Dermatan sulfate synergizes with heparin in murine sperm chromatin decondensation. (April 2013)
- Record Type:
- Journal Article
- Title:
- Dermatan sulfate synergizes with heparin in murine sperm chromatin decondensation. (April 2013)
- Main Title:
- Dermatan sulfate synergizes with heparin in murine sperm chromatin decondensation
- Authors:
- Sanchez, Melisa Celeste
Sedo, Cristian Alvarez
Julianelli, Vanina Laura
Romanato, Marina
Calvo, Lucrecia
Calvo, Juan Carlos
Fontana, Vanina Andrea - Abstract:
- <abstract> <title> <x xml:space="preserve">Abstract</x> </title> <p>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 <italic>in vivo</italic>. In the present paper, we analyze the role of heparin, structural analogue of HS, and dermatan sulfate (DS) in murine sperm chromatin decondensation <italic>in vitro</italic>, 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 <italic>in vitro</italic> but the decondensing ability of heparin was significantly higher. Use of both<abstract> <title> <x xml:space="preserve">Abstract</x> </title> <p>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 <italic>in vivo</italic>. In the present paper, we analyze the role of heparin, structural analogue of HS, and dermatan sulfate (DS) in murine sperm chromatin decondensation <italic>in vitro</italic>, 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 <italic>in vitro</italic> 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.</p> </abstract> … (more)
- Is Part Of:
- Systems biology in reproductive medicine. Volume 59:Number 2(2013:Apr.)
- Journal:
- Systems biology in reproductive medicine
- Issue:
- Volume 59:Number 2(2013:Apr.)
- Issue Display:
- Volume 59, Issue 2 (2013)
- Year:
- 2013
- Volume:
- 59
- Issue:
- 2
- Issue Sort Value:
- 2013-0059-0002-0000
- Page Start:
- 82
- Page End:
- 90
- Publication Date:
- 2013-04
- Subjects:
- Systems biology -- Periodicals
Andrology -- Periodicals
Generative organs, Male -- Diseases -- Periodicals
Biological systems -- Periodicals
Reproductive health -- Periodicals
Human reproduction -- Periodicals
612.61 - Journal URLs:
- http://informahealthcare.com/loi/aan ↗
http://www.tandf.co.uk/journals/titles/19396368.asp ↗
http://informahealthcare.com ↗ - DOI:
- 10.3109/19396368.2012.756952 ↗
- Languages:
- English
- ISSNs:
- 1939-6368
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 8589.323800
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 4297.xml