dc.contributor.author |
Jakop, Ulrike
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dc.contributor.author |
Muller, Karin
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dc.contributor.author |
Muller, Peter
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dc.contributor.author |
Neuhauser, Stefanie
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dc.contributor.author |
Rodrıguez, Isabel Callealta
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dc.contributor.author |
Grunewald, Sonja
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dc.contributor.author |
Schiller, Jurgen
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dc.contributor.author |
Engel, Kathrin M.
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dc.date.accessioned |
2022-11-07T11:45:05Z |
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dc.date.available |
2022-11-07T11:45:05Z |
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dc.date.issued |
2022-03-08 |
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dc.description |
SUPPLEMENTARY MATERIAL: S1 Fig. ESI spectra of lysophosphatidylcholine (LPC) fractions from boar, bull, stallion, lion and human samples. |
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dc.description |
S2 Fig. ESI spectra of sphingomyelin (SM) fractions from boar, bull, stallion, lion and human samples.
Lipid extracts were separated on a normal phase high performance thin-layer chromatography (HPTLC) plate with chloroform/ethanol/water/triethylamine (30:35:7:35, by vol.) as the mobile phase. Plates were air-dried and stained with primuline (Direct Yellow 59, Sigma-Aldrich, Taufkirchen, Germany) (50 mg/l dissolved in acetone/water 80:20, by vol.). Lipids were made visible under UV light and marked with a pencil. SM fractions were directly analyzed by coupling a TLC plate reader to an ESI mass spectrometer. Mass spectra were recorded in the positive ion mode. For further details on ESI-IT MS see main text. For peak assignment, please see S2 Table.
https://doi.org/10.1371/journal.pone.0264675.s002 |
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dc.description |
S3 Fig. ESI spectra of phosphatidylcholine (PC) fractions from boar, bull, stallion, lion and human samples.
Lipid extracts were separated on a normal phase high performance thin-layer chromatography (HPTLC) plate with chloroform/ethanol/water/triethylamine (30:35:7:35, by vol.) as the mobile phase. Plates were air-dried and stained with primuline (Direct Yellow 59, Sigma-Aldrich, Taufkirchen, Germany) (50 mg/l dissolved in acetone/water 80:20, by vol.). Lipids were made visible under UV light and marked with a pencil. PC fractions were directly analyzed by coupling a TLC plate reader to an ESI mass spectrometer. Mass spectra were recorded in the positive ion mode. For further details on ESI-IT MS see main text. For peak assignment, please see S3 Table.
https://doi.org/10.1371/journal.pone.0264675.s003 |
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dc.description |
S4 Fig. ESI spectra of phosphatidylinositol (PI) fractions from boar, bull, stallion and human lipid samples.
Lipid extracts were separated on a normal phase high performance thin-layer chromatography (HPTLC) plate with chloroform/ethanol/water/triethylamine (30:35:7:35, by vol.) as the mobile phase. Plates were air-dried and stained with primuline (Direct Yellow 59, Sigma-Aldrich, Taufkirchen, Germany) (50 mg/l dissolved in acetone/water 80:20, by vol.). Lipids were made visible under UV light and marked with a pencil. PI fractions were directly analyzed by coupling a TLC plate reader to an ESI mass spectrometer. Mass spectra were recorded in the negative ion mode. For further details on ESI-IT MS see main text. For peak assignment, please see S4 Table.
https://doi.org/10.1371/journal.pone.0264675.s004 |
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dc.description |
S5 Fig. ESI spectra of phosphatidylethanolamine (PE) fractions from boar, bull and stallion samples.
