Reduced Expression of MAD2, BCL2, and MAP Kinase Activity in Pig Oocytes after In Vitro Aging Are Associated with Defects in Sister Chromatid Segregation During Meiosis II and Embryo Fragmentation After Activation
This study was conducted to examine expression of centromere protein B (CENPB), spindle checkpoint protein MAD2 (mitotic arrest deficient protein), and antiapoptotic protein BCL2; activities of MAPK (mitogen-activated protein kinase) and mitochondria distribution in pig oocytes during aging, and the...
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| Veröffentlicht in: | Biology of reproduction 2005-02, Vol.72 (2), p.373-383 |
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| creator | WEI MA DONG ZHANG YI HOU LI, Yong-Hai SUN, Qing-Yuan SUN, Xiao-Fang WANG, Wei-Hua |
| description | This study was conducted to examine expression of centromere protein B (CENPB), spindle checkpoint protein MAD2 (mitotic arrest
deficient protein), and antiapoptotic protein BCL2; activities of MAPK (mitogen-activated protein kinase) and mitochondria
distribution in pig oocytes during aging, and their relationship with sister chromatid separation during meiosis II and embryo
fragmentation and apoptosis after activation. After immature oocytes were cultured for 40â72 h, CENPB, MAD2, tubulin, BCL2,
and MAPK in the oocytes were examined by immunoblotting. Spindles, chromosomes, kinetochores, and mitochondria were examined
by immunofluorescence staining and apoptosis was examined by TUNEL assay. It was found that tubulin and CENPB was not changed
during 40â72 h of culture. However, the expression of MAD2 and BCL2 and the activity of MAPK were gradually reduced during
oocyte aging. The percentages of oocytes with normal spindle, chromosomes, and kinetochores were also reduced as oocyte aged
from 9.5% at 40 h to 17.3%, 34.6%, and 42.9% at 48, 60, and 72 h, respectively. Aggregated mitochondria were found in the
aged oocytes as compared with the uniform distribution in young oocytes. After activation, the proportions of oocytes with
abnormal anaphase II were significantly increased in aged oocytes. More ( P < 0.001) oocytes cultured for 60â72 h fragmented and showed apoptosis after activation as compared with the oocytes cultured
for 40â48 h. This study indicates that aging reduces expression in spindle checkpoint protein and antiapoptosis protein and
MAPK activity in pig oocytes. These events in turn cause abnormal sister chromatid segregation during meiosis II, embryo fragmentation,
and apoptosis.
Abstract
Aging reduces expression of spindle checkpoint protein, anti-apoptosis protein, and MAPK activity in pig oocytes |
| doi_str_mv | 10.1095/biolreprod.104.030999 |
| format | Article |
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deficient protein), and antiapoptotic protein BCL2; activities of MAPK (mitogen-activated protein kinase) and mitochondria
distribution in pig oocytes during aging, and their relationship with sister chromatid separation during meiosis II and embryo
fragmentation and apoptosis after activation. After immature oocytes were cultured for 40â72 h, CENPB, MAD2, tubulin, BCL2,
and MAPK in the oocytes were examined by immunoblotting. Spindles, chromosomes, kinetochores, and mitochondria were examined
by immunofluorescence staining and apoptosis was examined by TUNEL assay. It was found that tubulin and CENPB was not changed
during 40â72 h of culture. However, the expression of MAD2 and BCL2 and the activity of MAPK were gradually reduced during
oocyte aging. The percentages of oocytes with normal spindle, chromosomes, and kinetochores were also reduced as oocyte aged
from 9.5% at 40 h to 17.3%, 34.6%, and 42.9% at 48, 60, and 72 h, respectively. Aggregated mitochondria were found in the
aged oocytes as compared with the uniform distribution in young oocytes. After activation, the proportions of oocytes with
abnormal anaphase II were significantly increased in aged oocytes. More ( P < 0.001) oocytes cultured for 60â72 h fragmented and showed apoptosis after activation as compared with the oocytes cultured
for 40â48 h. This study indicates that aging reduces expression in spindle checkpoint protein and antiapoptosis protein and
MAPK activity in pig oocytes. These events in turn cause abnormal sister chromatid segregation during meiosis II, embryo fragmentation,
and apoptosis.
