Cloning of Rainbow Trout Egg Envelope Proteins: Members of a Unique Group of Structural Proteins
All vertebrate eggs are surrounded by an extracellular envelope that protects the egg and is vital for a successful fertilization. The terminology and functions of the egg envelope vary in different vertebrate groups, but the envelope itself is consistently composed of a few major proteins that are...
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Veröffentlicht in: | Biology of reproduction 2001-03, Vol.64 (3), p.805-811 |
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creator | HYLLNER, Sven Johan WESTERLUND, Liselotte OLSSON, Per-Erik SCHOPEN, Arndt |
description | All vertebrate eggs are surrounded by an extracellular envelope that protects the egg and is vital for a successful fertilization.
The terminology and functions of the egg envelope vary in different vertebrate groups, but the envelope itself is consistently
composed of a few major proteins that are deposited around the oocyte during oocyte growth. Here, we describe the deduced
amino acid sequences and tissue expression patterns of the three major egg envelope proteins for rainbow trout ( Oncorhynchus mykiss ). All three vitelline envelope proteins (VEPs) are expressed in the livers of both male and female fish, with higher expression
in females. In addition, VEPγ mRNA is also detected in the female gonads. To our knowledge, this is the first time that expression
of a VEP protein gene has been demonstrated to occur in more than one organ. Sequence comparison reveals that all three VEP
proteins share distinct homology with their amphibian, avian, and mammalian counterparts. Whereas mammalian zona pellucida
protein 3 isoforms contain two conserved serines needed for sperm binding, these are not conserved in teleost species, in
which sperm entry is restricted to the micropyle. Besides the difference in VEPγ sperm-binding function, the high sequence
homology suggests that the egg envelope proteins from these distinct vertebrate groups share a common ancestry and form a
unique group of structural proteins. |
doi_str_mv | 10.1095/biolreprod64.3.805 |
format | Article |
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The terminology and functions of the egg envelope vary in different vertebrate groups, but the envelope itself is consistently
composed of a few major proteins that are deposited around the oocyte during oocyte growth. Here, we describe the deduced
amino acid sequences and tissue expression patterns of the three major egg envelope proteins for rainbow trout ( Oncorhynchus mykiss ). All three vitelline envelope proteins (VEPs) are expressed in the livers of both male and female fish, with higher expression
in females. In addition, VEPγ mRNA is also detected in the female gonads. To our knowledge, this is the first time that expression
of a VEP protein gene has been demonstrated to occur in more than one organ. Sequence comparison reveals that all three VEP
proteins share distinct homology with their amphibian, avian, and mammalian counterparts. Whereas mammalian zona pellucida
protein 3 isoforms contain two conserved serines needed for sperm binding, these are not conserved in teleost species, in
which sperm entry is restricted to the micropyle. Besides the difference in VEPγ sperm-binding function, the high sequence
homology suggests that the egg envelope proteins from these distinct vertebrate groups share a common ancestry and form a
unique group of structural proteins.</description><identifier>ISSN: 0006-3363</identifier><identifier>EISSN: 1529-7268</identifier><identifier>DOI: 10.1095/biolreprod64.3.805</identifier><identifier>PMID: 11207195</identifier><identifier>CODEN: BIREBV</identifier><language>eng</language><publisher>Madison, WI: Society for the Study of Reproduction</publisher><subject>Amino Acid Sequence ; Analytical, structural and metabolic biochemistry ; Animals ; Base Sequence ; Biological and medical sciences ; Blotting, Northern - veterinary ; Blotting, Western - veterinary ; Cloning, Molecular ; DNA Probes - chemistry ; Egg Proteins - chemistry ; Egg Proteins - genetics ; Escherichia coli - genetics ; Estradiol - pharmacology ; Female ; Fundamental and applied biological sciences. Psychology ; Gene Library ; Holoproteins ; Male ; Molecular Sequence Data ; Oncorhynchus mykiss - physiology ; Other proteins ; Protein Isoforms ; Proteins ; Sequence Alignment ; Sequence Analysis, DNA ; Sequence Analysis, Protein ; Sequence Homology, Amino Acid</subject><ispartof>Biology of reproduction, 2001-03, Vol.64 (3), p.805-811</ispartof><rights>2001 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=964913$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11207195$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>HYLLNER, Sven Johan</creatorcontrib><creatorcontrib>WESTERLUND, Liselotte</creatorcontrib><creatorcontrib>OLSSON, Per-Erik</creatorcontrib><creatorcontrib>SCHOPEN, Arndt</creatorcontrib><title>Cloning of Rainbow Trout Egg Envelope Proteins: Members of a Unique Group of Structural Proteins</title><title>Biology of reproduction</title><addtitle>Biol Reprod</addtitle><description>All vertebrate eggs are surrounded by an extracellular envelope that protects the egg and is vital for a successful fertilization.
