Proteomic analysis of extracellular medium of cryopreserved carp (Cyprinus carpio L.) semen

Dietrich, Mariola A.; Arnold, Georg J.; Fröhlich, Thomas; Otte, Kerstin; Dietrich, G.J.; Ciereszko, Andrzej

doi:10.1016/j.cbd.2015.05.003

Cited by 20 publications

(23 citation statements)

References 40 publications

(4 reference statements)

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“…It is well known that the cryopreservation process results in a decrease of carp sperm motility parameters (Li et al, 2010a(Li et al, , 2013Dietrich et al, 2015;Horokhovatskyi et al, 2016) and viability (Watson, 2000;Li et al, 2010a). Our results indicate that the motility parameters including VCL, VSL, VAP, and LIN were already affected by effector dilution.…”

Section: Discussionmentioning

confidence: 48%

“…Carbonylation of proteins involved in fusion and stabilization of plasma membranes can result in disturbances of intracellular transport and in lower freezability of carp semen due to reduced membrane stabilization. Moreover, loss of sperm plasma membrane stability can lead to a leakage of the intracellular proteins of spermatozoa into the extracellular medium, which was demonstrated in our previous study (Dietrich et al, 2015).…”

Section: Discussionmentioning

confidence: 52%

“…Some of the carbonylated carp sperm proteins identified in the present study correspond to proteins previously identified as being sensitive to cryopreservation. Creatine kinase B-type, proteasome subunit β, and HSC70 were reported to be released from spermatozoa into the extracellular medium (Dietrich et al, 2015), whereas α-SNAP (as indicated above) decreased in abundance in sperm cells after freezing/thawing (Li et al, 2010b). This suggests that for some proteins the mechanism of cryoinjuries includes both their release from spermatozoa and their oxidative damage.…”

Section: Discussionmentioning

confidence: 91%

“…Sperm extracts of fresh, fresh-diluted, and cryopreserved semen were prepared as previously described in Dietrich et al (2015). Fresh, fresh-diluted and cryopreserved sperm protein extracts (n = 6 in each group), containing 150 µg of proteins, were derivatized with a 4-fold volume of DNPH solution or derivatization-control solution (Oxyblot Protein Oxidation Detection Kit, EMD Millipore).…”

Section: Detection Of Oxidized Proteins With Oxyblotsmentioning

confidence: 99%

“…However, it is well established that cryopreservation causes osmotic changes and oxidative damage that have sublethal or lethal effects on vertebrate spermatozoa (Ball, 2008) 1 resulting in reduced semen quality, including that of carp (Li et al, 2010a). Proteomic studies revealed cryopreservation-induced changes in spermatozoa protein profiles (Li et al, 2010b) and disturbances of plasma membrane permeability leading to leakage of sperm proteins into the extracellular medium (Dietrich et al, 2015).…”

Section: Introductionmentioning

confidence: 99%

See 4 more Smart Citations

Identification of oxidatively modified proteins due to cryopreservation of carp semen1

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et al. 2018

Journal of Animal Science

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During semen cryopreservation, spermatozoa are exposed to physical and chemical stressors that result in their functional and structural damage. Growing evidence suggests that most cryoinjuries result from oxidative stress accompanying sperm cryopreservation. Elevated amounts of reactive oxygen species (ROS) generated during cryopreservation can react with sperm macromolecules, including proteins. The goal of this study was to investigate the oxidative modifications (measured as carbonylation level changes) of carp spermatozoa proteins triggered by the cryopreservation process. Flow cytometry and computer-assisted sperm analysis were used to evaluate changes in viability, ROS level, and motility of spermatozoa. The spermatozoa proteins that were specifically carbonylated were identified and quantified by Western blotting, in conjunction with 2-dimensional electrophoresis (2D-oxyblot) and matrix-assisted laser desorption/ionization time-of-flight/time-of-flight mass spectrometry. Cryopreservation decreased spermatozoa motility (P < 0.01) and viability (P < 0.0001) and significantly increased (P < 0.0001) the number of ROS-positive cells. We identified 25 protein spots, corresponding to 19 proteins, with increases (P < 0.05) in carbonylation level due to freezing/thawing. The identified proteins are involved in motility, metabolism, calcium-ion binding, signal transduction, protein folding, and intracellular transport. The results suggest that carbonylation of flagellar proteins can result in motility disorders and may contribute to the reduced percentage of motile spermatozoa and disturbances in movement trajectory after sperm cryopreservation. Moreover, cryopreservation may contribute to impaired cellular respiration, ATP regeneration, disturbances of Ca2+ turnover, unfolding of cytoplasmic or histone proteins, disturbances of cell signaling and intracellular transport, and reduced membrane stability. Our results contribute to the knowledge concerning cryoinjury and to further development of a modified cryopreservation procedure aimed at minimizing oxidative damage of carp sperm proteins.

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Section: Discussionmentioning

confidence: 48%

Section: Discussionmentioning

confidence: 52%

Section: Discussionmentioning

confidence: 91%

Section: Detection Of Oxidized Proteins With Oxyblotsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Identification of oxidatively modified proteins due to cryopreservation of carp semen1

Mostek

Słowińska

Judycka

et al. 2018

Journal of Animal Science

Self Cite

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DIGE Analysis of Fish Tissues

Nynca

Dietrich

Ciereszko

2022

Methods in Molecular Biology

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DIGE Analysis of Fish Tissues

Nynca

Dietrich

Ciereszko

2017

Methods in Molecular Biology

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Two-dimensional difference gel electrophoresis (2D-DIGE) appears to be especially useful in quantitative approaches, allowing the co-separation of proteins of control samples from proteins of treatment/disease samples on the same gel, eliminating gel-to-gel variability. The principle of 2D-DIGE is to label proteins prior to isoelectric focusing and use three spectrally resolvable fluorescent dyes, allowing the independent labeling of control and experimental samples. This procedure makes it possible to reduce the number of gels in an experiment, allowing the accurate and reproducible quantification of multiple samples. 2D-DIGE has been found to be an excellent methodical tool in several areas of fish research, including environmental pollution and toxicology, the mechanisms of development and disorders, reproduction, nutrition, evolution, and ecology.

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Proteomic analysis of extracellular medium of cryopreserved carp (Cyprinus carpio L.) semen

Cited by 20 publications

References 40 publications

Identification of oxidatively modified proteins due to cryopreservation of carp semen1

Identification of oxidatively modified proteins due to cryopreservation of carp semen1

DIGE Analysis of Fish Tissues

DIGE Analysis of Fish Tissues

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