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Andrologia2020; 52(3); e13530; doi: 10.1111/and.13530

Structural modelling of the equine protein disulphide isomerase A1 and its quantification in the epididymis and seminal plasma.

Abstract: The protein disulphide isomerase A1 (PDIA1) is an important chaperone involved in protein quality control and redox regulation. Also, the ability of PDIA1 to bind to oestrogens suggests that it may play a role in epididymal maturation and male fertility. The goals of this study were to (a) verify the possible interaction between 17β-estradiol and equine PDIA1 using bioinformatics; (b) identify and quantify PDIA1 protein in equine cauda epididymis throughout peripuberty; and (c) determine whether the amounts of PDIA1 in equine seminal plasma and spermatozoa are associated with fertility. Using in silico analysis, we were able to predict the tertiary structure of equine PDIA1 and to demonstrate the interaction between 17β-estradiol and the putative binding site in domains b and b'. Colts under 24 months of age had lower relative amounts of PDIA1 in cauda epididymal fluid in comparison with older males (p < .01). No difference was observed in seminal plasma PDIA1 between fertile and subfertile stallions. Our study demonstrates that PDIA1 expression in the epididymis increases during peripuberty. However, in the adult stallion, its quantity in seminal plasma is not associated with fertility.
Publication Date: 2020-02-06 PubMed ID: 32026504DOI: 10.1111/and.13530Google Scholar: Lookup
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  • Journal Article

Summary

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This research investigates the role and presence of a specific protein, known as protein disulphide isomerase A1 (PDIA1), in male horse fertility. Using several methods including structural modelling, the team reveals how this protein interacts with certain hormones and how its quantity changes as the horses mature, although these changes appear not to impact adult fertility.

Research Scope

  • The study’s main focus is on the protein disulphide isomerase A1 (PDIA1) which is seen as an essential chaperone protein that assists in regulating protein quality and redox (oxidation and reduction) reactions in the body.
  • Given that PDIA1 can bind to oestrogens, the researchers hypothesize that it could contribute to male fertility by influencing epididymal maturation – the process through which sperm gain their motility and ability to fertilize an egg.
  • This study particularly investigates the interaction between 17β‐estradiol, an oestrogen steroid hormone, and PDIA1 in horses. It also tracks the quantity of PDIA1 in the cauda epididymis (the last part of the epididymis) during ‘peripuberty’ (the stage leading up to puberty), and in the seminal plasma and spermatozoa.

Research Methodology

  • The researchers used what is known as in silico analysis – computer simulations – to predict the tertiary structure (the three-dimensional shape) of PDIA1 in horses.
  • They also used these simulations to illustrate how 17β-estradiol might interact with PDIA1, specifically by binding to a predicted site in two of the protein’s domains.
  • The team observed and compared the amounts of PDIA1 in the epididymal fluid of colts (young male horses) under 24 months of age to those in older males.
  • Additionally, they analyzed quantities of PDIA1 in the seminal plasma of fertile and subfertile adult stallions to see if there was any correlation between the protein level and fertility status.

Major Findings

  • The researchers were successful in predicting the tertiary structure of equine PDIA1 and demonstrating the theoretical interaction between 17β-estradiol and the protein.
  • The study found that younger colts have less PDIA1 in their epididymal fluid than older males, indicating that the protein’s expression in the epididymis increases through peripuberty – supporting the idea that PDIA1 might play a role in sperm maturation.
  • However, no significant difference was observed in the amount of PDIA1 in the seminal plasma between fertile and subfertile stallions, suggesting that, in adult horses, the level of this protein is not associated with fertility.

Cite This Article

APA
van der Linden LS, Bustamante-Filho IC, Souza APB, Lopes TN, da Silva AFT, Tomé LM, Timmers LFMS, Dos Santos SI, Neves AP. (2020). Structural modelling of the equine protein disulphide isomerase A1 and its quantification in the epididymis and seminal plasma. Andrologia, 52(3), e13530. https://doi.org/10.1111/and.13530

Publication

ISSN: 1439-0272
NlmUniqueID: 0423506
Country: Germany
Language: English
Volume: 52
Issue: 3
Pages: e13530

Researcher Affiliations

van der Linden, Liana de Salles
  • Programa de Pós-graduação em Medicina Animal: Equinos, Universidade Federal do Rio Grande do Sul (UFRGS), Porto Alegre, Brazil.
Bustamante-Filho, Ivan Cunha
  • Laboratório de Biotecnologia, Universidade do Vale do Taquari - Univates, Lajeado, Brazil.
Souza, Ana Paula Binato
  • Laboratório de Biotecnologia, Universidade do Vale do Taquari - Univates, Lajeado, Brazil.
Lopes, Tayná Nauê
  • Laboratório de Biotecnologia, Universidade do Vale do Taquari - Univates, Lajeado, Brazil.
da Silva, Anna Flávia Tischer
  • Laboratório de Biotecnologia, Universidade do Vale do Taquari - Univates, Lajeado, Brazil.
Tomé, Luise Marcon
  • Laboratório de Biotecnologia, Universidade do Vale do Taquari - Univates, Lajeado, Brazil.
Timmers, Luis Fernando Macedo Saraiva
  • Laboratório de Biotecnologia, Universidade do Vale do Taquari - Univates, Lajeado, Brazil.
Dos Santos, Sérgio Ivan
  • Universidade Federal do Pampa (UNIPAMPA), Dom Pedrito, Brazil.
Neves, Adriana Pires
  • Programa de Pós-graduação em Medicina Animal: Equinos, Universidade Federal do Rio Grande do Sul (UFRGS), Porto Alegre, Brazil.
  • Universidade Federal do Pampa (UNIPAMPA), Dom Pedrito, Brazil.

MeSH Terms

  • Animals
  • Computational Biology
  • Epididymis / chemistry
  • Epididymis / metabolism
  • Estradiol / chemistry
  • Estradiol / metabolism
  • Fertility
  • Horses / physiology
  • Male
  • Molecular Docking Simulation
  • Protein Disulfide-Isomerases / analysis
  • Protein Disulfide-Isomerases / metabolism
  • Protein Disulfide-Isomerases / ultrastructure
  • Protein Structure, Tertiary
  • Semen / chemistry
  • Semen / metabolism
  • Sexual Maturation / physiology

Grant Funding

  • 16/2551-0000223-1 / Fundau00e7u00e3o de Amparo u00e0 Pesquisa do Estado do Rio Grande do Sul
  • 447251/2014-7 / Conselho Nacional de Desenvolvimento Cientu00edfico e Tecnolu00f3gico
  • 08/Reitoria/Univates/2016 / Fundau00e7u00e3o Vale do Taquari de Educau00e7u00e3o e Desenvolvimento Social (FUVATES)

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