Abstract
Aging reduces expression of spindle checkpoint protein, anti-apoptosis protein, and MAPK activity in pig oocytes</description><identifier>ISSN: 0006-3363</identifier><identifier>EISSN: 1529-7268</identifier><identifier>DOI: 10.1095/biolreprod.104.030999</identifier><identifier>PMID: 15469999</identifier><identifier>CODEN: BIREBV</identifier><language>eng</language><publisher>Madison, WI: Society for the Study of Reproduction</publisher><subject>Anaphase - physiology ; Animals ; Apoptosis - drug effects ; Autoantigens - biosynthesis ; Biological and medical sciences ; Calcimycin - pharmacology ; Calcium - metabolism ; Carrier Proteins - biosynthesis ; Carrier Proteins - genetics ; Cell Cycle Proteins ; Cell Nucleus - physiology ; Centromere Protein B ; Chromosomal Proteins, Non-Histone - biosynthesis ; DNA-Binding Proteins - biosynthesis ; Early stages. Segmentation. Gastrulation. Neurulation ; Embryo, Mammalian - pathology ; Embryology: invertebrates and vertebrates. Teratology ; Fluorescent Antibody Technique ; Fundamental and applied biological sciences. Psychology ; Genes, bcl-2 - genetics ; In Situ Nick-End Labeling ; Ionophores - pharmacology ; Kinetochores - physiology ; Kinetochores - ultrastructure ; Meiosis - physiology ; Microscopy, Confocal ; Microtubules - physiology ; Microtubules - ultrastructure ; Mitochondria - physiology ; Mitochondria - ultrastructure ; Mitogen-Activated Protein Kinases - biosynthesis ; Mitogen-Activated Protein Kinases - metabolism ; Nuclear Proteins ; Oocytes - metabolism ; Parthenogenesis - physiology ; Sister Chromatid Exchange - physiology ; Swine ; Time Factors ; Tubulin - biosynthesis ; Vertebrates: reproduction</subject><ispartof>Biology of reproduction, 2005-02, Vol.72 (2), p.373-383</ispartof><rights>2005 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=16452088$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15469999$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>WEI MA</creatorcontrib><creatorcontrib>DONG ZHANG</creatorcontrib><creatorcontrib>YI HOU</creatorcontrib><creatorcontrib>LI, Yong-Hai</creatorcontrib><creatorcontrib>SUN, Qing-Yuan</creatorcontrib><creatorcontrib>SUN, Xiao-Fang</creatorcontrib><creatorcontrib>WANG, Wei-Hua</creatorcontrib><title>Reduced Expression of MAD2, BCL2, and MAP Kinase Activity in Pig Oocytes after In Vitro Aging Are Associated with Defects in Sister Chromatid Segregation During Meiosis II and Embryo Fragmentation After Activation</title><title>Biology of reproduction</title><addtitle>Biol Reprod</addtitle><description>This study was conducted to examine expression of centromere protein B (CENPB), spindle checkpoint protein MAD2 (mitotic arrest
deficient protein), and antiapoptotic protein BCL2; activities of MAPK (mitogen-activated protein kinase) and mitochondria
distribution in pig oocytes during aging, and their relationship with sister chromatid separation during meiosis II and embryo
fragmentation and apoptosis after activation. After immature oocytes were cultured for 40â72 h, CENPB, MAD2, tubulin, BCL2,
and MAPK in the oocytes were examined by immunoblotting. Spindles, chromosomes, kinetochores, and mitochondria were examined
by immunofluorescence staining and apoptosis was examined by TUNEL assay. It was found that tubulin and CENPB was not changed
during 40â72 h of culture. However, the expression of MAD2 and BCL2 and the activity of MAPK were gradually reduced during
oocyte aging. The percentages of oocytes with normal spindle, chromosomes, and kinetochores were also reduced as oocyte aged
from 9.5% at 40 h to 17.3%, 34.6%, and 42.9% at 48, 60, and 72 h, respectively. Aggregated mitochondria were found in the
aged oocytes as compared with the uniform distribution in young oocytes. After activation, the proportions of oocytes with
abnormal anaphase II were significantly increased in aged oocytes. More ( P < 0.001) oocytes cultured for 60â72 h fragmented and showed apoptosis after activation as compared with the oocytes cultured
for 40â48 h. This study indicates that aging reduces expression in spindle checkpoint protein and antiapoptosis protein and
MAPK activity in pig oocytes. These events in turn cause abnormal sister chromatid segregation during meiosis II, embryo fragmentation,
and apoptosis.
