Heparin Binding Sites Are Present at a Higher Concentration on Sperm of Subfertile Men Than Donors of Known Fertility

Carrell, Douglas T.; Liu, L.

doi:10.1080/014850102317267463

Cited by 3 publications

(2 citation statements)

References 15 publications

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“…However, the mechanism of action of heparin/HS in this process is still a matter of controversy. The presence of heparin receptors on the sperm plasma membrane has been described by several groups [Carrell and Liu 2002;Delgado et al 1982;Lassalle and Testart 1992], and Delgado et al [1982] have proposed that heparin binding to its receptors leads to the destabilization of the sperm plasma membrane, which in turn would allow the incorporation of other molecules, such as GSH, into the sperm nucleus [Romanato et al 2003]. Alternatively, a direct effect of heparin on sperm chromatin has been suggested since heparin has a strong affinity for protamines and can combine with them in vitro to form a highly insoluble complex [Romanato et al 2003].…”

Section: Introductionmentioning

confidence: 98%

Dermatan sulfate synergizes with heparin in murine sperm chromatin decondensation

Sanchez¹,

Sedó²,

Julianelli³

et al. 2013

Systems Biology in Reproductive Medicine

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The mammalian sperm nucleus contains an unusually condensed chromatin, due to replacement of the majority of histones by protamines. However, soon after the spermatozoon penetrates the ooplasm at fertilization, decondensation of this densely packed chromatin must occur to allow formation of the male pronucleus and syngamy. Decondensation is accomplished by protamine disulfide bond reduction by oocyte glutathione and replacement of protamines by oocyte histones with the aid of an acceptor molecule. Previous results from our laboratory have demonstrated that heparan sulfate (HS) present in the ooplasm functions as protamine acceptor during human sperm decondensation in vivo. In the present paper, we analyze the role of heparin, structural analogue of HS, and dermatan sulfate (DS) in murine sperm chromatin decondensation in vitro, including the possibility of a synergistic effect between both glycosaminoglycans. Decondensation was assessed under phase contrast microscopy following incubation of murine spermatozoa with glutathione and either heparin, DS, or a combination of both. Ultrastructural changes taking place during decondensation were analyzed by transmission electron microscopy. Both glycosaminoglycans were able to promote the decondensation of murine spermatozoa in vitro but the decondensing ability of heparin was significantly higher. Use of both glycosaminoglycans together revealed the existence of a synergistic effect. Transmission electron microscopy analysis of decondensing spermatozoa supported these findings. Synergism between heparin and DS was observed both in capacitated and non-capacitated spermatozoa but decondensation kinetics was faster in the former. The results obtained indicate a new potential role for dermatan sulfate in murine sperm decondensation at fertilization and provide evidence of differences in the degree of chromatin condensation throughout the murine sperm nucleus.

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Section: Introductionmentioning

confidence: 98%

Dermatan sulfate synergizes with heparin in murine sperm chromatin decondensation

Sanchez¹,

Sedó²,

Julianelli³

et al. 2013

Systems Biology in Reproductive Medicine

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“…Not only protein alterations in mature P1 and P2, but also in pre‐P2 seem to compromise male fertility, either due to incomplete processing of pre‐P2 or the total absence of mature P2 (Carrell & Liu, 2001; de Mateo et al, 2009; de Mateo, Ramos, et al, 2011; Rezaei‐Gazik et al, 2022), with impact on increased DNA damage, lower sperm count, reduced motility, abnormal morphology, and worse ART outcomes (Rezaei‐Gazik et al, 2022; Soler‐Ventura et al, 2018). It has recently been reported that increased retention of pre‐P2 in sperm is associated with fertilization failure, as well as to impaired nucleosome disassembly during spermatogenesis (Rezaei‐Gazik et al, 2022), which could explain the origin of the observed sperm defects.…”

Section: The Unique Features Of the Mature Sperm Chromatin Contentmentioning

confidence: 99%

Insights into the sperm chromatin and implications for male infertility from a protein perspective

Iglesia

Jodar

Oliva

et al. 2022

WIREs Mechanisms of Disease

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Male germ cells undergo an extreme but fascinating process of chromatin remodeling that begins in the testis during the last phase of spermatogenesis and continues through epididymal sperm maturation. Most of the histones are replaced by small proteins named protamines, whose high basicity leads to a tight genomic compaction. This process is epigenetically regulated at many levels, not only by posttranslational modifications, but also by readers, writers, and erasers, in a context of a highly coordinated postmeiotic gene expression program. Protamines are key proteins for acquiring this highly specialized chromatin conformation, needed for sperm functionality. Interestingly, and contrary to what could be inferred from its very specific DNA‐packaging function across protamine‐containing species, human sperm chromatin contains a wide spectrum of protamine proteoforms, including truncated and posttranslationally modified proteoforms. The generation of protamine knock‐out models revealed not only chromatin compaction defects, but also collateral sperm alterations contributing to infertile phenotypes, evidencing the importance of sperm chromatin protamination toward the generation of a new individual. The unique features of sperm chromatin have motivated its study, applying from conventional to the most ground‐breaking techniques to disentangle its peculiarities and the cellular mechanisms governing its successful conferment, especially relevant from the protein point of view due to the important epigenetic role of sperm nuclear proteins. Gathering and contextualizing the most striking discoveries will provide a global understanding of the importance and complexity of achieving a proper chromatin compaction and exploring its implications on postfertilization events and beyond. This article is categorized under: Reproductive System Diseases > Genetics/Genomics/Epigenetics Reproductive System Diseases > Molecular and Cellular Physiology

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Heparan sulphate: a putative decondensing agent for human spermatozoa in vivo

Romanato

Cameo²,

Bertolesi³

et al. 2003

Human Reproduction

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Heparin Binding Sites Are Present at a Higher Concentration on Sperm of Subfertile Men Than Donors of Known Fertility

Cited by 3 publications

References 15 publications

Dermatan sulfate synergizes with heparin in murine sperm chromatin decondensation

Dermatan sulfate synergizes with heparin in murine sperm chromatin decondensation

Insights into the sperm chromatin and implications for male infertility from a protein perspective

Heparan sulphate: a putative decondensing agent for human spermatozoa in vivo

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