The terminology and functions of the egg envelope vary in different vertebrate groups, but the envelope itself is consistently
composed of a few major proteins that are deposited around the oocyte during oocyte growth. Here, we describe the deduced
amino acid sequences and tissue expression patterns of the three major egg envelope proteins for rainbow trout ( Oncorhynchus mykiss ). All three vitelline envelope proteins (VEPs) are expressed in the livers of both male and female fish, with higher expression
in females. In addition, VEPγ mRNA is also detected in the female gonads. To our knowledge, this is the first time that expression
of a VEP protein gene has been demonstrated to occur in more than one organ. Sequence comparison reveals that all three VEP
proteins share distinct homology with their amphibian, avian, and mammalian counterparts. Whereas mammalian zona pellucida
protein 3 isoforms contain two conserved serines needed for sperm binding, these are not conserved in teleost species, in
which sperm entry is restricted to the micropyle. Besides the difference in VEPγ sperm-binding function, the high sequence
homology suggests that the egg envelope proteins from these distinct vertebrate groups share a common ancestry and form a
unique group of structural proteins.</description><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Blotting, Northern - veterinary</subject><subject>Blotting, Western - veterinary</subject><subject>Cloning, Molecular</subject><subject>DNA Probes - chemistry</subject><subject>Egg Proteins - chemistry</subject><subject>Egg Proteins - genetics</subject><subject>Escherichia coli - genetics</subject><subject>Estradiol - pharmacology</subject><subject>Female</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Library</subject><subject>Holoproteins</subject><subject>Male</subject><subject>Molecular Sequence Data</subject><subject>Oncorhynchus mykiss - physiology</subject><subject>Other proteins</subject><subject>Protein Isoforms</subject><subject>Proteins</subject><subject>Sequence Alignment</subject><subject>Sequence Analysis, DNA</subject><subject>Sequence Analysis, Protein</subject><subject>Sequence Homology, Amino Acid</subject><issn>0006-3363</issn><issn>1529-7268</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo90V1LwzAUBuAgipvTP-CFBETvOvPVNPFOxpzCRNHtuqZbukXSZiatxX9vxuauAuF5Xw7nAHCJ0RAjmd4VxlmvN94tORvSoUDpEejjlMgkI1wcgz5CiCeUctoDZyF8IYQZJfQU9DAmKMMy7YPPkXW1qVfQlfBdmbpwHZx51zZwvFrBcf2jrdto-OZdo00d7uGLrgrtw9YrOK_Nd6vhJAY225-PxreLpvXKHhLn4KRUNuiL_TsA88fxbPSUTF8nz6OHabImPG0Sxkq9VCIjcSzBhESIoFTJlBNGaYmElEpEyGlBldAlQkqRjOMi1SIGSUEH4HbXG_cRZwpNXpmw0NaqWrs25BmXXDBEI7zaw7ao9DLfeFMp_5v_7ySC6z1QYaFs6VW9MOHgJGcSb2tudmptVuvOeJ2HSlkbS2nedR1nOc3jRegf7ix-UA</recordid><startdate>20010301</startdate><enddate>20010301</enddate><creator>HYLLNER, Sven Johan</creator><creator>WESTERLUND, Liselotte</creator><creator>OLSSON, Per-Erik</creator><creator>SCHOPEN, Arndt</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>7X8</scope></search><sort><creationdate>20010301</creationdate><title>Cloning of Rainbow Trout Egg Envelope Proteins: Members of a Unique Group of Structural Proteins</title><author>HYLLNER, Sven Johan ; WESTERLUND, Liselotte ; OLSSON, Per-Erik ; SCHOPEN, Arndt</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-h265t-44feda872719848900205a9562433f0899a826563b3a8ef00aa2761b5e8fed2b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Blotting, Northern - veterinary</topic><topic>Blotting, Western - veterinary</topic><topic>Cloning, Molecular</topic><topic>DNA Probes - chemistry</topic><topic>Egg Proteins - chemistry</topic><topic>Egg Proteins - genetics</topic><topic>Escherichia coli - genetics</topic><topic>Estradiol - pharmacology</topic><topic>Female</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Library</topic><topic>Holoproteins</topic><topic>Male</topic><topic>Molecular