Subcellular localization of nardilysin during mouse oocyte maturation
We have previously shown that the peptidase, nardilysin, contains a bipartite nuclear localization signal that permits the enzyme to cycle between the nucleus and cytoplasm. In the present study, we report that nardilysin accumulates in the nucleus of an oocyte as a function of its maturation. Nardi...
Gespeichert in:
Veröffentlicht in: | Archives of biochemistry and biophysics 2005-02, Vol.434 (1), p.187-194 |
---|---|
Hauptverfasser: | , , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 194 |
---|---|
container_issue | 1 |
container_start_page | 187 |
container_title | Archives of biochemistry and biophysics |
container_volume | 434 |
creator | Ma, Zhangliang Wang, Xuebing Hockman, Steven Snow, E. Charles Hersh, Louis B. |
description | We have previously shown that the peptidase, nardilysin, contains a bipartite nuclear localization signal that permits the enzyme to cycle between the nucleus and cytoplasm. In the present study, we report that nardilysin accumulates in the nucleus of an oocyte as a function of its maturation. Nardilysin is predominantly localized in the cytoplasm of an oocyte when initially placed into culture. The enzyme starts to accumulate in the nucleus within 30
min of in vitro culture. After 3
h, nardilysin is found as a spherical structure surrounded by condensed chromosomal DNA. After 18
h of in vitro culture, it co-localizes with β-tubulin at the spindle apparatus. Cilostamide, a phosphodiesterase 3A inhibitor that inhibits meiosis, blocks accumulation of nuclear nardilysin. This finding demonstrates that the nuclear entry of nardilysin is tightly controlled in the oocyte. Taken together, these experiments strongly suggest a role for nardilysin in meiosis through its dynamic translocation from cytosol to nucleus, and then to the spindle apparatus. |
doi_str_mv | 10.1016/j.abb.2004.10.027 |
format | Article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_67334484</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0003986104006113</els_id><sourcerecordid>67334484</sourcerecordid><originalsourceid>FETCH-LOGICAL-c417t-cc03c08d35058806620cbecca5cc0e2916b2382e69bb68ed91be72124e0cd4633</originalsourceid><addsrcrecordid>eNp9kMtOwzAQRS0EoqXwAWxQVuwSxo86iVghVB5SJRbA2rKdKXKVxMVOkMrX49JK7FhZts9c3TmEXFIoKFB5sy60MQUDEOleACuPyJRCLXPglTgmUwDgeV1JOiFnMa4BKBWSnZIJnUtWU8amZPE6GottO7Y6ZK23unXfenC-z_wq63VoXLuNrs-aMbj-I-v8GDHz3m4HzDo9jOEXPicnK91GvDicM_L-sHi7f8qXL4_P93fL3ApaDrm1wC1UDZ_DvKpASgbWoLV6nn4wNZKG8YqhrI2RFTY1NVgyygSCbYTkfEau97mb4D9HjIPqXNzV1z2mZkqWnAtRiQTSPWiDjzHgSm2C63TYKgpq506tVXKndu52T8ldmrk6hI-mw-Zv4iArAbd7ANOKXw6DitZhb7FxAe2gGu_-if8BQpF_fg</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>67334484</pqid></control><display><type>article</type><title>Subcellular localization of nardilysin during mouse oocyte maturation</title><source>MEDLINE</source><source>ScienceDirect Journals (5 years ago - present)</source><creator>Ma, Zhangliang ; Wang, Xuebing ; Hockman, Steven ; Snow, E. Charles ; Hersh, Louis B.</creator><creatorcontrib>Ma, Zhangliang ; Wang, Xuebing ; Hockman, Steven ; Snow, E. Charles ; Hersh, Louis B.</creatorcontrib><description>We have previously shown that the peptidase, nardilysin, contains a bipartite nuclear localization signal that permits the enzyme to cycle between the nucleus and cytoplasm. In the present study, we report that nardilysin accumulates in the nucleus of an oocyte as a function of its maturation. Nardilysin is predominantly localized in the cytoplasm of an oocyte when initially placed into culture. The enzyme starts to accumulate in the nucleus within 30
min of in vitro culture. After 3
h, nardilysin is found as a spherical structure surrounded by condensed chromosomal DNA. After 18
