Deoxyribonuclease Activity in Semen

Pj, Quinn

doi:10.1530/jrf.0.0170035

Cited by 30 publications

(11 citation statements)

References 13 publications

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“…DNase 11 in whole sonicated bull, ram and mackerel sperm cells have already been demon5trated by Cordonnier and Bernardi [7] and Quinn [24]. However, the present work localized DNase 11 activity in sperm tail extract, and specifically in the mitochondrial fraction.…”

Section: Discussionmentioning

confidence: 47%

DNase II in Bull and Ram Sperm Tail and Mitochondria

Fisher

Bartoov

1980

Archives of Andrology

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Extracts of bull and ram sperm tails were prepared by DTT and CTAB treatment. Such extracts contained deoxyribonuclease 11, degrading only native double-stranded DNA at acid pH (3.9-4.5). At least three distinguishable DNase I1 activities were found in these extracts as judged by their sensitivity to thiol compounds and various anions and cations. The deoxyribonuclease I1 activity is apparently located in or in association with the mitochondria.

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Section: Discussionmentioning

confidence: 47%

DNase II in Bull and Ram Sperm Tail and Mitochondria

Fisher

Bartoov

1980

Archives of Andrology

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“…The longer incubation required to demonstrate loss of DNA from ram spermatozoa may be due to the action of deoxyribonucleases. A highly active DNase I is present in ram seminal plasma and this enzyme passes into the spermatozoa on freezing (Quinn, 1968). Loss of DNA from bull and boar spermatozoa aged in vitro has previously been repor¬ ted (Segina & Norman, 1964;Anand, Hoekstra & First, 1967).…”

Section: Discussionmentioning

confidence: 97%

Chemical and Ultrastructural Changes in Ram Spermatozoa After Washing, Cold Shock and Freezing

Quinn¹,

White²,

Cleland³

1969

Reproduction

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There was little or no loss of DNA or phospholipid from ram spermatozoa after washing three times with an equal volume of isotonic tris buffer. There was substantial loss of non-dialysable orcinoland biuret-reactive substances and also acid soluble phosphorus and phospholipids after cold-shocking and freezing ram spermatozoa. These components were also rendered more extractable with 10% NaCl after cold treatment. DNA was lost from cold-shocked and frozen ram spermatozoa after incubation at 37\s=deg\C for 6 hr and the rate of degradation of DNA into dialysable components was initially higher in coldshocked or frozen spermatozoa. Electron microscopy showed that cold shock and freezing caused profound changes in the appearance of the corrugated and terminal parts of the acrosome in the majority of spermatozoa but there were no apparent changes in the smooth region. There was considerable swelling of the acrosome with reduction in the density of the material contained within the acrosomal membranes. The effects were more pronounced in frozen than in cold-shocked spermatozoa. In the middle pieces, changes occurred in the matrix of the mitochondria making up the mitochondrial sheath. The matrix in cold-shocked and frozen spermatozoa appeared lighter than in the controls and loss of protein from the middle piece was confirmed histochemically.

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“…(3) Seminal plasma contains many chemicals, some of which may protect cfsDNA from degradation by binding with cfsDNA. In addition, some chemicals, especially some cations, such as Ca 2+ , Mg 2+ and Zn 2+ , may affect the activity of seminal DNases, which have been found in human semen with high activity dependent on Ca 2+ , Mg 2+ and other chemicals [22,23]. (4) It cannot be excluded that some pathological conditions, such as some inflammation, cancer, trauma etc., which cannot detected by the current WHO guidelines, may contribute to the high cfsDNA concentrations.…”

Section: Y Chromosome Microdeletionsmentioning

confidence: 99%

Quick recovery and characterization of cell-free DNA in seminal plasma of normozoospermia and azoospermia: implications for non-invasive genetic utilities

Li¹,

Huang²,

Zhou³

et al. 2009

Asian J Androl

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We established a quick and reliable method for recovering cell-free seminal DNA (cfsDNA), by using the binding-washing-elution procedure on the DNA purification column. Low variations (below 15%) among the triplicate values of cfsDNA quantity verified the reproducibility of our cfsDNA recovery method. Similar cfsDNA yield and size distribution between seminal plasma acquired by filtration and centrifugation confirmed the presence of cfsDNA. To investigate the general characterization of cfsDNA, the quantitation and size distribution of cfsDNA from normozoospermic and azoospermic semen were analyzed by real-time PCR and electrophoresis, respectively. CfsDNA concentration in semen with normozoospermia (n = 11) was 1.34 +/- 0.65 microg mL(-1), whereas a higher cfsDNA concentration was observed in azoospermia (2.56 +/- 1.43 microg mL(-1), n = 9). The continuous distribution of DNA fragments ranging from approximately 1 kb to 15 kb and a spectrum of multiples of 180-bp fragments were observed in each normozoospermic and azoospermic sample. Distinct characteristic DNA ladder fragmentations in some azoospermic samples implicated that cfsDNA originate partly from apoptotic cells. CfsDNAs of 36 selected azoospermic patients with known information of Y chromosome microdeletion were subjected to the same microdeletion analysis by multiplex PCR and PCR amplification of sY114 (1450 bp). All multiplex PCR reactions with cfsDNA amplified successfully and provided the same result as leukocyte DNA. PCR amplification of sY114 gave a 1450-bp amplicon as expected. Our data suggested the potential use of cfsDNA in search of biomarker or diagnostic procedures.

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Deoxyribonuclease Activity in Semen

Cited by 30 publications

References 13 publications

DNase II in Bull and Ram Sperm Tail and Mitochondria

DNase II in Bull and Ram Sperm Tail and Mitochondria

Chemical and Ultrastructural Changes in Ram Spermatozoa After Washing, Cold Shock and Freezing

Quick recovery and characterization of cell-free DNA in seminal plasma of normozoospermia and azoospermia: implications for non-invasive genetic utilities

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