Sequence Data</topic><topic>Oncorhynchus mykiss - physiology</topic><topic>Other proteins</topic><topic>Protein Isoforms</topic><topic>Proteins</topic><topic>Sequence Alignment</topic><topic>Sequence Analysis, DNA</topic><topic>Sequence Analysis, Protein</topic><topic>Sequence Homology, Amino Acid</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>HYLLNER, Sven Johan</creatorcontrib><creatorcontrib>WESTERLUND, Liselotte</creatorcontrib><creatorcontrib>OLSSON, Per-Erik</creatorcontrib><creatorcontrib>SCHOPEN, Arndt</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>MEDLINE - Academic</collection><jtitle>Biology of reproduction</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>HYLLNER, Sven Johan</au><au>WESTERLUND, Liselotte</au><au>OLSSON, Per-Erik</au><au>SCHOPEN, Arndt</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cloning of Rainbow Trout Egg Envelope Proteins: Members of a Unique Group of Structural Proteins</atitle><jtitle>Biology of reproduction</jtitle><addtitle>Biol Reprod</addtitle><date>2001-03-01</date><risdate>2001</risdate><volume>64</volume><issue>3</issue><spage>805</spage><epage>811</epage><pages>805-811</pages><issn>0006-3363</issn><eissn>1529-7268</eissn><coden>BIREBV</coden><abstract>All vertebrate eggs are surrounded by an extracellular envelope that protects the egg and is vital for a successful fertilization.
The terminology and functions of the egg envelope vary in different vertebrate groups, but the envelope itself is consistently
composed of a few major proteins that are deposited around the oocyte during oocyte growth. Here, we describe the deduced
amino acid sequences and tissue expression patterns of the three major egg envelope proteins for rainbow trout ( Oncorhynchus mykiss ). All three vitelline envelope proteins (VEPs) are expressed in the livers of both male and female fish, with higher expression
in females. In addition, VEPγ mRNA is also detected in the female gonads. To our knowledge, this is the first time that expression
of a VEP protein gene has been demonstrated to occur in more than one organ. Sequence comparison reveals that all three VEP
proteins share distinct homology with their amphibian, avian, and mammalian counterparts. Whereas mammalian zona pellucida
protein 3 isoforms contain two conserved serines needed for sperm binding, these are not conserved in teleost species, in
which sperm entry is restricted to the micropyle. Besides the difference in VEPγ sperm-binding function, the high sequence
homology suggests that the egg envelope proteins from these distinct vertebrate groups share a common ancestry and form a
unique group of structural proteins.</abstract><cop>Madison, WI</cop><pub>Society for the Study of Reproduction</pub><pmid>11207195</pmid><doi>10.1095/biolreprod64.3.805</doi><tpages>7</tpages></addata></record> |
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source | Oxford University Press Journals All Titles (1996-Current); MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; BioOne Complete |
subjects | Amino Acid Sequence Analytical, structural and metabolic biochemistry Animals Base Sequence Biological and medical sciences Blotting, Northern - veterinary Blotting, Western - veterinary Cloning, Molecular DNA Probes - chemistry Egg Proteins - chemistry Egg Proteins - genetics Escherichia coli - genetics Estradiol - pharmacology Female Fundamental and applied biological sciences. Psychology Gene Library Holoproteins Male Molecular Sequence Data Oncorhynchus mykiss - physiology Other proteins Protein Isoforms Proteins Sequence Alignment Sequence Analysis, DNA Sequence Analysis, Protein Sequence Homology, Amino Acid |
title | Cloning of Rainbow Trout Egg Envelope Proteins: Members of a Unique Group of Structural Proteins |
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