h of in vitro culture, it co-localizes with β-tubulin at the spindle apparatus. Cilostamide, a phosphodiesterase 3A inhibitor that inhibits meiosis, blocks accumulation of nuclear nardilysin. This finding demonstrates that the nuclear entry of nardilysin is tightly controlled in the oocyte. Taken together, these experiments strongly suggest a role for nardilysin in meiosis through its dynamic translocation from cytosol to nucleus, and then to the spindle apparatus.</description><identifier>ISSN: 0003-9861</identifier><identifier>EISSN: 1096-0384</identifier><identifier>DOI: 10.1016/j.abb.2004.10.027</identifier><identifier>PMID: 15629122</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Active Transport, Cell Nucleus - drug effects ; Animals ; Female ; In Vitro Techniques ; Maturation ; Meiosis ; Metalloendopeptidases - metabolism ; Mice ; Microscopy, Fluorescence ; Nardilysin ; Nuclear localization ; Oocyte ; Oocytes - cytology ; Oocytes - drug effects ; Oocytes - enzymology ; Oocytes - growth & development ; Quinolones - pharmacology ; Subcellular Fractions - enzymology ; Tubulin - metabolism</subject><ispartof>Archives of biochemistry and biophysics, 2005-02, Vol.434 (1), p.187-194</ispartof><rights>2004 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c417t-cc03c08d35058806620cbecca5cc0e2916b2382e69bb68ed91be72124e0cd4633</citedby><cites>FETCH-LOGICAL-c417t-cc03c08d35058806620cbecca5cc0e2916b2382e69bb68ed91be72124e0cd4633</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.abb.2004.10.027$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,777,781,3537,27905,27906,45976</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15629122$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ma, Zhangliang</creatorcontrib><creatorcontrib>Wang, Xuebing</creatorcontrib><creatorcontrib>Hockman, Steven</creatorcontrib><creatorcontrib>Snow, E. Charles</creatorcontrib><creatorcontrib>Hersh, Louis B.</creatorcontrib><title>Subcellular localization of nardilysin during mouse oocyte maturation</title><title>Archives of biochemistry and biophysics</title><addtitle>Arch Biochem Biophys</addtitle><description>We have previously shown that the peptidase, nardilysin, contains a bipartite nuclear localization signal that permits the enzyme to cycle between the nucleus and cytoplasm. In the present study, we report that nardilysin accumulates in the nucleus of an oocyte as a function of its maturation. Nardilysin is predominantly localized in the cytoplasm of an oocyte when initially placed into culture. The enzyme starts to accumulate in the nucleus within 30
min of in vitro culture. After 3
h, nardilysin is found as a spherical structure surrounded by condensed chromosomal DNA. After 18
h of in vitro culture, it co-localizes with β-tubulin at the spindle apparatus. Cilostamide, a phosphodiesterase 3A inhibitor that inhibits meiosis, blocks accumulation of nuclear nardilysin. This finding demonstrates that the nuclear entry of nardilysin is tightly controlled in the oocyte. Taken together, these experiments strongly suggest a role for nardilysin in meiosis through its dynamic translocation from cytosol to nucleus, and then to the spindle apparatus.</description><subject>Active Transport, Cell Nucleus - drug effects</subject><subject>Animals</subject><subject>Female</subject><subject>In Vitro Techniques</subject><subject>Maturation</subject><subject>Meiosis</subject><subject>Metalloendopeptidases - metabolism</subject><subject>Mice</subject><subject>Microscopy, Fluorescence</subject><subject>Nardilysin</subject><subject>Nuclear localization</subject><subject>Oocyte</subject><subject>Oocytes - cytology</subject><subject>Oocytes - drug effects</subject><subject>Oocytes - enzymology</subject><subject>Oocytes - growth & development</subject><subject>Quinolones - pharmacology</subject><subject>Subcellular Fractions - enzymology</subject><subject>Tubulin - metabolism</subject><issn>0003-9861</issn><issn>1096-0384</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kMtOwzAQRS0EoqXwAWxQVuwSxo86iVghVB5SJRbA2rKdKXKVxMVOkMrX49JK7FhZts9c3TmEXFIoKFB5sy60MQUDEOleACuPyJRCLXPglTgmUwDgeV1JOiFnMa4BKBWSnZIJnUtWU8amZPE6GottO7Y6ZK23unXfenC-z_wq63VoXLuNrs-aMbj-I-v8GDHz3m4HzDo9jOEXPicnK91GvDicM_L-sHi7f8qXL4_P93fL3ApaDrm1wC1UDZ_DvKpASgbWoLV6nn4wNZKG8YqhrI2RFTY1NVgyygSCbYTkfEau97mb4D9HjIPqXNzV1z2mZkqWnAtRiQTSPWiDjzHgSm2C63TYKgpq506tVXKndu52T8ldmrk6hI-mw-Zv4iArAbd7ANOKXw6DitZhb7FxAe2gGu_-if8BQpF_fg</recordid><startdate>20050201</startdate><enddate>20050201</enddate><creator>Ma, Zhangliang</creator><creator>Wang, Xuebing</creator><creator>Hockman, Steven</creator><creator>Snow, E. Charles</creator><creator>Hersh, Louis B.</creator><general>Elsevier Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20050201</creationdate><title>Subcellular localization of nardilysin during mouse oocyte maturation</title><author>Ma, Zhangliang ; Wang, Xuebing ; Hockman, Steven ; Snow, E. Charles ; Hersh, Louis B.