Mammalian zona pellucida glycoproteins: structure and function during fertilization
Zona pellucida (ZP) is a glycoproteinaceous translucent matrix that surrounds the mammalian oocyte and plays a critical role in the accomplishment of fertilization. In humans, it is composed of 4 glycoproteins designated as ZP1, ZP2, ZP3 and ZP4, whereas mouse ZP is composed of ZP1, ZP2 and ZP3 ( Zp...
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| Veröffentlicht in: | Cell and tissue research 2012-09, Vol.349 (3), p.665-678 |
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| description | Zona pellucida (ZP) is a glycoproteinaceous translucent matrix that surrounds the mammalian oocyte and plays a critical role in the accomplishment of fertilization. In humans, it is composed of 4 glycoproteins designated as ZP1, ZP2, ZP3 and ZP4, whereas mouse ZP is composed of ZP1, ZP2 and ZP3 (
Zp4
being a pseudogene). In addition to a variable sequence identity of a given zona protein among various species, human ZP1 and ZP4 are paralogs and mature polypeptide chains share an identity of 47%. Employing either affinity purified native or recombinant human zona proteins, it has been demonstrated that ZP1, ZP3 and ZP4 bind to the capacitated human spermatozoa and induce an acrosome reaction, whereas in mice, ZP3 acts as the putative primary sperm receptor. Human ZP2 only binds to acrosome-reacted spermatozoa and thus may be acting as a secondary sperm receptor. In contrast to
O
-linked glycans of ZP3 in mice,
N
-linked glycans of human ZP3 and ZP4 are more relevant for induction of the acrosome reaction. Recent studies suggest that Sialyl-Lewis
x
sequence present on both
N
- and
O
-glycans of human ZP play an important role in human sperm–egg binding. There are subtle differences in the downstream signaling events associated with ZP3 versus ZP1/ZP4-mediated induction of the acrosome reaction. For example, ZP3 but not ZP1/ZP4-mediated induction of the acrosome reaction is dependent on the activation of the G
i
protein-coupled receptor. Thus, various studies suggest that, in contrast to mice, in humans more than one zona protein binds to spermatozoa and induces an acrosome reaction. |
| doi_str_mv | 10.1007/s00441-011-1319-y |
| format | Article |
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Zp4
being a pseudogene). In addition to a variable sequence identity of a given zona protein among various species, human ZP1 and ZP4 are paralogs and mature polypeptide chains share an identity of 47%. Employing either affinity purified native or recombinant human zona proteins, it has been demonstrated that ZP1, ZP3 and ZP4 bind to the capacitated human spermatozoa and induce an acrosome reaction, whereas in mice, ZP3 acts as the putative primary sperm receptor. Human ZP2 only binds to acrosome-reacted spermatozoa and thus may be acting as a secondary sperm receptor. In contrast to
O
-linked glycans of ZP3 in mice,
N
-linked glycans of human ZP3 and ZP4 are more relevant for induction of the acrosome reaction. Recent studies suggest that Sialyl-Lewis
x
sequence present on both
N
- and
O
-glycans of human ZP play an important role in human sperm–egg binding. There are subtle differences in the downstream signaling events associated with ZP3 versus ZP1/ZP4-mediated induction of the acrosome reaction. For example, ZP3 but not ZP1/ZP4-mediated induction of the acrosome reaction is dependent on the activation of the G
i
protein-coupled receptor. Thus, various studies suggest that, in contrast to mice, in humans more than one zona protein binds to spermatozoa and induces an acrosome reaction.