Ready for the journey: a comparative proteome profiling of porcine cauda epididymal fluid and spermatozoa

Weber, Augusto Ferreira; Argenti, Laura Espíndola; Souza, Ana Paula Binato de; Santi, Lucélia; Beys‐da‐Silva, Walter O.; Bustamante‐Filho, Ivan Cunha

doi:10.1007/s00441-019-03080-0

Cited by 12 publications

(11 citation statements)

References 58 publications

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“…Scan functions of the mass spectrometer and HPLC solvent gradients were controlled through the XCalibur data system. All MS/MS spectra were analyzed as proposed by Santi et al (2014) and Weber et al (2019). Briefly, protein identification and quantification analysis were done with Integrated Proteomics Pipeline (http://www.integratedproteomics.com/).…”

Section: Methodsmentioning

confidence: 99%

Changes in porcine cauda epididymal fluid proteome by disrupting the HPT axis: Unveiling potential mechanisms of male infertility

Souza

Lopes

Silva

et al. 2020

Molecular Reproduction Devel

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Male infertility or subfertility is frequently associated with disruption of the hypothalamic-pituitary-testis axis events, like secondary hypogonadism. However, little is known how this condition affects the proteomic composition of the epididymal fluid. In the present study, we evaluated the proteomic changes in the cauda epididymal fluid (CEF) in a swine model of secondary hypogonadism induced by anti-GnRH immunization using multidimensional protein identification technology. Seven hundred and eighteen proteins were identified in both GnRH-immunized and control groups. GnRH immunization doubled the number of proteins in the CEF, with 417 proteins being found exclusively in samples from GnRH-immunized boars. CEF from GnRH-immunized boars presented an increase in the number of proteins related to cellular and metabolic processes, with affinity to organic cyclic compounds, small molecules, and heterocyclic compounds, as well changed the enzymatic profile of the CEF. Also, a significant increase in the number of proteins associated to the ubiquitin-proteasome system was identified in CEF from GnRH-immunized animals. These results bring strong evidence of the impact of secondary hypogonadism on the epididymal environment, which is responsible for sperm maturation and storage prior ejaculation. Finally, the differently expressed proteins in the CEF are putative seminal biomarkers for testicular and epididymal disorders caused by secondary hypogonadism.

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Section: Methodsmentioning

confidence: 99%

Changes in porcine cauda epididymal fluid proteome by disrupting the HPT axis: Unveiling potential mechanisms of male infertility

Souza

Lopes

Silva

et al. 2020

Molecular Reproduction Devel

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“…CD44 has been localised in bovine cumulus-oocyte complexes (Schoenfelder & Einspanier, 2003) and pre-implantation embryos (Furnus et al, 2003) as well as in human (Bains et al, 2002), porcine (Weber et al, 2020) and rat spermatozoa (Borg & Holland, 2008). motif is involved with the interaction between αVβ3 but not α5β1.…”

Section: F I G U R Ementioning

confidence: 99%

Bovine seminal plasma osteopontin: Structural modelling, recombinant expression and its relationship with semen quality

et al. 2020

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“…Legumain was first observed to be located in the endosome/lysosome, 53 in the nucleus, 54,55 on the surface of cells, 56 and in the ECM 57 . In reproductive tissues, legumain can be found in the testis, 53 epididymal fluid, 58 and seminal plasma 59,60 in different species. Similar to cathepsin B, legumain is involved in many physiological and pathological processes, 61 such as antigen processing, 62 cell migration, 56 and proliferation 55 .…”

Section: Discussionmentioning

confidence: 99%

“…As previously mentioned, proteases such as cathepsins and legumain are key proteins in a myriad of physiological pathways involving the activation of MMPs, important constituents of epididymal 58 and ejaculated semen 75 . These proteins belong to a group of proteolytic zinc‐dependent enzymes (endopeptidases), which, alongside their inhibitors (tissue inhibitors of metalloproteinases, TIMPs), have a role in remodeling the extracellular matrix.…”

Section: Discussionmentioning

confidence: 99%

Differential seminal plasma proteome signatures of boars with high and low resistance to hypothermic semen preservation at 5°C

et al. 2020

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Background Hypothermic storage at 5°C has been investigated as an alternative to promote the prudent use of antibiotics for boar artificial insemination doses. However, this temperature is challenging for some ejaculates or boars. Objective The present study aimed to identify putative biomarkers for semen resistance to hypothermic storage at 5°C by comparing the seminal plasma proteomes of boars with high and low seminal resistance to preservation at 5°C. Materials and methods From an initial group of 34 boars, 15 were selected based on the following criteria: ejaculate with ≤20% abnormal spermatozoa and at least 70% progressive motility at 120 hours of storage at 17°C. Then, based on the response to semen hypothermic storage at 5°C, boars were classified into two categories: high resistance—progressive motility of >75% in the three collections (n = 3); and low resistance—progressive motility of <75% in the three collections (n = 3). Seminal plasma proteins were analyzed in pools, and differential proteomics was performed using Multidimensional Protein Identification Technology. Results Progressive motility was lower at 120 hours of storage in low resistance, compared to high resistance boars (P < .05). Acrosome and plasma membrane integrity were not affected by the boar category, storage time, or their interaction (P ≥ .104). Sixty‐five proteins were considered for differential proteomics. Among the differentially expressed and exclusive proteins, the identification of proteins such cathepsin B, legumain, and cystatin B suggests significant changes in key enzymes (eg, metalloproteinases) involved in spermatogenesis, sperm integrity, and fertilizing potential. Discussion and Conclusion Differences in the seminal plasma suggest that proteins involved in the proteolytic activation of metalloproteinases and proteins related to immune response modulation could disrupt key cellular pathways during spermatogenesis and epididymal maturation, resulting in altered resistance to chilling injury. Further in vivo studies focusing on the immunological crosstalk between epithelial cells and gametes might explain how the immune regulators influence sperm resistance to hipothermic storage.

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Ready for the journey: a comparative proteome profiling of porcine cauda epididymal fluid and spermatozoa

Cited by 12 publications

References 58 publications

Changes in porcine cauda epididymal fluid proteome by disrupting the HPT axis: Unveiling potential mechanisms of male infertility

Changes in porcine cauda epididymal fluid proteome by disrupting the HPT axis: Unveiling potential mechanisms of male infertility

Bovine seminal plasma osteopontin: Structural modelling, recombinant expression and its relationship with semen quality

Differential seminal plasma proteome signatures of boars with high and low resistance to hypothermic semen preservation at 5°C

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