Investigation of CD133 and CD24 as candidate azoospermia markers and their relationship with spermatogenesis defects

Yükselten, Yunus; Aydos, Oya Sena; Sunguroğlu, Asuman; Aydos, Kaan

doi:10.1016/j.gene.2019.04.028

Cited by 13 publications

(21 citation statements)

References 56 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Moreover, PROM1 was localized in the spermatozoa and columnar epithelium of the epididymis (Figure 2E–H). Although the above results were from β‐gal staining and did not completely reflect the actual localization, the observations are in agreement with those of physiological studies that reported that PROM1 is expressed in sperm flagella 25,27 . Furthermore, our fertility tests revealed that the functional deletion of Prom1 resulted in complete infertility (Figure 3).…”

Section: Discussionsupporting

confidence: 90%

Prominin‐1 deletion results in spermatogenic impairment, sperm morphological defects, and infertility in mice

Matsukuma

Kobayashi

Oka

et al. 2023

Reprod Medicine & Biology

View full text Add to dashboard Cite

PurposeSpermatogenesis is a complex process orchestrated by several essential genes. Prominin‐1 (Prom1/PROM1) is a gene that is expressed in the testis but with a poorly understood role in spermatogenesis.MethodsWe used Prom1 knockout (Prom1 KO) mice to assess the role of Prom1 in spermatogenesis. To this end, we performed immunohistochemistry, immunofluorescence, western blotting, β‐galactosidase staining, and apoptosis assay. Additionally, we analyzed the morphology of sperm and assessed litter sizes.ResultsWe observed that PROM1 is localized to the dividing spermatocytes in seminiferous epithelial cells, sperm, and columnar epithelium in the epididymis. In the Prom1 KO testis, an aberrant increase in apoptotic cells and a decrease in proliferating seminiferous epithelial cells were observed. Cellular FLICE‐like inhibitory protein (c‐FLIP) and extracellular signal‐regulated kinase 1/2 (ERK1/2) expression were also significantly decreased in Prom1 KO testis. In addition, a significantly increased number of epididymal spermatozoa with abnormal morphology and less motility was found in Prom1 KO mice.ConclusionsPROM1 maintains spermatogenic cell proliferation and survival via c‐FLIP expression in the testis. It is also involved in sperm motility and fertilization potential. The mechanism underlying the effect of Prom1 on sperm morphology and motility remains to be identified.

show abstract

Section: Discussionsupporting

confidence: 90%

Prominin‐1 deletion results in spermatogenic impairment, sperm morphological defects, and infertility in mice

Matsukuma

Kobayashi

Oka

et al. 2023

Reprod Medicine & Biology

View full text Add to dashboard Cite

show abstract

“…52−54 It has been confirmed to be important in the spermatogenic processes governing male infertility and in the germ cell maturation. 50,55 Although N-glycans and glycoproteins are already known to be essential during spermatogenesis. The understanding of specific roles of glycans and glycoproteins involved in spermatogenesis mechanism is still limited.…”

Section: Specific Functions Of Glycosylation During Spermatogenesismentioning

confidence: 99%

“…Prominin-1 (PROM1), a glycoprotein found in the male reproductive system, has been correlated with the formation and maturation of spermatozoa. It is highly expressed in healthy commercially sourced Sertoli cells and is postulated to be associated with a spermatogenesis defect. , CD24 is an intensely glycosylated cell surface protein and has been reported to play a role in the regulation of cell proliferation and cell–cell interaction. − It has been confirmed to be important in the spermatogenic processes governing male infertility and in the germ cell maturation. , …”