</description><identifier>ISSN: 0302-766X</identifier><identifier>EISSN: 1432-0878</identifier><identifier>DOI: 10.1007/s00441-011-1319-y</identifier><identifier>PMID: 22298023</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer-Verlag</publisher><subject>Acrosome Reaction - physiology ; Amino Acid Sequence ; Animals ; Binding sites ; Biomedical and Life Sciences ; Biomedicine ; Cellular biology ; Egg Proteins - chemistry ; Egg Proteins - physiology ; Female ; Fertilization - physiology ; Glycoproteins ; Human Genetics ; Humans ; Male ; Mammals ; Membrane Glycoproteins - chemistry ; Membrane Glycoproteins - physiology ; Mice ; Mice, Transgenic ; Models, Molecular ; Molecular Medicine ; Molecular Sequence Data ; Oocytes - metabolism ; Oocytes - physiology ; Protein binding ; Proteomics ; Receptors, Cell Surface - chemistry ; Receptors, Cell Surface - physiology ; Review ; Sequence Alignment ; Signal Transduction ; Sperm ; Spermatozoa - metabolism ; Spermatozoa - physiology ; Structure-Activity Relationship ; Zona Pellucida Glycoproteins</subject><ispartof>Cell and tissue research, 2012-09, Vol.349 (3), p.665-678</ispartof><rights>Springer-Verlag 2012</rights><rights>COPYRIGHT 2012 Springer</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c470t-3c213da809ad292ee3bd1d58c5ee68f92eb288fd632e7772d28d9ff61f1733ce3</citedby><cites>FETCH-LOGICAL-c470t-3c213da809ad292ee3bd1d58c5ee68f92eb288fd632e7772d28d9ff61f1733ce3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00441-011-1319-y$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00441-011-1319-y$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27903,27904,41467,42536,51297</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22298023$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gupta, Satish K.</creatorcontrib><creatorcontrib>Bhandari, Beena</creatorcontrib><creatorcontrib>Shrestha, Abhinav</creatorcontrib><creatorcontrib>Biswal, Bichitra K.</creatorcontrib><creatorcontrib>Palaniappan, Chetna</creatorcontrib><creatorcontrib>Malhotra, Sudha Saryu</creatorcontrib><creatorcontrib>Gupta, Neha</creatorcontrib><title>Mammalian zona pellucida glycoproteins: structure and function during fertilization</title><title>Cell and tissue research</title><addtitle>Cell Tissue Res</addtitle><addtitle>Cell Tissue Res</addtitle><description>Zona pellucida (ZP) is a glycoproteinaceous translucent matrix that surrounds the mammalian oocyte and plays a critical role in the accomplishment of fertilization. In humans, it is composed of 4 glycoproteins designated as ZP1, ZP2, ZP3 and ZP4, whereas mouse ZP is composed of ZP1, ZP2 and ZP3 (
Zp4
being a pseudogene). In addition to a variable sequence identity of a given zona protein among various species, human ZP1 and ZP4 are paralogs and mature polypeptide chains share an identity of 47%. Employing either affinity purified native or recombinant human zona proteins, it has been demonstrated that ZP1, ZP3 and ZP4 bind to the capacitated human spermatozoa and induce an acrosome reaction, whereas in mice, ZP3 acts as the putative primary sperm receptor. Human ZP2 only binds to acrosome-reacted spermatozoa and thus may be acting as a secondary sperm receptor. In contrast to
O
-linked glycans of ZP3 in mice,
N
-linked glycans of human ZP3 and ZP4 are more relevant for induction of the acrosome reaction. Recent studies suggest that Sialyl-Lewis
x
sequence present on both
N
- and
O
-glycans of human ZP play an important role in human sperm–egg binding. There are subtle differences in the downstream signaling events associated with ZP3 versus ZP1/ZP4-mediated induction of the acrosome reaction. For example, ZP3 but not ZP1/ZP4-mediated induction of the acrosome reaction is dependent on the activation of the G
i
protein-coupled receptor. Thus, various studies suggest that, in contrast to mice, in humans more than one zona protein binds to spermatozoa and induces an acrosome reaction.