دورية أكاديمية
The nuclear form of phospholipid hydroperoxide glutathione peroxidase is a protein thiol peroxidase contributing to sperm chromatin stability.
| العنوان: | The nuclear form of phospholipid hydroperoxide glutathione peroxidase is a protein thiol peroxidase contributing to sperm chromatin stability. |
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| المؤلفون: | Conrad M; Institute of Clinical Molecular Biology and Tumour Genetics, GSF Research Centre for Environment and Health, Munich, Germany. marcus.conrad@gsf.de, Moreno SG, Sinowatz F, Ursini F, Kölle S, Roveri A, Brielmeier M, Wurst W, Maiorino M, Bornkamm GW |
| المصدر: | Molecular and cellular biology [Mol Cell Biol] 2005 Sep; Vol. 25 (17), pp. 7637-44. |
| نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: Taylor & Francis Country of Publication: United States NLM ID: 8109087 Publication Model: Print Cited Medium: Print ISSN: 0270-7306 (Print) Linking ISSN: 02707306 NLM ISO Abbreviation: Mol Cell Biol Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: 2023- : [Philadelphia] : Taylor & Francis Original Publication: [Washington, D.C.] : American Society for Microbiology, [c1981- |
| مواضيع طبية MeSH: | Cell Nucleus/*enzymology , Cell Nucleus/*genetics , Chromatin/*metabolism , Glutathione Peroxidase/*metabolism , Spermatozoa/*cytology , Spermatozoa/*enzymology, Animals ; Cell Shape ; Chromatin/chemistry ; Epithelium/metabolism ; Fertility/genetics ; Glutathione Peroxidase/deficiency ; Glutathione Peroxidase/genetics ; Male ; Mice ; Mice, Knockout ; Phospholipid Hydroperoxide Glutathione Peroxidase ; Spermatozoa/metabolism ; Sulfhydryl Compounds/metabolism |
| مستخلص: | The selenoenzyme phospholipid hydroperoxide glutathione peroxidase (PHGPx) is regarded as the major molecular target of selenodeficiency in rodents, accounting for most of the histopathological and structural abnormalities of testicular tissue and male germ cells. PHGPx exists as a cytosolic form, mitochondrial form, and nuclear form (nPHGPx) predominantly expressed in late spermatids and spermatozoa. Here, we demonstrate that mice with a targeted deletion of the nPHGPx gene were, unlike mice with the full knockout (KO) of PHGPx, not only viable but also, surprisingly, fully fertile. While both morphological analysis of testis and epididymis and sperm parameter measurements did not show any apparent abnormality, toluidine blue and acridine orange stainings of spermatozoa indicated defective chromatin condensation in the KO sperm isolated from the caput epididymis. Furthermore, upon drying and hydrating, KO sperm exhibited a significant proportion of morphologically abnormal heads. Monobromobimane labeling and protein-free thiol titration revealed significantly less extensive oxidation in the cauda epididymis when compared to that in the wild type. We conclude that nPHGPx, by acting as a protein thiol peroxidase in vivo, contributes to the structural stability of sperm chromatin. |
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| المشرفين على المادة: | 0 (Chromatin) 0 (Sulfhydryl Compounds) EC 1.11.1.12 (Phospholipid Hydroperoxide Glutathione Peroxidase) EC 1.11.1.9 (Glutathione Peroxidase) |
| تواريخ الأحداث: | Date Created: 20050819 Date Completed: 20050922 Latest Revision: 20191210 |
| رمز التحديث: | 20221213 |
| مُعرف محوري في PubMed: | PMC1190272 |
| DOI: | 10.1128/MCB.25.17.7637-7644.2005 |
| PMID: | 16107710 |
| قاعدة البيانات: | MEDLINE |
PDF full text from Publisher | تدمد: | 0270-7306 |
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| DOI: | 10.1128/MCB.25.17.7637-7644.2005 |