Lipid extracts were separated on a normal phase high performance thin-layer chromatography (HPTLC) plate with chloroform/ethanol/water/triethylamine (30:35:7:35, by vol.) as the mobile phase. Plates were air-dried and stained with primuline (Direct Yellow 59, Sigma-Aldrich, Taufkirchen, Germany) (50 mg/l dissolved in acetone/water 80:20, by vol.). Lipids were made visible under UV light and marked with a pencil. PE fractions were directly analyzed by coupling a TLC plate reader to an ESI mass spectrometer. Mass spectra were recorded in the negative ion mode. For further details on ESI-IT MS see main text. For peak assignment, please see S5 Table.
https://doi.org/10.1371/journal.pone.0264675.s005 |
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dc.description |
S6 Fig. ESI spectra of phosphatidylethanolamine (PE) fractions from lion and human samples.
Lipid extracts were separated on a normal phase high performance thin-layer chromatography (HPTLC) plate with chloroform/ethanol/water/triethylamine (30:35:7:35, by vol.) as the mobile phase. Plates were air-dried and stained with primuline (Direct Yellow 59, Sigma-Aldrich, Taufkirchen, Germany) (50 mg/l dissolved in acetone/water 80:20, by vol.). Lipids were made visible under UV light and marked with a pencil. PE fractions were directly analyzed by coupling a TLC plate reader to an ESI mass spectrometer. Mass spectra were recorded in the negative ion mode. For further details on ESI-IT MS see main text. For peak assignment, please see S5 Table.
https://doi.org/10.1371/journal.pone.0264675.s006 |
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dc.description |
S7 Fig. Hydrolysis of selected seminal fluid samples over time.
The plots of hydrolysis measurements from boar and stallion seminal fluid were fitted by a linear curve (f(x) = a + b×x) and the plots from bull, lion and human were fitted by an exponential growth to a maximum (f(x) = a×e-b×x). Due to these different courses of the hydrolysis reaction between the species, the absolute hydrolysis at a given time point (10 min) was used to compare the mean values of the investigated individuals between the species (see Table 2 of the main text).
https://doi.org/10.1371/journal.pone.0264675.s007 |
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dc.description |
S8 Fig. Effect of artificial LPC on boar sperm.
Beltsville Thawing Solution (BTS, Minitüb GmbH)-diluted boar semen (20 × 106 sperm/ml) was mixed with 20 μM lysophosphatidylcholine (LPC 16:0, Avanti Polar Lipids®, No 855675C). After incubation at 38°C for 30 min, the ratios of total motility (blank boxes) and sperm with an intact acrosome (striped boxes) were analyzed. The lipid extract of washed sperm of this experiment was analyzed by MALDI-TOF MS and the ratio of LPC to total GPC was calculated (for details see Material and Methods of the main text). Incubation with 20 μM LPC led to 2.4 ± 3.6% inserted LPC in sperm cell membranes. Significant differences in total motility and the percentage of sperm with an intact acrosome between the incubation with 20 μM LPC and controls are marked by asterisks (P = 0.006 and 0.003, respectively, Wilcoxon signed-rank test, n = 11).
https://doi.org/10.1371/journal.pone.0264675.s008 |
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dc.description |
S9 Fig. Original TLC pictures.
Lipid extracts were separated on normal phase high performance thin-layer chromatography (HPTLC) plates with chloroform/ethanol/water/triethylamine (30:35:7:35, by vol.) as the mobile phase. Plates were air-dried and stained with primuline (Direct Yellow 59, Sigma-Aldrich, Taufkirchen, Germany) (50 mg/l dissolved in acetone/water 80:20, by vol.). BP–blood plasma, SF–seminal fluid, st.–lipid standard mixture made of LPC16:0, SM16:0, PC16:0/18:1, PA 16:0/18:1, PI 16:1/18:1, PE 16:0/18:1, PG 16:0/18:1 (bottom up).
https://doi.org/10.1371/journal.pone.0264675.s009 |
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dc.description |
S1 Table. Assignment of signals detected in ESI spectra from lysophosphatidylcholine (LPC) spots.
https://doi.org/10.1371/journal.pone.0264675.s010 |
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dc.description |
S2 Table. Assignment of signals detected in ESI spectra from sphingomyelin (SM) spots.