</description><subject>Acrosome Reaction - physiology</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Binding sites</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Cellular biology</subject><subject>Egg Proteins - chemistry</subject><subject>Egg Proteins - physiology</subject><subject>Female</subject><subject>Fertilization - physiology</subject><subject>Glycoproteins</subject><subject>Human Genetics</subject><subject>Humans</subject><subject>Male</subject><subject>Mammals</subject><subject>Membrane Glycoproteins - chemistry</subject><subject>Membrane Glycoproteins - physiology</subject><subject>Mice</subject><subject>Mice, Transgenic</subject><subject>Models, Molecular</subject><subject>Molecular Medicine</subject><subject>Molecular Sequence Data</subject><subject>Oocytes - metabolism</subject><subject>Oocytes - physiology</subject><subject>Protein binding</subject><subject>Proteomics</subject><subject>Receptors, Cell Surface - chemistry</subject><subject>Receptors, Cell Surface - physiology</subject><subject>Review</subject><subject>Sequence Alignment</subject><subject>Signal Transduction</subject><subject>Sperm</subject><subject>Spermatozoa - metabolism</subject><subject>Spermatozoa - physiology</subject><subject>Structure-Activity Relationship</subject><subject>Zona Pellucida Glycoproteins</subject><issn>0302-766X</issn><issn>1432-0878</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNp1kVFrFDEUhYModlv9Ab7IgCC-TM1NZmcS30rRKlR8UMG3kE1utikzyZpMHra_3gxbZStKHgKH71zOvYeQF0DPgdLhbaa066ClAC1wkO3-EVlBx1lLxSAekxXllLVD3_84Iac531IKXd_Lp-SEMSYFZXxFvn7W06RHr0NzF4NudjiOxXirm-24N3GX4ow-5HdNnlMxc0nY6GAbV4KZfQyNLcmHbeMwzX70d3oRn5EnTo8Zn9__Z-T7h_ffLj-211-uPl1eXLemG-jccsOAWy2o1JZJhsg3FuxamDViL1xVNkwIZ3vOcBgGZpmw0rkeHAycG-Rn5M1hbk35s2Ce1eSzqQvogLFkBQCdXAPnUNFXf6G3saRQ0ymgfGACODuitnpE5YOLc9JmGaou-LqTnPdUVur8H1R9FidvYkDnq_7A8PrIcIN6nG9yHMtyq_wQhANoUsw5oVO75Ced9jWkWhpXh8ZVbVwtjat99by836xsJrR_HL8rrgA7AHm3VIXpePX_Tf0F9IW1Jg</recordid><startdate>20120901</startdate><enddate>20120901</enddate><creator>Gupta, Satish K.</creator><creator>Bhandari, Beena</creator><creator>Shrestha, Abhinav</creator><creator>Biswal, Bichitra K.</creator><creator>Palaniappan, Chetna</creator><creator>Malhotra, Sudha Saryu</creator><creator>Gupta, Neha</creator><general>Springer-Verlag</general><general>Springer</general><general>Springer Nature B.V</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>3V.</scope><scope>7QP</scope><scope>7QR</scope><scope>7RV</scope><scope>7SS</scope><scope>7TK</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB0</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>NAPCQ</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20120901</creationdate><title>Mammalian zona pellucida glycoproteins: structure and function during fertilization</title><author>Gupta, Satish K. ; Bhandari, Beena ; Shrestha, Abhinav ; Biswal, Bichitra K. ; Palaniappan, Chetna ; Malhotra, Sudha Saryu ; Gupta, Neha</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c470t-3c213da809ad292ee3bd1d58c5ee68f92eb288fd632e7772d28d9ff61f1733ce3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Acrosome Reaction - physiology</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Binding sites</topic><topic>Biomedical and Life Sciences</topic><topic>Biomedicine</topic><topic>Cellular biology</topic><topic>Egg Proteins - chemistry</topic><topic>Egg Proteins - physiology</topic><topic>Female</topic><topic>Fertilization - physiology</topic><topic>Glycoproteins</topic><topic>Human Genetics</topic><topic>Humans</topic><topic>Male</topic><topic>Mammals</topic><topic>Membrane Glycoproteins - chemistry</topic><topic>Membrane Glycoproteins - physiology</topic><topic>Mice</topic><topic>Mice, Transgenic</topic><topic>Models, Molecular</topic><topic>Molecular Medicine</topic><topic>Molecular Sequence Data</topic><topic>Oocytes - metabolism</topic><topic>Oocytes - physiology</topic><topic>Protein binding</topic><topic>Proteomics</topic><topic>Receptors, Cell Surface - chemistry</topic><topic>Receptors, Cell Surface - physiology</topic><topic>Review</topic><topic>Sequence Alignment</topic><topic>Signal Transduction</topic><topic>Sperm</topic><topic>Spermatozoa - metabolism</topic><topic>Spermatozoa - physiology</topic><topic>Structure-Activity Relationship</topic><topic>Zona Pellucida Glycoproteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gupta, Satish K.</creatorcontrib><creatorcontrib>Bhandari, Beena</creatorcontrib><creatorcontrib>Shrestha, Abhinav</creatorcontrib><creatorcontrib>Biswal, Bichitra K.