ArticleMolecular human reproduction2012
Alteration in the processing of the ACRBP/sp32 protein and sperm head/acrosome malformations in proprotein convertase 4 (PCSK4) null mice.
Article in Molecular human reproduction, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 40 citations in OpenAlex.
- Characterization of acrosin and acrosin binding protein as novel CRISP2 interacting proteins in boar spermatozoa.Andrology · 2023Article
- Mini Bioreactor Can SupportCell journal · 2022Article
- Mutation ofFrontiers in physiology · 2022Article
- Proteolysis in Reproduction: Lessons From Gene-Modified Organism Studies.Frontiers in endocrinology · 2022Review
- Mouse Models of Human Proprotein Convertase Insufficiency.Endocrine reviews · 2021Review
- Sperm acrosome overgrowth and infertility in mice lacking chromosome 18 pachytene piRNA.PLoS genetics · 2021Article
- Diverse functions of myosin VI in spermiogenesis.Histochemistry and cell biology · 2021Review
- ACRBP (Sp32) is involved in priming sperm for the acrosome reaction and the binding of sperm to the zona pellucida in a porcine model.PloS one · 2021Article
- Loss of myosin VI expression affects acrosome/acroplaxome complex morphology during mouse spermiogenesis†.Biology of reproduction · 2020Article
- Sperm Differentiation: The Role of Trafficking of Proteins.International journal of molecular sciences · 2020Review
- In vitro transplantation of spermatogonial stem cells isolated from human frozen-thawed testis tissue can induce spermatogenesis under 3-dimensional tissue culture conditions.Biological research · 2019Article
- Detection of sperm-reactive antibodies in wild sika deer and identification of the sperm antigens.The Journal of veterinary medical science · 2018Article
- iTRAQ-based analysis of sperm proteome from normozoospermic men achieving the rescue-ICSI pregnancy after the IVF failure.Clinical proteomics · 2018Article
- The control of male fertility by spermatid-specific factors: searching for contraceptive targets from spermatozoon's head to tail.Cell death & disease · 2016Review
- Biogenesis of sperm acrosome is regulated by pre-mRNA alternative splicing of Acrbp in the mouse.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- The Acrosomal Matrix.Advances in anatomy, embryology, and cell biology · 2016Review
- Genetics of the first seven proprotein convertase enzymes in health and disease.Current genomics · 2013Article
- Isolation and proteomic characterization of the mouse sperm acrosomal matrix.Molecular & cellular proteomics : MCP · 2012Article
- Proteomic signatures of infertile men with clinical varicocele and their validation studies reveal mitochondrial dysfunction leading to infertility.Asian journal of andrologyArticle
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Proprotein convertase 4 (PCSK4) is a member of a family of proprotein convertases that convert inactive precursor proteins into their mature and active forms. PCSK4 is expressed by testicular germ cells and localizes to the sperm acrosome, suggesting roles in fertilization. Mice lacking PCSK4 exhibit a profound fertility defect; yet, to date, few substrates for PCSK4 are known. In this study, two-dimensional differential in-gel electrophoresis analysis was carried out in order to identify proteins that are altered in spermatozoa from PCSK4 null mice. Herein, we report that the sperm fertilization molecule acrosin-binding protein (ACRBP)/sp32, which normally undergoes processing from a 58.5 kDa precursor to a 27.5 kDa mature form, is not proteolytically processed in PCSK4 null mice and thus may be a substrate for PCSK4. However, analysis of the ACRBP sequence did not show a strong consensus site for convertase cleavage, suggesting that ACRBP processing may require the activity of a yet unknown enzyme that itself may be a PCSK4 substrate. Further analysis of spermatozoa from the PCSK4 null mice showed that proacrosin did not undergo autoactivation, supporting a role for the mature form of ACRBP in the regulation of proacrosin conversion into different acrosin isoforms. Finally, examination of ACRBP localization revealed a previously undetected morphological defect in the head/acrosomes of spermatozoa from PCSK4 null mice. Taken together, these results demonstrate that the fertility defect in the PCSK4 null mice may in part be due to altered ACRBP protein processing as well as abnormalities in the sperm head/acrosome.
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