Section: Role Of Glycosylation In Semen Functionsmentioning

confidence: 99%

Biological Functions and Large-Scale Profiling of Protein Glycosylation in Human Semen

et al. 2020

View full text Add to dashboard Cite

Glycosylation is one of the most important post-translational modifications of proteins and plays an essential role in spermatogenesis, maturation, extracellular quality control, capacitation, sperm−egg recognition, and final fertilization. Spermatozoa are synthesized in the testes inactively with a thick glycocalyx and passed through the epididymis for further modification by glycosylation, deglycosylation, and integration to reach maturation. Subsequently, sperm capacitation and further fertilization require redistribution of glycoconjugates and dramatic glycocalyx modification of the spermatozoa surface. Furthermore, glycoproteins and glycans in seminal plasma are functional in maintaining spermatozoa structure and stability. Therefore, aberrant glycosylation may cause alteration of semen function and even infertility. Currently, mass spectrometry-based technologies have allowed large-scale profiling of glycans and glycoproteins in human semen. Quantitative analysis of semen glycosylation has also indicated many involved glycoproteome issues in male infertility and the potential biomarkers for diagnosis of male infertility in clinical. This review summarizes the role of glycosylation during spermatozoa development, the large-scale profiling of glycome and glycoproteome in human semen, as well as the association of aberrant glycosylation with infertility.

show abstract

“…Although proteomics analysis of FFPE tissues could be challenging, we have used an extraction/digestion procedure that gives an almost identical number of proteins from fresh and FFPE tissues with excellent extraction of proteins from the whole isoelectric point range, good preservation of high-MW proteins and excellent technical reproducibility [29]. We discovered 795 differentially expressed proteins, from which three proteins (H1-6, RANBP1, TKTL2) discriminated quantitatively all three groups, 58 proteins had the power to quantitatively discriminate There is also one study that analyzed the expression and protein levels of two genes (CD133 and CD24) in testicular tissue, in four groups of patients: hypospermatogeneis (n = 20), MA (n = 20), SCO syndrome (n = 20), and OA (n = 10) [30]. The results showed that the expression of CD133 was significantly reduced in NOA, whereas the expression of CD24 did not show a statistically significant difference.…”

Section: Tissue Biomarkersmentioning

confidence: 99%

“…There is also one study that analyzed the expression and protein levels of two genes (CD133 and CD24) in testicular tissue, in four groups of patients: hypospermatogeneis ( n = 20), MA ( n = 20), SCO syndrome ( n = 20), and OA ( n = 10) [30]. The results showed that the expression of CD133 was significantly reduced in NOA, whereas the expression of CD24 did not show a statistically significant difference.…”

Section: Proteomics Biomarkers For Azoospermiamentioning

confidence: 99%

Proteomics of azoospermia: Towards the discovery of reliable markers for non‐invasive diagnosis

Rusevski

Plaseska‐Karanfilska

Davalieva

2022

Proteomics Clinical Apps

View full text Add to dashboard Cite

Purpose: Azoospermia, as the most severe form of male infertility, no longer indicates sterility due to modern medical advancements. The current diagnostic procedure based on testicular biopsy has several drawbacks which urges the development of novel, non-invasive diagnostic procedures based on biomarkers. In the last two decades, there have been many proteomics studies investigating potential azoospermia biomarkers. In this review, we aimed to provide a critical evaluation of these studies.Experimental Design: Published articles were gathered by systematic literature search using Pubmed, Science Direct, and Google Scholar databases until March 2022 and were further preselected to include only studies on human samples.Results: A detailed review of these studies encompassed the proteomics platforms, sources of material, proposed candidate biomarkers, and their potential diagnostic specificity and sensitivity. In addition, emphasis was put on the top, most identified and validated biomarker candidates and their potential for discriminating azoospermia types and subtypes as well as predicting sperm retrieval success rate.Conclusions: Proteomics research of azoospermia has laid the groundwork for the development of a more streamlined biomarker testing. The future research should be focused on well-designed studies including samples from all types/subtypes as well as further testing of the most promising biomarkers identified so far.

show abstract

Investigation of CD133 and CD24 as candidate azoospermia markers and their relationship with spermatogenesis defects

Cited by 13 publications

References 56 publications

Prominin‐1 deletion results in spermatogenic impairment, sperm morphological defects, and infertility in mice

Prominin‐1 deletion results in spermatogenic impairment, sperm morphological defects, and infertility in mice

Biological Functions and Large-Scale Profiling of Protein Glycosylation in Human Semen

Proteomics of azoospermia: Towards the discovery of reliable markers for non‐invasive diagnosis

Contact Info

Product

Resources

About