AI Article Synopsis

  • DNA oxidative damage significantly affects cell health and is linked to various human diseases, particularly impacting male gametes due to their sensitivity to damaged DNA.
  • In a study, researchers examined how excess copper and chromium in semen alters protamines/histones ratios and DNA binding modes in sperm cells from healthy males.
  • The findings suggest that sperm nuclear basic proteins contribute to oxidative DNA damage by facilitating the Fenton reaction, which may enhance the presence of damaging metals near DNA, providing new insights into the mechanisms of oxidative damage in human sperm.

Article Abstract

DNA oxidative damage is one of the main concerns being implicated in severe cell alterations, promoting different types of human disorders and diseases. For their characteristics, male gametes are the most sensitive cells to the accumulation of damaged DNA. We have recently reported the relevance of arginine residues in the Cu(II)-induced DNA breakage of sperm H1 histones. In this work, we have extended our previous findings investigating the involvement of human sperm nuclear basic proteins on DNA oxidative damage in healthy males presenting copper and chromium excess in their semen. We found in 84% of those males an altered protamines/histones ratio and a different DNA binding mode even for those presenting a canonical protamines/histones ratio. Furthermore, all the sperm nuclear basic proteins from these samples that resulted were involved in DNA oxidative damage, supporting the idea that these proteins could promote the Fenton reaction in DNA proximity by increasing the availability of these metals near the binding surface of DNA. In conclusion, our study reveals a new and unexpected behavior of human sperm nuclear basic proteins in oxidative DNA damage, providing new insights for understanding the mechanisms related to processes in which oxidative DNA damage is implicated.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7349829PMC
http://dx.doi.org/10.3390/ijms21124198DOI Listing

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