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c417t-cc03c08d35058806620cbecca5cc0e2916b2382e69bb68ed91be72124e0cd4633</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Active Transport, Cell Nucleus - drug effects</topic><topic>Animals</topic><topic>Female</topic><topic>In Vitro Techniques</topic><topic>Maturation</topic><topic>Meiosis</topic><topic>Metalloendopeptidases - metabolism</topic><topic>Mice</topic><topic>Microscopy, Fluorescence</topic><topic>Nardilysin</topic><topic>Nuclear localization</topic><topic>Oocyte</topic><topic>Oocytes - cytology</topic><topic>Oocytes - drug effects</topic><topic>Oocytes - enzymology</topic><topic>Oocytes - growth & development</topic><topic>Quinolones - pharmacology</topic><topic>Subcellular Fractions - enzymology</topic><topic>Tubulin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ma, Zhangliang</creatorcontrib><creatorcontrib>Wang, Xuebing</creatorcontrib><creatorcontrib>Hockman, Steven</creatorcontrib><creatorcontrib>Snow, E. Charles</creatorcontrib><creatorcontrib>Hersh, Louis B.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Archives of biochemistry and biophysics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ma, Zhangliang</au><au>Wang, Xuebing</au><au>Hockman, Steven</au><au>Snow, E. Charles</au><au>Hersh, Louis B.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Subcellular localization of nardilysin during mouse oocyte maturation</atitle><jtitle>Archives of biochemistry and biophysics</jtitle><addtitle>Arch Biochem Biophys</addtitle><date>2005-02-01</date><risdate>2005</risdate><volume>434</volume><issue>1</issue><spage>187</spage><epage>194</epage><pages>187-194</pages><issn>0003-9861</issn><eissn>1096-0384</eissn><abstract>We have previously shown that the peptidase, nardilysin, contains a bipartite nuclear localization signal that permits the enzyme to cycle between the nucleus and cytoplasm. In the present study, we report that nardilysin accumulates in the nucleus of an oocyte as a function of its maturation. Nardilysin is predominantly localized in the cytoplasm of an oocyte when initially placed into culture. The enzyme starts to accumulate in the nucleus within 30
min of in vitro culture. After 3
h, nardilysin is found as a spherical structure surrounded by condensed chromosomal DNA. After 18
h of in vitro culture, it co-localizes with β-tubulin at the spindle apparatus. Cilostamide, a phosphodiesterase 3A inhibitor that inhibits meiosis, blocks accumulation of nuclear nardilysin. This finding demonstrates that the nuclear entry of nardilysin is tightly controlled in the oocyte. Taken together, these experiments strongly suggest a role for nardilysin in meiosis through its dynamic translocation from cytosol to nucleus, and then to the spindle apparatus.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>15629122</pmid><doi>10.1016/j.abb.2004.10.027</doi><tpages>8</tpages></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0003-9861 |
ispartof | Archives of biochemistry and biophysics, 2005-02, Vol.434 (1), p.187-194 |
issn | 0003-9861 1096-0384 |
language | eng |
recordid | cdi_proquest_miscellaneous_67334484 |
source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
subjects | Active Transport, Cell Nucleus - drug effects Animals Female In Vitro Techniques Maturation Meiosis Metalloendopeptidases - metabolism Mice Microscopy, Fluorescence Nardilysin Nuclear localization Oocyte Oocytes - cytology Oocytes - drug effects Oocytes - enzymology Oocytes - growth & development Quinolones - pharmacology Subcellular Fractions - enzymology Tubulin - metabolism |
title | Subcellular localization of nardilysin during mouse oocyte maturation |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-19T17%3A54%3A10IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Subcellular%20localization%20of%20nardilysin%20during%20mouse%20oocyte%20maturation&rft.jtitle=Archives%20of%20biochemistry%20and%20biophysics&rft.au=Ma,%20Zhangliang&rft.date=2005-02-01&rft.volume=434&rft.issue=1&rft.spage=187&rft.epage=194&rft.pages=187-194&rft.issn=0003-9861&rft.eissn=1096-0384&rft_id=info:doi/10.1016/j.abb.2004.10.027&rft_dat=%3Cproquest_cross%3E67334484%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=67334484&rft_id=info:pmid/15629122&rft_els_id=S0003986104006113&rfr_iscdi=true |