Abstract
Aging reduces expression of spindle checkpoint protein, anti-apoptosis protein, and MAPK activity in pig oocytes</description><subject>Anaphase - physiology</subject><subject>Animals</subject><subject>Apoptosis - drug effects</subject><subject>Autoantigens - biosynthesis</subject><subject>Biological and medical sciences</subject><subject>Calcimycin - pharmacology</subject><subject>Calcium - metabolism</subject><subject>Carrier Proteins - biosynthesis</subject><subject>Carrier Proteins - genetics</subject><subject>Cell Cycle Proteins</subject><subject>Cell Nucleus - physiology</subject><subject>Centromere Protein B</subject><subject>Chromosomal Proteins, Non-Histone - biosynthesis</subject><subject>DNA-Binding Proteins - biosynthesis</subject><subject>Early stages. Segmentation. Gastrulation. Neurulation</subject><subject>Embryo, Mammalian - pathology</subject><subject>Embryology: invertebrates and vertebrates. Teratology</subject><subject>Fluorescent Antibody Technique</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genes, bcl-2 - genetics</subject><subject>In Situ Nick-End Labeling</subject><subject>Ionophores - pharmacology</subject><subject>Kinetochores - physiology</subject><subject>Kinetochores - ultrastructure</subject><subject>Meiosis - physiology</subject><subject>Microscopy, Confocal</subject><subject>Microtubules - physiology</subject><subject>Microtubules - ultrastructure</subject><subject>Mitochondria - physiology</subject><subject>Mitochondria - ultrastructure</subject><subject>Mitogen-Activated Protein Kinases - biosynthesis</subject><subject>Mitogen-Activated Protein Kinases - metabolism</subject><subject>Nuclear Proteins</subject><subject>Oocytes - metabolism</subject><subject>Parthenogenesis - physiology</subject><subject>Sister Chromatid Exchange - physiology</subject><subject>Swine</subject><subject>Time Factors</subject><subject>Tubulin - biosynthesis</subject><subject>Vertebrates: reproduction</subject><issn>0006-3363</issn><issn>1529-7268</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkVFv0zAUhSMEYt3gJ4D8Ak9kOHac2I9Z20FFp00MeI2c-CYxSuJiO2T9ofwf3K5oj7zYvtZ3zj3SiaI3Cb5MsGAfK216CztrVJjTS0yxEOJZtEgYEXFOMv48WmCMs5jSjJ5F5879xDhJKaEvo7OEpVnAxSL68xXUVINC64edBee0GZFp0E2xIh_Q1XIbTjmqMN-hL3qUDlBRe_1b-z3SI7rTLbo19d6DQ7LxYNFmRD-0twYVrR5bVNggcM7UWvqwZNa-QytooPbuoL_X7iBadtYM0muF7qG10IZniLGa7MHiBrRx2qHN5phkPVR2b9C1le0Ao39Ei-PuY7Ljx6voRSN7B69P90X0_Xr9bfk53t5-2iyLbdxRjH3MVEWUwKKiikucJnnFZNrQXGaKs4RSJvNUZJiDAMEZSbhkAqcMYymIanhDL6L3j76hh18TOF8O2tXQ93IEM7kyy2kemiH_BZOcJ4TjPIBvT-BUDaDKndWDtPvyX2MBeHcCpKtl31g51to9cVnKCOb8iet0283aQukG2ffBlpbzPOekJCXNKf0LIiC1Ng</recordid><startdate>20050201</startdate><enddate>20050201</enddate><creator>WEI MA</creator><creator>DONG ZHANG</creator><creator>YI HOU</creator><creator>LI, Yong-Hai</creator><creator>SUN, Qing-Yuan</creator><creator>SUN, Xiao-Fang</creator><creator>WANG, Wei-Hua</creator><general>Society for the Study of Reproduction</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20050201</creationdate><title>Reduced Expression of MAD2, BCL2, and MAP Kinase Activity in Pig Oocytes after In Vitro Aging Are Associated with Defects in Sister Chromatid Segregation During Meiosis II and Embryo Fragmentation After Activation</title><author>WEI MA ; DONG ZHANG ; YI HOU ; LI, Yong-Hai ; SUN, Qing-Yuan ; SUN, Xiao-Fang ; WANG, Wei-Hua</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-h300t-5db2d909b3d8a0417b5a4f37a6d851335a749608e9e985218a5904500a92df8f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Anaphase - physiology</topic><topic>Animals</topic><topic>Apoptosis - drug effects</topic><topic>Autoantigens - biosynthesis</topic><topic>Biological and medical sciences</topic><topic>Calcimycin - pharmacology</topic><topic>Calcium - metabolism</topic><topic>Carrier Proteins - biosynthesis</topic><topic>Carrier Proteins - genetics</topic><topic>Cell Cycle Proteins</topic><topic>Cell Nucleus - physiology</topic><topic>Centromere Protein B</topic><topic>Chromosomal Proteins, Non-Histone - biosynthesis</topic><topic>DNA-Binding Proteins - biosynthesis</topic><topic>Early stages. Segmentation. Gastrulation. Neurulation</topic><topic>Embryo, Mammalian - pathology</topic><topic>Embryology: invertebrates and vertebrates. Teratology</topic><topic>Fluorescent Antibody Technique</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genes, bcl-2 - genetics</topic><topic>In Situ Nick-End Labeling</topic><topic>Ionophores - pharmacology</topic><topic>Kinetochores - physiology</topic><topic>Kinetochores - ultrastructure</topic><topic>Meiosis - physiology</topic><topic>Microscopy, Confocal</topic><topic>Microtubules - physiology</topic><topic>Microtubules - ultrastructure</topic><topic>Mitochondria - physiology</topic><topic>Mitochondria - ultrastructure</topic><topic>Mitogen-Activated Protein Kinases - biosynthesis</topic><topic>Mitogen-Activated Protein Kinases - metabolism</topic><topic>Nuclear Proteins</topic><topic>Oocytes - metabolism</topic><topic>Parthenogenesis - physiology</topic><topic>Sister Chromatid Exchange - physiology</topic><topic>Swine</topic><topic>Time Factors</topic><topic>Tubulin - biosynthesis</topic><topic>Vertebrates: reproduction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>WEI MA</creatorcontrib><creatorcontrib>DONG ZHANG</creatorcontrib><creatorcontrib>YI HOU</creatorcontrib><creatorcontrib>LI, Yong-Hai</creatorcontrib><creatorcontrib>SUN, Qing-Yuan</creatorcontrib><creatorcontrib>SUN, Xiao-Fang</creatorcontrib><creatorcontrib>WANG, Wei-Hua</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biology of reproduction</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>WEI MA</au><au>DONG ZHANG</au><au>YI HOU</au><au>LI, Yong-Hai</au><au>SUN, Qing-Yuan</au><au>SUN, Xiao-Fang</au><au>WANG, Wei-Hua</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Reduced Expression of MAD2, BCL2, and MAP Kinase Activity in Pig Oocytes after In Vitro Aging Are Associated with Defects in Sister Chromatid Segregation During Meiosis II and Embryo Fragmentation After Activation</atitle><jtitle>Biology of reproduction</jtitle><addtitle>Biol Reprod</addtitle><date>2005-02-01</date><risdate>2005</risdate><volume>72</volume><issue>2</issue><spage>373</spage><epage>383</epage><pages>373-383</pages><issn>0006-3363</issn><eissn>1529-7268</eissn><coden>BIREBV</coden><abstract>This study was conducted to examine expression of centromere protein B (CENPB), spindle checkpoint protein MAD2 (mitotic arrest
deficient protein), and antiapoptotic protein BCL2; activities of MAPK (mitogen-activated protein kinase) and mitochondria
distribution in pig oocytes during aging, and their relationship with sister chromatid separation during meiosis II and embryo
fragmentation and apoptosis after activation. After immature oocytes were cultured for 40â72 h, CENPB, MAD2, tubulin, BCL2,
