Expressions of HSPA1L and HSPA9 are associated with poor sperm quality of low‐motility spermatozoa in fertile men

Abstract

Male infertility is a major reproductive health problem (Henkel et al., 2021;Liu et al., 2021). About 10-15% of couples worldwide suffer from reproductive problems, due to about equal male and female factors (Liu, Zhang, et al., 2016). Clinically, conventional diagnosis of male fertility is mainly relied on the routine laboratory analysis of semen quality (Kliesch, & Cooper, 2008). Male infertility usually manifests as defective sperm motility and morphology, resulting in diagnosis of asthenozoospermia or teratozoospermia, etc (Gunes, & Esteves, 2021). The detective thresholds of normal motility (40%) and morphology (4%) are far from full scores, indicating that ejaculated spermatozoa are heterogeneous population. However, the underlying causes and physiological resultant are still unclear.Spermatozoa are produced in the testis undergoing the processes of mitosis and meiosis. During their transition in epididymal tubule, they obtain the fertility potential including sperm progressive motility,

Comparative Proteome Analysis of Four Stages of Spermatogenesis in the Small-Spotted Catshark (Scyliorhinus canicula), Using High-Resolution NanoLC-ESI-MS/MS

“…These proteins are Hspa1a and Hspa1l, which are members of the heat shock protein family A (Hsp70), member 1A and member 1-like, respectively. As Hsp70 proteins are pleiotropic and involved in a wide range of cellular processes as molecular chaperones, it would be speculative to focus on their function here, however it has been reported that HSPA1L is localized in mouse spermatids and human spermatozoa, albeit with no clear explanation of its function. , …”

“…As Hsp70 proteins are pleiotropic and involved in a wide range of cellular processes as molecular chaperones, it would be speculative to focus on their function here, however it has been reported that HSPA1L is localized in mouse spermatids and human spermatozoa, albeit with no clear explanation of its function. 110,111 Post-transcriptional Regulation. During spermiogenesis, spermatids become transcriptionally inactive due to extensive remodelling of their nuclei by the replacement of histones with protamines.…”

Sperm Phosphoproteome: Unraveling Male Infertility

“…Other chaperones HSPs (HSPA5, HSPA9, and HSPA1L) were also found downregulated in asthenozoospermic men [41,43]. Additionally, in a recent study comparing proteomes of high or low-motility human spermatozoa, HSPA1L and HSPA9 were also significantly decreased in low-motility spermatozoa [49]. Conversely, in other comparative sperm proteomics studies, the expression level of chaperones did not indicate significant differences [37,[44][45][46].…”

“…Moreover, a reduction in sperm motility may be affected by other proteins, such as SEMG1 and SEMG2, which work as seminal plasma motility inhibitor proteins and are found up-regulated in asthenozoospermic men [37,38,46]. Another group of proteins with altered expression in spermatozoa with impaired motility involves different subunits of the proteasome such as PSMA3, PSMB3, PSMB4, PSMB5, PSMB6, PSMC2, PSMC6, and PSMD11 [37][38][39]42,45,49]. The proteasome plays a key role in the formation of condensed spermatozoa because it mediates the protein turnover of ubiquitinated proteins during spermatogenesis, when many proteins and organelles are degraded [55].…”

“…It is worth noting that SEMG1 and PSMB5 are also downregulated in a proteomic study that compares the proteomic profiles of human sperm samples that had or had not achieved a previous pregnancy via ART [56]. In addition, low levels of the major cytoskeleton components in spermatozoa flagella such as tektins (TEK1, TEK4, and TEK5) [39,41,42], outer dense fibers (ODF2) [41,43,49], or tubulin proteins (TUBB2C, TUBB2B, and TUBA3C) [39,43,49] are also associated with reduced sperm motility in comparative proteomics studies. On the other hand, altered levels of another protein that plays a role in the movement and structural organization of cells, such as CLU, have been found.…”