Explore chapters and articles related to this topic
Computational characterization and integrative analysis of proteins involved in spermatogenesis
Published in C. Yan Cheng, Spermatogenesis, 2018
Pranitha Jenardhanan, Manivel Panneerselvam, Premendu P. Mathur
In another study,55 Liu et al. analyzed the proteome expression pattern in patients affected with obesity. The authors found that 105 proteins shown less abundance while 22 were enriched in obesity-associated asthenozoospermic patients. They further analyzed the functionality of these proteins and found them involved in actin organization, flagellar assembly, vesicule traffic, signaling, metabolism, protein degradation, and stress resistance. They observed decreased expression of tektin, myosin, and septin, which are involved in acrosome formation and sperm motility, and therefore, their low abundance in obesity-associated asthenozoospermic patients renders the sperm immotile.55 Low expression of proteins involved in glucose metabolism, such as fructose-bisphosphatealdolase, glyceraldehyde-3-phosphate dehydrogenase, aldose reductase, glyoxylatereductase, cytochrome c oxidase, and pyruvate dehydrogenase, were also observed, which directly implies that their low expression affects energy metabolism in sperms. As well, for the first time they reported the association with the decreased expression of two novel proteins ERp57 and actin-related protein ACTRT2 with the progression of obesity-associated asthenozoospermia, which they proposed as the potential biomarkers for diagnosis and therapeutic intervention.
New knowledge about adenomyosis
Published in Carlos Simón, Linda C. Giudice, The Endometrial Factor, 2017
Giuseppe Benagiano, Beatrice Ermini, Marwan Habiba, Ivo Brosens
Using Illumina® HT-12 v3 Expression BeadChip gene expression analysis, Mehasseb et al. (79) reported that Wnt5a was consistently downregulated in both the inner and the outer myometrium during both the secretory and the proliferative phases of the cycles. The top five downregulated genes in the inner myometrium of adenomyotic uteri (compared with controls), in the proliferative phase, were ELMO/CED-12 domain containing 1 (ELMOD1), forkhead box L2 (FOXL2), SH3 domain GRB2-like 3 (SH3GL3), FLJ43329 protein (LOC401089), and transcription factor AP-2 gamma (activating enhancer binding protein 2 gamma) (TFAP2C). The top five upregulated genes in the inner myometrium of adenomyotic uteri (compared with controls), in the proliferative phase, were immunoglobulin superfamily, member 10 (IGSF10); Fms-related tyrosine kinase 1 (vascular endothelial growth factor/vascular permeability factor receptor) (FLT1); SH3 and cysteine-rich domain (STAC); p300/CBP-associated factor (PCAF); and parathyroid hormone 2 receptor (PTH2R). The top five downregulated genes in the inner myometrium of adenomyotic uteri (compared with controls), in the secretory phase, were solute carrier family 3 (cystine, dibasic, and neutral amino acid transporters, activator of cystine, dibasic, and neutral amino acid transport), member 1 (SLC3A1); keratin 86 (KRT86); forkhead box Q1 (FOXQ1); tektin 1 (TEKT1); and prominin 1 (PROM1). The top five upregulated genes in the inner myometrium of adenomyotic uteri (compared with controls), in the secretory phase, were gliomedin (GLDN), peripherin (PRPH), mohawk homeobox (MKX), peptidase inhibitor 16 (PI16), and myotilin (MYOT) (80).
Differentiation of neonate mouse spermatogonial stem cells on three-dimensional agar/polyvinyl alcohol nanofiber scaffold
Published in Systems Biology in Reproductive Medicine, 2020
Marzieh Ziloochi Kashani, Zohreh Bagher, Hamid Reza Asgari, Mohammad Najafi, Morteza Koruji, Fereshteh Mehraein
We next measured the expression levels of pre-meiotic (i.e., ID-4 and GFRα-1), meiotic (Synaptonemal complex protein 3, SYCP-3), and post-meiotic (i.e., Tektin 1, TEKT-1) markers in the cells that had been induced to differentiate by RA and BMP-4 (i.e., ‘Dif’ media) (Figures 5 and 6). As shown in Figure 5A, the expression of Id-4 was down-regulated ~2.8-fold, ~3.3-fold, ~22.3-fold, and ~40.3-fold in Dif/2D/–GF, Dif/3D/–GF, Dif/2D/+GF, and Dif/3D/+GF groups, respectively, when compared with the corresponding pre-differentiation groups (i.e., 2D/–GF, 3D/–GF, 2D/+GF, and 3D/+GF, respectively). There was no significant difference in terms of Id-4 gene expression between 2D and 3D cultures supplemented with or without growth factors after the differentiation induction (P = 0.073 for Dif/2D/–GF vs. Dif/3D/–GF, and P = 0.998 for Dif/2D/+GF vs. Dif/3D/+GF) (Figure 5A). However, the relative mRNA levels of ID-4 were found to be about ~75.4-fold lower in the Dif/2D/+GF group as compared to the Dif/2D/–GF group (P = 0.001). A comparable difference was detected between Dif/3D/–GF versus Dif/3D/+GF group. In fact, cells from Dif/3D/+GF group had approximately 69-fold lower levels of ID-4 transcript than cells from Dif/3D/–GF group (P = 0.018) (Figure 5A).