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Proteomic analysis of rabbit fresh and cryopreserved semen (seminal plasma)

ABSTRACT: Cryoinjury and protein changes are a consequence of cryopreservation and may have a negative impact on sperm quality regarding motility, viability and fertilizing ability. However, potential proteomic changes in rabbit semen throughout the cryopreservation process have never been investigated previously. The aim of the present study was to compare the whole proteome of fresh and cryopreserved rabbit extracellular fluid of semen. Comparative analysis and identification of proteins were performed using 2-dimensional difference in-gel electrophoresis (2D-DIGE) coupled with matrix-assisted laser desorption/ionization mass (MALDI TOF/TOF) spectrometry. We found that 28 proteins differed in abundance between fresh and frozen extracellular fluid.

INSTRUMENT(S): autoflex

ORGANISM(S): Oryctolagus Cuniculus (rabbit)

TISSUE(S): Seminal Plasma

SUBMITTER: Mariola Słowińska

LAB HEAD: Mariola Słowińska

PROVIDER: PXD034853 | Pride | 2022-10-13

REPOSITORIES: Pride

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Proteomic analysis of rabbit fresh and cryopreserved semen provides an important insight into molecular mechanisms of cryoinjuries to spermatozoa.

Rusco Giusy G Słowińska Mariola M Di Iorio Michele M Cerolini Silvia S Maffione Angela B AB Ciereszko Andrzej A Iaffaldano Nicolaia N

Theriogenology 20220805

Cryoinjury and protein changes are a consequence of cryopreservation and may have a negative impact on sperm quality regarding motility, viability and fertilizing ability. However, potential proteomic changes in rabbit semen throughout the cryopreservation process have never been previously investigated. The aim of the present study was to compare the whole proteome of fresh and cryopreserved rabbit semen (spermatozoa and extracellular fluid), to examine the effects of freeze-thawing on proteins ...[more]

PMID: 35964478

Similar Datasets

Proteomic analysis of rabbit fresh and cryopreserved semen (spermatozoa)

Project description:Cryoinjury and protein changes are a consequence of cryopreservation and may have a negative impact on sperm quality regarding motility, viability and fertilizing ability. However, potential proteomic changes in rabbit semen throughout the cryopreservation process have never been investigated previously. The aim of the present study was to compare the whole proteome of fresh and cryopreserved rabbit spermatozoa. Comparative analysis and identification of proteins were performed using 2-dimensional difference in-gel electrophoresis (2D-DIGE) coupled with matrix-assisted laser desorption/ionization mass (MALDI TOF/TOF) spectrometry. We found that 108 proteins differed in abundance in spermatozoa between fresh and frozen semen. Most of these proteins was involved in pathways related to energy metabolism and protein quality control under stress conditions, reproductive processes and mechanisms of cell death/survival regulation, resulting in a significant decrease of motility and viability of post-thawing rabbit sperm and its potential fertilizing ability.

2022-10-14 | PXD034832 | Pride

Proteomic characterization of fresh spermatozoa and supernatant after cryopreservation in relation to freezability of carp (Cyprinus carpio) semen

Project description:Our recent studies suggested that the freezability of carp semen is related to seminal plasma protein profiles. Here, we aimed to compare the spermatozoa proteomes of good (GF) and poor (PF) freezability semen of carp. To achieve this, we used two-dimensional difference in gel electrophoresis followed by MALDI-TOF/TOF mass spectrometry. The semen was classified as GF or PF based on sperm motility after freeze/thawing. We identified proteins enriched in spermatozoa of GF (22 proteins) and PF (18 proteins) semen. We also identified 12 proteins enriched in the supernatant after cryopreservation of PF semen. Good freezability is related to high concentrations of proteins involved in the maintenance of flagella structure, membrane fluidity, efficient control of Ca2+ and sperm motility, energy production, and antioxidative protection, which likely reflects the full maturation status of spermatozoa of GF semen. On the other hand poor freezability seems to be related to the presence of proteins identified as released in high quantities from cryopreserved sperm of PF. Thus, the identified proteins might be useful bioindicators of freezing resilience and could be used to screen carp males before cryopreservation, thus improve long-term sperm preservation in carp.