</creatorcontrib><creatorcontrib>Palaniappan, Chetna</creatorcontrib><creatorcontrib>Malhotra, Sudha Saryu</creatorcontrib><creatorcontrib>Gupta, Neha</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Nursing & Allied Health Database</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Neurosciences Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Nursing & Allied Health Database (Alumni Edition)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>Nursing & Allied Health Premium</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Cell and tissue research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gupta, Satish K.</au><au>Bhandari, Beena</au><au>Shrestha, Abhinav</au><au>Biswal, Bichitra K.</au><au>Palaniappan, Chetna</au><au>Malhotra, Sudha Saryu</au><au>Gupta, Neha</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Mammalian zona pellucida glycoproteins: structure and function during fertilization</atitle><jtitle>Cell and tissue research</jtitle><stitle>Cell Tissue Res</stitle><addtitle>Cell Tissue Res</addtitle><date>2012-09-01</date><risdate>2012</risdate><volume>349</volume><issue>3</issue><spage>665</spage><epage>678</epage><pages>665-678</pages><issn>0302-766X</issn><eissn>1432-0878</eissn><abstract>Zona pellucida (ZP) is a glycoproteinaceous translucent matrix that surrounds the mammalian oocyte and plays a critical role in the accomplishment of fertilization. In humans, it is composed of 4 glycoproteins designated as ZP1, ZP2, ZP3 and ZP4, whereas mouse ZP is composed of ZP1, ZP2 and ZP3 (
Zp4
being a pseudogene). In addition to a variable sequence identity of a given zona protein among various species, human ZP1 and ZP4 are paralogs and mature polypeptide chains share an identity of 47%. Employing either affinity purified native or recombinant human zona proteins, it has been demonstrated that ZP1, ZP3 and ZP4 bind to the capacitated human spermatozoa and induce an acrosome reaction, whereas in mice, ZP3 acts as the putative primary sperm receptor. Human ZP2 only binds to acrosome-reacted spermatozoa and thus may be acting as a secondary sperm receptor. In contrast to
O
-linked glycans of ZP3 in mice,
N
-linked glycans of human ZP3 and ZP4 are more relevant for induction of the acrosome reaction. Recent studies suggest that Sialyl-Lewis
x
sequence present on both
N
- and
O
-glycans of human ZP play an important role in human sperm–egg binding. There are subtle differences in the downstream signaling events associated with ZP3 versus ZP1/ZP4-mediated induction of the acrosome reaction. For example, ZP3 but not ZP1/ZP4-mediated induction of the acrosome reaction is dependent on the activation of the G
i
protein-coupled receptor. Thus, various studies suggest that, in contrast to mice, in humans more than one zona protein binds to spermatozoa and induces an acrosome reaction.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer-Verlag</pub><pmid>22298023</pmid><doi>10.1007/s00441-011-1319-y</doi><tpages>14</tpages></addata></record> |
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| ispartof | Cell and tissue research, 2012-09, Vol.349 (3), p.665-678 |
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| language | eng |
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| source | MEDLINE; SpringerLink Journals - AutoHoldings |
| subjects | Acrosome Reaction - physiology Amino Acid Sequence Animals Binding sites Biomedical and Life Sciences Biomedicine Cellular biology Egg Proteins - chemistry Egg Proteins - physiology Female Fertilization - physiology Glycoproteins Human Genetics Humans Male Mammals Membrane Glycoproteins - chemistry Membrane Glycoproteins - physiology Mice Mice, Transgenic Models, Molecular Molecular Medicine Molecular Sequence Data Oocytes - metabolism Oocytes - physiology Protein binding Proteomics Receptors, Cell Surface - chemistry Receptors, Cell Surface - physiology Review Sequence Alignment Signal Transduction Sperm Spermatozoa - metabolism Spermatozoa - physiology Structure-Activity Relationship Zona Pellucida Glycoproteins |
| title | Mammalian zona pellucida glycoproteins: structure and function during fertilization |
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