Analysis of protein thiol changes occurring during rat sperm epididymal maturation

Mark A Baker, Anita Weinberg, Louise Hetherington, Ana-Izabel S B Villaverde, Tony Velkov

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12 Citations (Scopus)

Abstract

The maturation of spermatozoa throughout the epididymal environment occurs in the complete absence of nuclear protein biosynthesis. As such, these cells rely heavily on posttranslational modifications of existing proteins in order to obtain the potential for fertilization. We have used an OxiCat approach to label both free and oxidized cysteine residues in rat sperm proteins and compared the ratio of reduced:oxidized peptides as these cells undergo epididymal transit. In all, 20 peptides, corresponding to 15 proteins, underwent a change in their redox status. Included in this list were A-kinase anchoring protein 4 and fatty acid-binding protein 9. Both of these proteins undergo intradisulfide bonding, leading to reduced solubility and, in the case of the latter, is likely to cause a loss of protein function. Interestingly, two glycolytic enzymes, hexokinase-1 and lactate dehydrogenase, also display increased cysteine oxidation during epididymal transit, which may be involved in the regulation of the enzyme activities.
Original languageEnglish
Article number11
Pages (from-to)1-10
Number of pages10
JournalBiology of Reproduction
Volume92
Issue number1
DOIs
Publication statusPublished - 2015

Keywords

  • Cysteine oxidation
  • Epididymis
  • OxiCat
  • Proteomics
  • Sperm maturation

Cite this

Baker, M. A., Weinberg, A., Hetherington, L., Villaverde, A-I. S. B., & Velkov, T. (2015). Analysis of protein thiol changes occurring during rat sperm epididymal maturation. Biology of Reproduction, 92(1), 1-10. [11]. https://doi.org/10.1095/biolreprod.114.123679