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Home / Equine Research Bank / Anim Reprod Sci / Thiol-disulfide proteins of stallion epididymal spermatozoa.
Animal reproduction science2013; 145(1-2); 29-39; doi: 10.1016/j.anireprosci.2013.12.007

Thiol-disulfide proteins of stallion epididymal spermatozoa.

Abstract: Thiol groups of cysteine residues represent redox centers involved in multiple biological functions. It has been postulated that changes in the redox status of mammalian epididymal spermatozoa contribute to the sperm maturation process. The present work shows the thiol-disulfide protein profile of stallion epididymal spermatozoa achieved by two-dimension electrophoresis and MALDI-TOF/TOF mass spectrometry of proteins labeled with a thiol-reactive fluorescent tag, monobromobimane. Our results have shown the formation of disulfide bonds in several sperm protein fractions during the epididymal maturation process. The majority of the oxidized thiol sperm proteins identified correspond to structural molecules of the flagellum (as the outer dense fiber-1 protein - ODF1), followed by glycolytic enzymes (as glyceraldehyde-3-phosphate dehydrogenase spermatogenic), antioxidant protectors (as glutathione S-transferase and phospholipid hydroperoxide glutathione peroxidase - PHGPx). The magnitude of the thiol oxidation differs between proteins, and was more drastic in polypeptides with molecular weights of up to 33kDa, identified as ODF1 and PHGPx. A kinase anchor protein, a voltage-dependent anion channel protein and a zona pellucida-binding protein were also found in the polypeptide samples that contained oxidized SH groups. These proteins may be modified or controlled by the mechanisms involved in the cysteine-redox changes, corroborating the belief that a correct degree of protein oxidation is required for the stabilization of sperm structure, protection against oxidative damage, induction of progressive sperm motility and fertilization.
Published by Elsevier B.V.
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Publication Date: 2013-12-31 PubMed ID: 24418125DOI: 10.1016/j.anireprosci.2013.12.007Google Scholar: Lookup
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  • Journal Article
  • Research Support
  • Non-U.S. Gov't

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The research explores the role of thiol-disulfide proteins in the maturation process of stallion sperm cells. By using advanced lab techniques, scientists identified several proteins that undergo oxidation, contributing to the stabilization and protection of sperm structure.

Objective of Study

  • This study aims to examine the redox status of thiol-disulfide proteins in stallion epididymal sperm and understand its role in the maturation and functioning of sperm cells.

Study Methods

  • The research uses two-dimensional electrophoresis and MALDI-TOF/TOF mass spectrometry to analyze proteins labeled with a thiol-reactive fluorescent tag, monobromobimane.
  • This approach allowed scientists to observe the formation of disulfide bonds in various sperm protein fractions during the epididymal maturation process.

Results and Findings

  • The majority of the oxidized thiol sperm proteins identified are related to the structural molecules of the flagellum, such as the outer dense fiber-1 protein (ODF1).
  • Glycolytic enzymes, as well as antioxidant protectors like glutathione S-transferase and phospholipid hydroperoxide glutathione peroxidase (PHGPx), were also identified among the oxidized proteins.
  • The level of thiol oxidation varied between proteins, with a more dramatic change in polypeptides with molecular weights of up to 33kDa, identified as ODF1 and PHGPx.
  • A kinase anchor protein, a voltage-dependent anion channel protein, and a zona pellucida-binding protein, which contained oxidized SH groups, were also identified. These proteins could be modified or controlled by cysteine-redox changes.

Implications of the Study

  • The findings support the idea that a correct degree of protein oxidation is needed for the stabilization of sperm structure, protection against oxidative damage, promotion of progressive sperm motility and fertility.
  • The research provides valuable insights into understanding the molecular mechanisms involved in sperm maturation and function, which could lead to advances in male infertility treatments in the future.