2018-03-23 | PXD008187 | Pride

Proteomic analysis of fresh and liquid stored turkey spermatozoa

Project description:The liquid storage of turkey semen without the loss of fertilizing ability is of practical interest to poultry industry. However, fertility rates from liquid stored turkey semen decline within a few hours. A clear cause of the decline in spermatozoa quality is unknown. Therefore, the purpose of the present study was to monitor dynamic of proteomic changes of spermatozoa during liquid storage at three time points (2, 24 and 48h) by 2-dimensional difference in-gel electrophoresis (2D-DIGE) coupled with a matrix-assisted laser desorption/ionization mass (MALDI TOF/TOF) spectrometry. A total of 57 protein spots were differentially expressed in fresh and stored spermatozoa; 42 spots were more- and 15 were less- abundant in spermatozoa after 48 h of semen storage. Most of the proteins that changed in response to liquid storage were related to i) flagellum dependent cell motility, ii) energy derivation by oxidation of organic compounds and iii) introduction of fertilization, suggesting complexity of the processes leading to decreases of stored semen quality.

2024-01-26 | PXD043050 | Pride

Application of Two-Dimensional Difference Gel Electrophoresis to Identify Protein Changes between Center, Margin, and Adjacent Non-Tumor Tissues Obtained from Non-Small-Cell Lung Cancer with Squamous Cell Carcinoma Subtype

Project description:Lung cancer is responsible for the most cancer-related mortality worldwide and the mechanism of its development is poorly understood. Proteomics has become a powerful tool offering vital knowledge related to cancer development. Using a two-dimensional difference gel electrophoresis (2D-DIGE) approach, we sought to compare tissue samples from non-small-cell lung cancer (NSCLC) patients, exactly squamous cell carcinoma (SCC), taken from the tumor center and tumor margin and control (adjacent non-tumor) tissues. We found and 21 spots representing 20 proteins differentiating center and margin. We found 111 differentially expressed protein spots representing 95 proteins; 84, 7, and 20 spots differed between the control and center and margin, control and center, and control and margin, respectively. Nine significant canonical pathways were identified, including hypoxia-inducible factor-1α signaling, thyroid hormone biosynthesis, and phagosome maturation. Several pathways related to disease and function were identified as related to cell death and survival, and several related to cancer, organismal injury, and abnormalities. Proteins differentiating the tumor center and tumor margin were linked to cancer invasion and progression, including cell migration, adhesion and invasion, cytoskeletal structure, protein folding, anaerobic metabolism, tumor angiogenesis, epithelialmesenchymal transition, epithelial adherens junctions, and inflammatory responses.

2022-05-20 | PXD032962 | Pride

Project description:Lung cancer is responsible for the most cancer-related mortality worldwide and the mechanism of its development is poorly understood. Proteomics has become a powerful tool offering vital knowledge related to cancer development. Using a two-dimensional difference gel electrophoresis (2D-DIGE) approach, we sought to compare tissue samples from non-small-cell lung cancer (NSCLC) patients, exactly adenocarcinoma (ADC), taken from the tumor center and tumor margin and control (adjacent non-tumor) tissues . We found 22 differentially abundant spots representing 17 proteins differentiating center and margin. Sixty eight proteins; represented by 79 spots :40, 20, and 19 spots differed between the control and center and margin, control and center, and control and margin, respectively. Twenty six significant canonical pathways were identified, including Rho signaling pathways, a semaphorin neuronal repulsive signaling pathway, and epithelial adherens junction signaling. Proteins differentiating the tumor center and tumor margin were linked to cancer invasion and progression, including cell migration, adhesion and invasion, cytoskeletal structure, protein folding, anaerobic metabolism, tumor angiogenesis, EMC transition, epithelial adherens junctions, and inflammatory responses.

2022-05-20 | PXD032736 | Pride

Hormonal stimulation of carp is accompanied with changes of seminal plasma and spermatozoa proteome

Project description:Hormonal stimulation in common carp is a routine practice to enhance sperm production and control gamete maturation. The mechanism regulating functional changes of semen composition upon hormone treatment is unknown at present. The aim of the study was to compare proteome of carp spermatozoa and seminal plasma from control (PBS, n=10) and hormonally stimulated males (D-Ala6,Pro9-NEt)-mGnRH+metoclopramide, n=10). Comparative proteomics based on two-dimensional differential in-gel electrophoresis was employed to quantitatively analyze the spermatozoa and seminal plasma proteins changed in abundance due to hormonal stimulation. Changes in phosphorylation and oxidation level of spermatozoa proteins were also analyzed. The proteomic results were validated by western blot, enzymatic assay and mRNA expression analysis.In total we identified 62 spots (38 up and 24 down regulated) corresponding to 48 proteins with differential abundance in spermatozoa and 36 spots (23 up and 13 down regulated) corresponding to 23 proteins differentially abundant in seminal plasma upon hormone treatment (P<0.05; fold change 1.2). The majority of spermatozoa proteins changed in abundance as well as phosphorylation and carbonylation level were involved in cillium assembly and organization, energy metabolism, protein folding, and signal transduction while differentially abundant seminal plasma proteins were associated with immune and stress response, lipid metabolism and tissue remodelling. Our results strongly suggest that hormonal treatment is not only related to hydration of testis but also induces modification of spermatozoa proteins and synthesis of seminal plasma proteins. ROS signaling and cAMP/PKA and calcium/calmodulin pathways are involved in sperm response to hormonal stimulation.

