The Control of Oxidant Stress at Fertilization
Metazoan eggs alter their coats after fertilization to protect the early embryo. In sea urchins, this modification consists of a rapid, coordinated set of noncovalent macromolecular assembly steps that are stabilized by protein cross-linking. The sea urchin egg uses an oxidative cross-linking reacti...
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 1991-04, Vol.252 (5005), p.533-536 |
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| creator | Shapiro, Bennett M. |
| description | Metazoan eggs alter their coats after fertilization to protect the early embryo. In sea urchins, this modification consists of a rapid, coordinated set of noncovalent macromolecular assembly steps that are stabilized by protein cross-linking. The sea urchin egg uses an oxidative cross-linking reaction that requires hydrogen peroxide and a secreted peroxidase and thus faces the challenge of oxidant stress at the beginning of its development. Protection from the deleterious effects of this oxidative mechanism is afforded by regulation of the production and utilization of oxidizing species. This regulation requires a specific protein kinase C-activated oxidase and ovothiol, an intracellular antioxidant. |
| doi_str_mv | 10.1126/science.1850548 |
| format | Article |
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In sea urchins, this modification consists of a rapid, coordinated set of noncovalent macromolecular assembly steps that are stabilized by protein cross-linking. The sea urchin egg uses an oxidative cross-linking reaction that requires hydrogen peroxide and a secreted peroxidase and thus faces the challenge of oxidant stress at the beginning of its development. Protection from the deleterious effects of this oxidative mechanism is afforded by regulation of the production and utilization of oxidizing species. This regulation requires a specific protein kinase C-activated oxidase and ovothiol, an intracellular antioxidant.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.1850548</identifier><identifier>PMID: 1850548</identifier><identifier>CODEN: SCIEAS</identifier><language>eng</language><publisher>Washington, DC: American Society for the Advancement of Science</publisher><subject>Amino Acids, Sulfur - physiology ; Animals ; association ; Biochemical mechanisms ; Biochemistry ; Biological and medical sciences ; Cell membranes ; Cells ; Cortical granules ; Echinodermata ; Eggs ; Embryo, Nonmammalian - physiology ; Eukaryota - physiology ; Fertilization ; Fertilization (Biology) ; fertilization envelopes ; Fetuses ; Free Radicals ; Fundamental and applied biological sciences. Psychology ; Hydrogen Peroxide - metabolism ; Hydroxides - metabolism ; Hydroxyl Radical ; Invertebrates ; Marine biology ; mechanisms ; Methylhistidines ; Models, Biological ; oocytes ; Ova ; Oxidases ; oxidation ; Oxidation, Physiological ; Oxidative stress ; Oxygen Consumption ; regulation ; Reproduction ; reviews ; Sea urchins ; Sea Urchins - physiology ; Spermatozoa</subject><ispartof>Science (American Association for the Advancement of Science), 1991-04, Vol.252 (5005), p.533-536</ispartof><rights>Copyright 1991 American Association for the Advancement of Science</rights><rights>1991 INIST-CNRS</rights><rights>COPYRIGHT 1991 American Association for the Advancement of Science</rights><rights>COPYRIGHT 1991 American Association for the Advancement of Science</rights><rights>Copyright American Association for the Advancement of Science Apr 26, 1991</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c802t-d44f3c8d1a9357fed519a21acd44c44f7e028d6cdf5612445ea0d1b290a8b34f3</citedby><cites>FETCH-LOGICAL-c802t-d44f3c8d1a9357fed519a21acd44c44f7e028d6cdf5612445ea0d1b290a8b34f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/2875478$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/2875478$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,780,784,803,2884,2885,27924,27925,58017,58250</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19724460$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1850548$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Shapiro, Bennett M.</creatorcontrib><title>The Control of Oxidant Stress at Fertilization</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>Metazoan eggs alter their coats after fertilization to protect the early embryo. In sea urchins, this modification consists of a rapid, coordinated set of noncovalent macromolecular assembly steps that are stabilized by protein cross-linking. The sea urchin egg uses an oxidative cross-linking reaction that requires hydrogen peroxide and a secreted peroxidase and thus faces the challenge of oxidant stress at the beginning of its development. Protection from the deleterious effects of this oxidative mechanism is afforded by regulation of the production and utilization of oxidizing species. This regulation requires a specific protein kinase C-activated oxidase and ovothiol, an intracellular antioxidant.</description><subject>Amino Acids, Sulfur - physiology</subject><subject>Animals</subject><subject>association</subject><subject>Biochemical mechanisms</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Cell membranes</subject><subject>Cells</subject><subject>Cortical granules</subject><subject>Echinodermata</subject><subject>Eggs</subject><subject>Embryo, Nonmammalian - physiology</subject><subject>Eukaryota - physiology</subject><subject>Fertilization</subject><subject>Fertilization (Biology)</subject><subject>fertilization envelopes</subject><subject>Fetuses</subject><subject>Free Radicals</subject><subject>Fundamental and applied biological sciences. 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In sea urchins, this modification consists of a rapid, coordinated set of noncovalent macromolecular assembly steps that are stabilized by protein cross-linking. The sea urchin egg uses an oxidative cross-linking reaction that requires hydrogen peroxide and a secreted peroxidase and thus faces the challenge of oxidant stress at the beginning of its development. Protection from the deleterious effects of this oxidative mechanism is afforded by regulation of the production and utilization of oxidizing species. This regulation requires a specific protein kinase C-activated oxidase and ovothiol, an intracellular antioxidant.</abstract><cop>Washington, DC</cop><pub>American Society for the Advancement of Science</pub><pmid>1850548</pmid><doi>10.1126/science.1850548</doi><tpages>4</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0036-8075 |
| ispartof | Science (American Association for the Advancement of Science), 1991-04, Vol.252 (5005), p.533-536 |
| issn | 0036-8075 1095-9203 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_80528371 |
| source | MEDLINE; JSTOR Archive Collection A-Z Listing; American Association for the Advancement of Science |
| subjects | Amino Acids, Sulfur - physiology Animals association Biochemical mechanisms Biochemistry Biological and medical sciences Cell membranes Cells Cortical granules Echinodermata Eggs Embryo, Nonmammalian - physiology Eukaryota - physiology Fertilization Fertilization (Biology) fertilization envelopes Fetuses Free Radicals Fundamental and applied biological sciences. Psychology Hydrogen Peroxide - metabolism Hydroxides - metabolism Hydroxyl Radical Invertebrates Marine biology mechanisms Methylhistidines Models, Biological oocytes Ova Oxidases oxidation Oxidation, Physiological Oxidative stress Oxygen Consumption regulation Reproduction reviews Sea urchins Sea Urchins - physiology Spermatozoa |
| title | The Control of Oxidant Stress at Fertilization |
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