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A Kinase Anchor Protein 4 Is Vulnerable to Oxidative Adduction in Male Germ Cells

Oxidative stress is a leading causative agent in the defective sperm function associated with male infertility. Such stress commonly manifests via the accumulation of pathological levels of the electrophilic aldehyde, 4-hydroxynonenal (4HNE), generated as a result of lipid peroxidation. This highly...

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Autores principales: Nixon, Brett, Bernstein, Ilana R., Cafe, Shenae L., Delehedde, Maryse, Sergeant, Nicolas, Anderson, Amanda L., Trigg, Natalie A., Eamens, Andrew L., Lord, Tessa, Dun, Matthew D., De Iuliis, Geoffry N., Bromfield, Elizabeth G.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6933317/
https://www.ncbi.nlm.nih.gov/pubmed/31921838
http://dx.doi.org/10.3389/fcell.2019.00319
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author Nixon, Brett
Bernstein, Ilana R.
Cafe, Shenae L.
Delehedde, Maryse
Sergeant, Nicolas
Anderson, Amanda L.
Trigg, Natalie A.
Eamens, Andrew L.
Lord, Tessa
Dun, Matthew D.
De Iuliis, Geoffry N.
Bromfield, Elizabeth G.
author_facet Nixon, Brett
Bernstein, Ilana R.
Cafe, Shenae L.
Delehedde, Maryse
Sergeant, Nicolas
Anderson, Amanda L.
Trigg, Natalie A.
Eamens, Andrew L.
Lord, Tessa
Dun, Matthew D.
De Iuliis, Geoffry N.
Bromfield, Elizabeth G.
author_sort Nixon, Brett
collection PubMed
description Oxidative stress is a leading causative agent in the defective sperm function associated with male infertility. Such stress commonly manifests via the accumulation of pathological levels of the electrophilic aldehyde, 4-hydroxynonenal (4HNE), generated as a result of lipid peroxidation. This highly reactive lipid aldehyde elicits a spectrum of cytotoxic lesions owing to its propensity to form stable adducts with biomolecules. Notably however, not all elements of the sperm proteome appear to display an equivalent vulnerability to 4HNE modification, with only a small number of putative targets having been identified to date. Here, we validate one such target of 4HNE adduction, A-Kinase Anchor Protein 4 (AKAP4); a major component of the sperm fibrous sheath responsible for regulating the signal transduction and metabolic pathways that support sperm motility and capacitation. Our data confirm that both the precursor (proAKAP4), and mature form of AKAP4, are conserved targets of 4HNE adduction in primary cultures of post-meiotic male germ cells (round spermatids) and in mature mouse and human spermatozoa. We further demonstrate that 4HNE treatment of round spermatids and mature spermatozoa results in a substantial reduction in the levels of both proAKAP4 and AKAP4 proteins. This response proved refractory to pharmacological inhibition of proteolysis, but coincided with an apparent increase in the degree of protein aggregation. Further, we demonstrate that 4HNE-mediated protein degradation and/or aggregation culminates in reduced levels of capacitation-associated phosphorylation in mature human spermatozoa, possibly due to dysregulation of the signaling framework assembled around the AKAP4 scaffold. Together, these findings suggest that AKAP4 plays an important role in the pathophysiological responses to 4HNE, thus strengthening the importance of AKAP4 as a biomarker of sperm quality, and providing the impetus for the design of an efficacious antioxidant-based intervention strategy to alleviate sperm dysfunction.
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spelling pubmed-69333172020-01-09 A Kinase Anchor Protein 4 Is Vulnerable to Oxidative Adduction in Male Germ Cells Nixon, Brett Bernstein, Ilana R. Cafe, Shenae L. Delehedde, Maryse Sergeant, Nicolas Anderson, Amanda L. Trigg, Natalie A. Eamens, Andrew L. Lord, Tessa Dun, Matthew D. De Iuliis, Geoffry N. Bromfield, Elizabeth G. Front Cell Dev Biol Cell and Developmental Biology Oxidative stress is a leading causative agent in the defective sperm function associated with male infertility. Such stress commonly manifests via the accumulation of pathological levels of the electrophilic aldehyde, 4-hydroxynonenal (4HNE), generated as a result of lipid peroxidation. This highly reactive lipid aldehyde elicits a spectrum of cytotoxic lesions owing to its propensity to form stable adducts with biomolecules. Notably however, not all elements of the sperm proteome appear to display an equivalent vulnerability to 4HNE modification, with only a small number of putative targets having been identified to date. Here, we validate one such target of 4HNE adduction, A-Kinase Anchor Protein 4 (AKAP4); a major component of the sperm fibrous sheath responsible for regulating the signal transduction and metabolic pathways that support sperm motility and capacitation. Our data confirm that both the precursor (proAKAP4), and mature form of AKAP4, are conserved targets of 4HNE adduction in primary cultures of post-meiotic male germ cells (round spermatids) and in mature mouse and human spermatozoa. We further demonstrate that 4HNE treatment of round spermatids and mature spermatozoa results in a substantial reduction in the levels of both proAKAP4 and AKAP4 proteins. This response proved refractory to pharmacological inhibition of proteolysis, but coincided with an apparent increase in the degree of protein aggregation. Further, we demonstrate that 4HNE-mediated protein degradation and/or aggregation culminates in reduced levels of capacitation-associated phosphorylation in mature human spermatozoa, possibly due to dysregulation of the signaling framework assembled around the AKAP4 scaffold. Together, these findings suggest that AKAP4 plays an important role in the pathophysiological responses to 4HNE, thus strengthening the importance of AKAP4 as a biomarker of sperm quality, and providing the impetus for the design of an efficacious antioxidant-based intervention strategy to alleviate sperm dysfunction. Frontiers Media S.A. 2019-12-20 /pmc/articles/PMC6933317/ /pubmed/31921838 http://dx.doi.org/10.3389/fcell.2019.00319 Text en Copyright © 2019 Nixon, Bernstein, Cafe, Delehedde, Sergeant, Anderson, Trigg, Eamens, Lord, Dun, De Iuliis and Bromfield. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Cell and Developmental Biology
Nixon, Brett
Bernstein, Ilana R.
Cafe, Shenae L.
Delehedde, Maryse
Sergeant, Nicolas
Anderson, Amanda L.
Trigg, Natalie A.
Eamens, Andrew L.
Lord, Tessa
Dun, Matthew D.
De Iuliis, Geoffry N.
Bromfield, Elizabeth G.
A Kinase Anchor Protein 4 Is Vulnerable to Oxidative Adduction in Male Germ Cells
title A Kinase Anchor Protein 4 Is Vulnerable to Oxidative Adduction in Male Germ Cells
title_full A Kinase Anchor Protein 4 Is Vulnerable to Oxidative Adduction in Male Germ Cells
title_fullStr A Kinase Anchor Protein 4 Is Vulnerable to Oxidative Adduction in Male Germ Cells
title_full_unstemmed A Kinase Anchor Protein 4 Is Vulnerable to Oxidative Adduction in Male Germ Cells
title_short A Kinase Anchor Protein 4 Is Vulnerable to Oxidative Adduction in Male Germ Cells
title_sort kinase anchor protein 4 is vulnerable to oxidative adduction in male germ cells
topic Cell and Developmental Biology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6933317/
https://www.ncbi.nlm.nih.gov/pubmed/31921838
http://dx.doi.org/10.3389/fcell.2019.00319
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