and MAPK in the oocytes were examined by immunoblotting. Spindles, chromosomes, kinetochores, and mitochondria were examined
by immunofluorescence staining and apoptosis was examined by TUNEL assay. It was found that tubulin and CENPB was not changed
during 40â72 h of culture. However, the expression of MAD2 and BCL2 and the activity of MAPK were gradually reduced during
oocyte aging. The percentages of oocytes with normal spindle, chromosomes, and kinetochores were also reduced as oocyte aged
from 9.5% at 40 h to 17.3%, 34.6%, and 42.9% at 48, 60, and 72 h, respectively. Aggregated mitochondria were found in the
aged oocytes as compared with the uniform distribution in young oocytes. After activation, the proportions of oocytes with
abnormal anaphase II were significantly increased in aged oocytes. More ( P < 0.001) oocytes cultured for 60â72 h fragmented and showed apoptosis after activation as compared with the oocytes cultured
for 40â48 h. This study indicates that aging reduces expression in spindle checkpoint protein and antiapoptosis protein and
MAPK activity in pig oocytes. These events in turn cause abnormal sister chromatid segregation during meiosis II, embryo fragmentation,
and apoptosis.
Abstract
Aging reduces expression of spindle checkpoint protein, anti-apoptosis protein, and MAPK activity in pig oocytes</abstract><cop>Madison, WI</cop><pub>Society for the Study of Reproduction</pub><pmid>15469999</pmid><doi>10.1095/biolreprod.104.030999</doi><tpages>11</tpages></addata></record> |
| fulltext | fulltext |
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| ispartof | Biology of reproduction, 2005-02, Vol.72 (2), p.373-383 |
| issn | 0006-3363 1529-7268 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_67370302 |
| source | Oxford University Press Journals All Titles (1996-Current); MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; BioOne Complete |
| subjects | Anaphase - physiology Animals Apoptosis - drug effects Autoantigens - biosynthesis Biological and medical sciences Calcimycin - pharmacology Calcium - metabolism Carrier Proteins - biosynthesis Carrier Proteins - genetics Cell Cycle Proteins Cell Nucleus - physiology Centromere Protein B Chromosomal Proteins, Non-Histone - biosynthesis DNA-Binding Proteins - biosynthesis Early stages. Segmentation. Gastrulation. Neurulation Embryo, Mammalian - pathology Embryology: invertebrates and vertebrates. Teratology Fluorescent Antibody Technique Fundamental and applied biological sciences. Psychology Genes, bcl-2 - genetics In Situ Nick-End Labeling Ionophores - pharmacology Kinetochores - physiology Kinetochores - ultrastructure Meiosis - physiology Microscopy, Confocal Microtubules - physiology Microtubules - ultrastructure Mitochondria - physiology Mitochondria - ultrastructure Mitogen-Activated Protein Kinases - biosynthesis Mitogen-Activated Protein Kinases - metabolism Nuclear Proteins Oocytes - metabolism Parthenogenesis - physiology Sister Chromatid Exchange - physiology Swine Time Factors Tubulin - biosynthesis Vertebrates: reproduction |
| title | Reduced Expression of MAD2, BCL2, and MAP Kinase Activity in Pig Oocytes after In Vitro Aging Are Associated with Defects in Sister Chromatid Segregation During Meiosis II and Embryo Fragmentation After Activation |
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