n.a.—not assigned.
https://doi.org/10.1371/journal.pone.0264675.s011 |
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dc.description |
S3 Table. Assignment of signals detected in ESI spectra from phosphatidylcholine (PC) spots.
https://doi.org/10.1371/journal.pone.0264675.s012 |
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dc.description |
S4 Table. Assignment of signals detected in ESI spectra from phosphatidylinositol (PI) spots.
https://doi.org/10.1371/journal.pone.0264675.s013 |
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dc.description |
S5 Table. Assignment of signals detected in ESI spectra from phosphatidylethanolamine (PE) spots.
https://doi.org/10.1371/journal.pone.0264675.s014 |
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dc.description.abstract |
On their way to the oocyte, sperm cells are subjected to oxidative stress, which may trigger
the oxidation of phospholipids (PL). Applying MALDI-TOF MS, HPTLC and ESI-IT MS, we
comparatively analyzed the PL compositions of semen and blood of species differing in their
reproductive systems and types of nutrition (bull, boar, stallion, lion and man) with regard to
the sensitivity to oxidation as well as the accumulation of harmful lyso-PL (LPL), transient
products of lipid oxidation. In addition, the protective capacity of seminal fluid (SF) was also
examined. The PL composition of erythrocytes and blood plasma is similar across the species, while pronounced differences exist for sperm and SF. Since the blood function is
largely conserved across mammalian species, but the reproductive systems may vary in
many aspects, the obtained results suggest that the PL composition is not determined by
the type of nutrition, but by the relatedness of species and by functional requirements of cell
membranes such as fluidity. Sperm motion and fertilization of oocytes require a rather flexible membrane, which is accomplished by significant moieties of unsaturated fatty acyl residues in sperm lipids of most species, but implies a higher risk of oxidation. Due to a high
content of plasmalogens (alkenyl ether lipids), bull sperm are most susceptible to oxidation.
Our data indicate that bull sperm possess the most effective protective power in SF. Obviously, a co-evolution of PL composition and protective mechanisms has occurred in semen
and is related to the reproductive characteristics. Although the protective capacity in human
SF seems well developed, we recorded the most pronounced individual contaminations with
LPL in human semen. Probably, massive oxidative challenges related to lifestyle factors
interfere with natural conditions. |
en_US |
dc.description.department |
Veterinary Tropical Diseases |
en_US |
dc.description.librarian |
dm2022 |
en_US |
dc.description.sponsorship |
The German Research Council. |
en_US |
dc.description.uri |
http://www.plosone.org |
en_US |
dc.identifier.citation |
Jakop, U., Müller, K., Müller, P., Neuhauser, S., Rodríguez, I.C., Grunewald, S. et al. (2022) Seminal lipid profiling and antioxidant capacity: A
species comparison. PLoS One 17(3): e0264675.
https://doi.org/10.1371/journal.pone.0264675. |
en_US |
dc.identifier.issn |
1932-6203 (online) |
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dc.identifier.other |
10.1371/journal.pone.0264675 |
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dc.identifier.uri |
https://repository.up.ac.za/handle/2263/88172 |
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dc.language.iso |
en |
en_US |
dc.publisher |
Public Library of Science |
en_US |
dc.rights |
© 2022 Jakop et al. This is an open
access article distributed under the terms of the
Creative Commons Attribution License. |
en_US |
dc.subject |
Sperm |
en_US |
dc.subject |
Lipids |
en_US |
dc.subject |
Semen |
en_US |
dc.subject |
Lions |
en_US |
dc.subject |
Red blood cells |
en_US |
dc.subject |
Thin-layer chromatography |
en_US |
dc.subject |
Oxidation |
en_US |
dc.title |
Seminal lipid profiling and antioxidant capacity : a species comparison |
en_US |
dc.type |
Article |
en_US |