to “HSP70”, neglecting the existence of multiple isoforms in this chaperone family, or focused only on one specific isoform. To the best of our knowledge, only the isoforms HSPA5 [ 82 ] and HSPA2 [ 20 , 26 , 27 , 29 ] were given specific attention in the context of sperm capacitation. In the present work, we studied the effect of capacitation on all the HSP70 isoforms identified in our human sperm proteome.…”

Section: Discussionmentioning

confidence: 99%

“…Next, we investigated the cellular localization of HSP70 by immunofluorescence on capacitated and non-capacitated spermatozoa. To the best of our knowledge, only the localization of HSPA2 and HSPA5 isoforms have been studied in a capacitation context [ 20 , 26 , 27 , 29 , 82 ]. While HSPA5 was found to have a constant localization, mainly at the level of the neck, following capacitation [ 82 , 89 , 90 ], controverted results were obtained for HSPA2.…”

Section: Discussionmentioning

confidence: 99%

“…Indeed, it was shown to be intracellular [ 20 , 27 ], on the plasma membrane surface [ 28 ], or intracellular and then relocated on the plasma membrane surface during capacitation [ 23 ]. In addition, the protein was described in different regions of the spermatozoa with variations according to the studies (head, acrosomial/ post-acrosomial region, neck, equatorial segment, tail, or connecting piece) and some authors stated that the protein distribution varied following capacitation while others showed the opposite [ 20 , 23 , 26 , 27 , 29 , 30 ]. In proteomic studies, HSPA2 abundance was found to vary following capacitation [ 31 ] or acrosome reaction [ 32 ].…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Targeted Analysis of HSP70 Isoforms in Human Spermatozoa in the Context of Capacitation and Motility

Grassi

Bisconti²,

Martinet³

et al. 2022

IJMS

View full text Add to dashboard Cite

HSP70s constitute a family of chaperones, some isoforms of which appear to play a role in sperm function. Notably, global proteomic studies analyzing proteins deregulated in asthenozoospermia, a main cause of male infertility characterized by low sperm motility, showed the dysregulation of some HSP70 isoforms. However, to date, no clear trend has been established since the variations in the abundance of HSP70 isoforms differed between studies. The HSPA2 isoform has been reported to play a key role in fertilization, but its dysregulation and possible relocation during capacitation, a maturation process making the spermatozoon capable of fertilizing an oocyte, is debated in the literature. The aim of the present study was to investigate the fate of all sperm HSP70 isoforms during capacitation and in relation to sperm motility. Using Multiple-Reaction Monitoring (MRM) mass spectrometry, we showed that the relative abundance of all detected isoforms was stable between non-capacitated and capacitated spermatozoa. Immunofluorescence using two different antibodies also demonstrated the stability of HSP70 isoform localization during capacitation. We also investigated spermatozoa purified from 20 sperm samples displaying various levels of total and progressive sperm motility. We showed that the abundance of HSP70 isoforms is not correlated to sperm total or progressive motility.

show abstract

Paternal factors in recurrent pregnancy loss: an insight through analysis of non-synonymous single-nucleotide polymorphism in human testis-specific chaperone HSPA2 gene

Mohanty

Jena

Kar

et al. 2021

Environ Sci Pollut Res

View full text Add to dashboard Cite

Human sperm chaperone HSPA2 distribution during in vitro capacitation

Cited by 12 publications

References 52 publications

Immunofluorescence and High-Resolution Microscopy Reveal New Insights in Human Globozoospermia

Immunofluorescence and High-Resolution Microscopy Reveal New Insights in Human Globozoospermia

Targeted Analysis of HSP70 Isoforms in Human Spermatozoa in the Context of Capacitation and Motility

Paternal factors in recurrent pregnancy loss: an insight through analysis of non-synonymous single-nucleotide polymorphism in human testis-specific chaperone HSPA2 gene

Contact Info

Product

Resources

About