Decoding the role of cytochrome c in metabolism of human spermatozoa by Raman imaging
The normal functioning of sperm cells requires cytochrome c in the redox balanced forms: reduced and oxidized. The oxidized form of cytochrome c is localized in the mitochondrial intermembrane space and is a part of the electron transport chain. This ensures that electron shuttling between the compl...
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Frontiers Media S.A.
2022-11-01
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Series: | Frontiers in Cell and Developmental Biology |
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Online Access: | https://www.frontiersin.org/articles/10.3389/fcell.2022.983993/full |
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author | Halina Abramczyk Bogna Sobkiewicz Renata Walczak-Jędrzejowska Katarzyna Marchlewska Jakub Surmacki |
author_facet | Halina Abramczyk Bogna Sobkiewicz Renata Walczak-Jędrzejowska Katarzyna Marchlewska Jakub Surmacki |
author_sort | Halina Abramczyk |
collection | DOAJ |
description | The normal functioning of sperm cells requires cytochrome c in the redox balanced forms: reduced and oxidized. The oxidized form of cytochrome c is localized in the mitochondrial intermembrane space and is a part of the electron transport chain. This ensures that electron shuttling between the complex III, cytochrome c, and complex IV can occur leading to controlled effective oxidative phosphorylation (respiration) and ATP production needed for most steps in spermatozoal maturation, motility, hyperactivation and fertilization. We studied the biochemical composition of specific organelles in sperm cells by Raman imaging. The structures of the head consisting of the nucleus and acrosome, the midpiece representing mitochondria, and the tail characterized by the sperm axoneme surrounded by outer dense fiber and covered by the membrane were measured. Metabolic biochemical analysis of mitochondria, head and tail of sperm cells, and seminal plasma by using Raman imaging combined with chemometric classification method of Cluster Analysis has been obtained. Our results show that cytochrome c, which is a key protein that is needed to maintain life (respiration) and cell death (apoptosis), is located in sperm mitochondria in the oxidized or reduced form of the heme group. This work demonstrated that an application of Raman micro-spectroscopy can be extended to monitoring the redox state of mitochondrial cytochrome c in sperm cells. |
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id | doaj.art-8a8dfa18afd04e22bf2e3a910b06df26 |
institution | Directory Open Access Journal |
issn | 2296-634X |
language | English |
last_indexed | 2024-04-12T05:27:03Z |
publishDate | 2022-11-01 |
publisher | Frontiers Media S.A. |
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series | Frontiers in Cell and Developmental Biology |
spelling | doaj.art-8a8dfa18afd04e22bf2e3a910b06df262022-12-22T03:46:13ZengFrontiers Media S.A.Frontiers in Cell and Developmental Biology2296-634X2022-11-011010.3389/fcell.2022.983993983993Decoding the role of cytochrome c in metabolism of human spermatozoa by Raman imagingHalina Abramczyk0Bogna Sobkiewicz1Renata Walczak-Jędrzejowska2Katarzyna Marchlewska3Jakub Surmacki4Lodz University of Technology, Institute of Applied Radiation Chemistry, Laboratory of Laser Molecular Spectroscopy, Lodz, PolandFertility Clinic Salve Medica, Lodz, PolandDepartment of Andrology and Reproductive Endocrinology, Medical University of Lodz, Lodz, PolandDepartment of Andrology and Reproductive Endocrinology, Medical University of Lodz, Lodz, PolandLodz University of Technology, Institute of Applied Radiation Chemistry, Laboratory of Laser Molecular Spectroscopy, Lodz, PolandThe normal functioning of sperm cells requires cytochrome c in the redox balanced forms: reduced and oxidized. The oxidized form of cytochrome c is localized in the mitochondrial intermembrane space and is a part of the electron transport chain. This ensures that electron shuttling between the complex III, cytochrome c, and complex IV can occur leading to controlled effective oxidative phosphorylation (respiration) and ATP production needed for most steps in spermatozoal maturation, motility, hyperactivation and fertilization. We studied the biochemical composition of specific organelles in sperm cells by Raman imaging. The structures of the head consisting of the nucleus and acrosome, the midpiece representing mitochondria, and the tail characterized by the sperm axoneme surrounded by outer dense fiber and covered by the membrane were measured. Metabolic biochemical analysis of mitochondria, head and tail of sperm cells, and seminal plasma by using Raman imaging combined with chemometric classification method of Cluster Analysis has been obtained. Our results show that cytochrome c, which is a key protein that is needed to maintain life (respiration) and cell death (apoptosis), is located in sperm mitochondria in the oxidized or reduced form of the heme group. This work demonstrated that an application of Raman micro-spectroscopy can be extended to monitoring the redox state of mitochondrial cytochrome c in sperm cells.https://www.frontiersin.org/articles/10.3389/fcell.2022.983993/fullhuman spermatozoasemen analysiscytochrome cmitochondriaRaman spectroscopy and imaging |
spellingShingle | Halina Abramczyk Bogna Sobkiewicz Renata Walczak-Jędrzejowska Katarzyna Marchlewska Jakub Surmacki Decoding the role of cytochrome c in metabolism of human spermatozoa by Raman imaging Frontiers in Cell and Developmental Biology human spermatozoa semen analysis cytochrome c mitochondria Raman spectroscopy and imaging |
title | Decoding the role of cytochrome c in metabolism of human spermatozoa by Raman imaging |
title_full | Decoding the role of cytochrome c in metabolism of human spermatozoa by Raman imaging |
title_fullStr | Decoding the role of cytochrome c in metabolism of human spermatozoa by Raman imaging |
title_full_unstemmed | Decoding the role of cytochrome c in metabolism of human spermatozoa by Raman imaging |
title_short | Decoding the role of cytochrome c in metabolism of human spermatozoa by Raman imaging |
title_sort | decoding the role of cytochrome c in metabolism of human spermatozoa by raman imaging |
topic | human spermatozoa semen analysis cytochrome c mitochondria Raman spectroscopy and imaging |
url | https://www.frontiersin.org/articles/10.3389/fcell.2022.983993/full |
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