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Golgi apparatus regulation of differentiation
Published in C. Yan Cheng, Spermatogenesis, 2018
Louis Hermo, Regiana L. Oliveira, Charles E. Smith, Catherine E. Au, John J. M. Bergeron
HSP70.2 (HspA2) is part of the heat shock protein (HSP)70 family of molecular chaperones needed to stabilize otherwise labile proteins.123 The HSP70 family of chaperones usually masks exposed hydrophobic residues on client proteins, preventing their aggregation and insolubility. Our recent study51 represents the first localization of the germ cell cytosolic chaperone HSP70.2 to the acrosome and Golgi apparatus of steps 1–7 spermatids (Figure 1.13d), which we found to be antibody-specific.124 As for its somatic counterpart Hsc70,125 HSP70.2 may participate in clathrin-coated vesicle trafficking known to be prominent during acrosome formation.26
The Importance of Sperm Surface Markers in Reproductive Success: Sperm Hyaluronan Binding
Published in Nicolás Garrido, Rocio Rivera, A Practical Guide to Sperm Analysis, 2017
Although a highly predictive test for fertilization success remains to be developed, the potential use of HspA2 as a positive biomarker of fertilization success has been widely discussed.26,27 Bromfield et al.28 recently showed angiotensin-converting enzyme (ACE) and protein disulfide isomerase A6 (PDIA6) as potential HspA2-interacting proteins. The surface expression of PDIA6, but not of ACE, was shown to be dynamically regulated during sperm capacitation and, like that of previously characterized HspA2-interacting proteins, this surface expression proved vulnerable to oxidative stress.28
Mapping the human sperm proteome – novel insights into reproductive research
Published in Expert Review of Proteomics, 2023
Mika Alexia Miyazaki, Raquel Lozano Guilharducci, Paula Intasqui, Ricardo Pimenta Bertolla
In addition, heat shock protein family A (HSP70) member 2 and member 9 (HSPA2 and HSPA9) were shown to be deregulated. In previous studies with HSPA2-null mice, there were several germ cells and spermatogenesis cells getting into apoptosis, when compared to wild-type mice, leading these animals to be infertile [59,60]. These HSP70 family of proteins participates in mitochondrial protein folding and energy generation. Once again, results converge to energy metabolism alterations, but, in this case, the altered protein levels were from post-glycolytic proteins, what confirms the crucial role of mitochondria for sperm motility [52,54].
Assessing the potential of HSPA2 and ADAM2 as two biomarkers for human sperm selection
Published in Human Fertility, 2020
Mahnaz Heidari, Sara Darbani, Mahsa Darbandi, Niknam Lakpour, Zohreh Fathi, Amir Hasan Zarnani, Hodjat Zeraati, Mohammad Mehdi Akhondi, Mohammad Reza Sadeghi
Selecting sperm based on surface functional biomarkers is thought to be one such innovation. Sperm membrane glycoproteins have a direct role in sperm-egg adhesion and fusion during the fertilization process (Bronson, Fusi, Calzi, Doldi, & Ferrari, 1999; Wolfsberg et al., 1993). The two membrane proteins on the surface of sperm involved in fertilization of oocytes are the heat shock protein A2 (HSPA2) and ADAM metallopeptidase domain 2 (ADAM2) (Redgrove et al., 2012; Yuan, Primakoff, & Myles, 1997). HSPA2, as a molecular chaperone, is a member of the HSP family. It is a testis-specific gene expressed during spermatogenesis and is an index of sperm maturity (Eddy, 1999; Scieglinska & Krawczyk, 2015). Repairing sperm DNA breaks, replacement of protamine during nuclear compaction and removing the cytoplasm during the final phases of sperm maturation are the specific functions that are proposed for HSPA2 in human testis (Dix et al., 1996; Engh, Clausen, Scholberg, Tollefsrud, & Purvis, 1992; Gomez et al., 1996; Govin et al., 2006; Motiei, Tavalaee, Rabiei, Hajihosseini, & Nasr-Esfahani, 2013; Nixon, Bromfield, Cui, & De Iuliis, 2017). It was reported that complete absence of HSPA2 is associated with spermatogenesis being blocked at the primary spermatogenesis phase, which leads to azoospermia (Tian et al., 2014). ADAM2 as a heterodimeric glycoprotein, belonging to the disintegrin and metalloproteinase (ADAMs) family. Molecules containing ADAMs domains, have important roles in cell adhesion, migration, proteolysis and signalling that are usually distributed over the entire head of testicular sperm (Choi et al., 2016; Wolfsberg et al., 1995; Wolfsberg & White, 1996). However, once these sperm pass through the epididymis during their maturation, the protein migrates to plasma membrane of the posterior region of the sperm head (Sullivan, 2016).