Cite This Article

APA
Dias GM, López ML, Ferreira AT, Chapeaurouge DA, Rodrigues A, Perales J, Retamal CA. (2013). Thiol-disulfide proteins of stallion epididymal spermatozoa. Anim Reprod Sci, 145(1-2), 29-39. https://doi.org/10.1016/j.anireprosci.2013.12.007

Publication

Animal reproduction science
ISSN: 1873-2232
NlmUniqueID: 7807205
Country: Netherlands
Language: English
Volume: 145
Issue: 1-2
Pages: 29-39
PII: S0378-4320(13)00362-X

Researcher Affiliations

Dias, G M
  • Laboratório de Biologia Celular e Tecidual, Centro de Biociências e Biotecnologia, UENF, Campos dos Goytacazes, RJ, Brazil.
López, M L
  • Laboratório de Biologia Celular e Tecidual, Centro de Biociências e Biotecnologia, UENF, Campos dos Goytacazes, RJ, Brazil. Electronic address: mlopez@uenf.br.
Ferreira, A T S
  • Laboratório de Toxinologia, Instituto Oswaldo Cruz, Fiocruz, Rio de Janeiro, Brazil.
Chapeaurouge, D A
  • Laboratório de Toxinologia, Instituto Oswaldo Cruz, Fiocruz, Rio de Janeiro, Brazil.
Rodrigues, A
  • Laboratório de Biologia Celular e Tecidual, Centro de Biociências e Biotecnologia, UENF, Campos dos Goytacazes, RJ, Brazil.
Perales, J
  • Laboratório de Toxinologia, Instituto Oswaldo Cruz, Fiocruz, Rio de Janeiro, Brazil.
Retamal, C A
  • Laboratório de Biologia Celular e Tecidual, Centro de Biociências e Biotecnologia, UENF, Campos dos Goytacazes, RJ, Brazil.

MeSH Terms

  • Animals
  • Disulfides / analysis
  • Electrophoresis, Gel, Two-Dimensional
  • Horses / metabolism
  • Male
  • Proteome / analysis
  • Proteome / metabolism
  • Seminal Plasma Proteins / analysis
  • Seminal Plasma Proteins / chemistry
  • Seminal Plasma Proteins / metabolism
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
  • Sperm Retrieval / veterinary
  • Spermatozoa / chemistry
  • Spermatozoa / metabolism
  • Sulfhydryl Compounds / analysis

Citations

This article has been cited 9 times.
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    doi: 10.3390/ijms23169143pubmed: 36012418google scholar: lookup
  2. Zmudzinska A, Bromke MA, Strzezek R, Zielinska M, Olejnik B, Mogielnicka-Brzozowska M. Proteomic Analysis of Intracellular and Membrane-Associated Fractions of Canine (Canis lupus familiaris) Epididymal Spermatozoa and Sperm Structure Separation. Animals (Basel) 2022 Mar 18;12(6).
    doi: 10.3390/ani12060772pubmed: 35327169google scholar: lookup
  3. Tedesco B, Cristofani R, Ferrari V, Cozzi M, Rusmini P, Casarotto E, Chierichetti M, Mina F, Galbiati M, Piccolella M, Crippa V, Poletti A. Insights on Human Small Heat Shock Proteins and Their Alterations in Diseases. Front Mol Biosci 2022;9:842149.
    doi: 10.3389/fmolb.2022.842149pubmed: 35281256google scholar: lookup
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    doi: 10.3390/ani11123487pubmed: 34944263google scholar: lookup
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    doi: 10.7554/eLife.55474pubmed: 32729827google scholar: lookup
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    doi: 10.1016/j.redox.2019.101130pubmed: 30737169google scholar: lookup
  7. Gervasi MG, Visconti PE. Molecular changes and signaling events occurring in spermatozoa during epididymal maturation. Andrology 2017 Mar;5(2):204-218.
    doi: 10.1111/andr.12320pubmed: 28297559google scholar: lookup
  8. Ren H, Wen X, He Q, Yi M, Dugarjaviin M, Bou G. Comparative Study on the Sperm Proteomes of Horses and Donkeys. Animals (Basel) 2024 Jul 31;14(15).
    doi: 10.3390/ani14152237pubmed: 39123763google scholar: lookup
  9. Wang H, Dou Q, Jeong KJ, Choi J, Gladyshev VN, Chung JJ. Redox regulation by TXNRD3 during epididymal maturation underlies capacitation-associated mitochondrial activity and sperm motility in mice. J Biol Chem 2022 Jul;298(7):102077.
    doi: 10.1016/j.jbc.2022.102077pubmed: 35643315google scholar: lookup
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