2021-04-20 | PXD011049 | Pride

Hypoxia induces Foxn1 and Mmp-9 expression in keratinocytes: proteomics analysis of mouse keratinocytes transiently activated by Foxn1

Project description:Recent studies have shown that transcription factor Foxn1 expressed in keratinocytes is involved in skin wound healing process, yet how Foxn1 functions remains largely unknown. Proteomic analysis using a two-dimensional differential gel electrophoresis (2D-DIGE) technique coupled with MALDI-TOF/TOF was used to analyze in vitro cultured keratinocytes transfected with adenoviral vector carrying Foxn1-GFP or GFP-alone (control). Sixty-six of sixty-nine protein spots differed in abundance between compared groups were identified.

2018-04-09 | PXD007843 | Pride

Distinct Serum Proteome Profiles Associated with Collagen-induced Arthritis, and Complete Freund’s Adjuvant-induced Inflammation in CD38-/- mice: the Discriminative Power of Protein Species or Proteoforms. Spot 269_Spot 500

Project description:Collagen-type-II-induced arthritis (CIA) is an autoimmune disease, which involves a complex host systemic response including inflammatory and autoimmune reactions. CIA in C57BL/6 mice resembles human rheumatoid arthritis (RA) in terms of its disease course, histological findings, and in its response to commonly used anti-arthritic drugs. In this study, the goal has been to identify proteins from serum that change in their abundance in CD38-KO versus WT mice which may reflect their distinct response to an antigen-challenge that induces the development of an autoimmune disease.CIA is milder in CD38-/- than in Wild-type (WT) mice. We analyzed the sera from CD38-/- versus WT mice either with arthritis (CIA+), with no arthritis (CIA-), or with inflammation (Complete Freund’s adjuvant (CFA)-treated mice). To decrease the dynamic concentration range of serum a combinatorial ligand library composed of hexapeptides was used (called ProteoMiner). ProteoMiner-equalized serum samples were then subjected to 2D-DiGE and MS-MALDI-TOF/TOF analyses to identify proteins that changed in their relative abundances. Multivariate analyses revealed that a multi-protein signature (n = 28) was able to discriminate CIA+ from CIA- mice, and WT from CD38-/- mice within each condition. Likewise, a distinct multi-protein signature (n = 16) was identified which differentiated CIA+CD38-/- mice from CIA+ WT mice, and lastly, a third multi-protein signature (n = 18) indicated that CD38-/- and WT mice could be segregated in response to CFA treatment This approach allows the identification of multiple protein species, or proteoforms of a given protein in a single analysis, and therefore, to focus the interest in fully characterize just the protein species that differ in abundance.

2015-07-17 | PXD002071 | Pride

Identification of multiple transferrin species in spleen from mice with collagen-induced arthritis which may reflect changes in transferrin glycosylation associated with the disease activity. Role of CD38. Set 2 of identified proteins (MALDI TOF/TOF UltrafleXtreme, Bruker).

Project description:Collagen type II-induced arthritis (CIA) is an autoimmune disease that is accompanied by a complex host systemic response, which includes inflammatory and autoimmune reactions. Since to develop CIA is required the injection of antigen in complete Freund’s adjuvant (CFA), which is a water-in-mineral-oil emulsion containing killed Mycobacteria, systemic response proteins related with inflammation can confound the detection or diagnosis of arthritis. CIA in CD38 deficient mice (CD38 KO) is milder than that in C57BL/6 (B6 WT) mice. Protein extracts from spleen were subjected to 2D-DiGE and MS-MALDI-TOF/TOF analysis to identify proteins that were differentially expressed in CD38 KO and B6 WT mice with arthritis, with inflammation, or non-immunized. Differential protein expression was validated by ELISA, or Western-blotting.

2015-12-10 | PXD002643 | Pride

2015-12-11 | PXD003183 | Pride

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