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Egg envelope glycoprotein gp37 as a Xenopus homolog of mammalian ZP1, based on cDNA cloning
The egg envelope is a kind of extracellular matrix, which surrounds growing oocytes, ovulated eggs and early embryos. Among the glycoprotein components of the Xenopus laevis egg envelope, gp43/gp41 and gp69/64 have already been shown to be frog homologs of the mammalian zona pellucida components ZP3...
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Published in: | Development, growth & differentiation growth & differentiation, 2000-08, Vol.42 (4), p.419-427 |
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creator | Kubo, Hideo Kawano, Takehiro Tsubuki, Satoshi Kotani, Masaharu Kawasaki, Hiroshi Kawashima, Seiichi |
description | The egg envelope is a kind of extracellular matrix, which surrounds growing oocytes, ovulated eggs and early embryos. Among the glycoprotein components of the Xenopus laevis egg envelope, gp43/gp41 and gp69/64 have already been shown to be frog homologs of the mammalian zona pellucida components ZP3 and ZP2, respectively. To determine the structure of another major component of egg envelope, gp37, the peptides isolated from the lysyl endopeptidase digests of gp37 were sequenced for amino acids to design degenerate primers for polymerase chain reaction. By reverse transcription–polymerase chain reaction with a poly(A)+ RNA from the ovary of a postovulated female Xenopus, a specifically amplified band was obtained and sequenced. The upstream and downstream sequences of the sequenced region were completed by 5′‐ and 3′‐rapid amplification of cDNA ends, respectively. The gp37 cDNA comprises 1674 bp and contains one open reading frame encoding a polypeptide with 543 amino acids. The predicted amino acid sequence of the gp37 cDNA has a close similarity to that of mammalian ZP1. Northern blot and in situ hybridization studies indicated that the transcript (1.8 kb) is exclusively expressed in the oocytes, particularly in the previtellogenic young oocytes, just like the expression pattern of gp43 mRNA, suggesting a coordinate transcription of the gp43 and gp37 genes in Xenopus. |
doi_str_mv | 10.1046/j.1440-169x.2000.00526.x |
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Among the glycoprotein components of the Xenopus laevis egg envelope, gp43/gp41 and gp69/64 have already been shown to be frog homologs of the mammalian zona pellucida components ZP3 and ZP2, respectively. To determine the structure of another major component of egg envelope, gp37, the peptides isolated from the lysyl endopeptidase digests of gp37 were sequenced for amino acids to design degenerate primers for polymerase chain reaction. By reverse transcription–polymerase chain reaction with a poly(A)+ RNA from the ovary of a postovulated female Xenopus, a specifically amplified band was obtained and sequenced. The upstream and downstream sequences of the sequenced region were completed by 5′‐ and 3′‐rapid amplification of cDNA ends, respectively. The gp37 cDNA comprises 1674 bp and contains one open reading frame encoding a polypeptide with 543 amino acids. The predicted amino acid sequence of the gp37 cDNA has a close similarity to that of mammalian ZP1. Northern blot and in situ hybridization studies indicated that the transcript (1.8 kb) is exclusively expressed in the oocytes, particularly in the previtellogenic young oocytes, just like the expression pattern of gp43 mRNA, suggesting a coordinate transcription of the gp43 and gp37 genes in Xenopus.</description><identifier>ISSN: 0012-1592</identifier><identifier>EISSN: 1440-169X</identifier><identifier>DOI: 10.1046/j.1440-169x.2000.00526.x</identifier><identifier>PMID: 10969742</identifier><language>eng</language><publisher>Melbourne, Australia: Blackwell Science Pty</publisher><subject>Amino Acid Sequence ; Animals ; Base Sequence ; Blotting, Northern ; Cloning, Molecular ; DNA Primers - chemistry ; DNA, Complementary - genetics ; egg envelope ; Egg Proteins - genetics ; Egg Proteins - metabolism ; Female ; glycoprotein gp37 ; gp37 ; In Situ Hybridization ; Mammals ; Membrane Glycoproteins - genetics ; Membrane Glycoproteins - metabolism ; Microscopy, Electron ; Molecular Sequence Data ; Ovary - metabolism ; Ovary - ultrastructure ; Receptors, Cell Surface ; Reverse Transcriptase Polymerase Chain Reaction ; RNA, Messenger - metabolism ; Sequence Homology, Amino Acid ; Vitelline Membrane - metabolism ; Xenopus laevis ; Xenopus laevis - genetics ; Xenopus laevis - metabolism ; Xenopus oocytes ; Zona Pellucida Glycoproteins ; ZP1 homolog ; ZP1 protein</subject><ispartof>Development, growth & differentiation, 2000-08, Vol.42 (4), p.419-427</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4126-13fad15e5fd3275bef9e2027c071d0747abe8448b28c195c5d4135754d956b1f3</citedby><cites>FETCH-LOGICAL-c4126-13fad15e5fd3275bef9e2027c071d0747abe8448b28c195c5d4135754d956b1f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10969742$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kubo, Hideo</creatorcontrib><creatorcontrib>Kawano, Takehiro</creatorcontrib><creatorcontrib>Tsubuki, Satoshi</creatorcontrib><creatorcontrib>Kotani, Masaharu</creatorcontrib><creatorcontrib>Kawasaki, Hiroshi</creatorcontrib><creatorcontrib>Kawashima, Seiichi</creatorcontrib><title>Egg envelope glycoprotein gp37 as a Xenopus homolog of mammalian ZP1, based on cDNA cloning</title><title>Development, growth & differentiation</title><addtitle>Dev Growth Differ</addtitle><description>The egg envelope is a kind of extracellular matrix, which surrounds growing oocytes, ovulated eggs and early embryos. Among the glycoprotein components of the Xenopus laevis egg envelope, gp43/gp41 and gp69/64 have already been shown to be frog homologs of the mammalian zona pellucida components ZP3 and ZP2, respectively. To determine the structure of another major component of egg envelope, gp37, the peptides isolated from the lysyl endopeptidase digests of gp37 were sequenced for amino acids to design degenerate primers for polymerase chain reaction. By reverse transcription–polymerase chain reaction with a poly(A)+ RNA from the ovary of a postovulated female Xenopus, a specifically amplified band was obtained and sequenced. The upstream and downstream sequences of the sequenced region were completed by 5′‐ and 3′‐rapid amplification of cDNA ends, respectively. The gp37 cDNA comprises 1674 bp and contains one open reading frame encoding a polypeptide with 543 amino acids. The predicted amino acid sequence of the gp37 cDNA has a close similarity to that of mammalian ZP1. Northern blot and in situ hybridization studies indicated that the transcript (1.8 kb) is exclusively expressed in the oocytes, particularly in the previtellogenic young oocytes, just like the expression pattern of gp43 mRNA, suggesting a coordinate transcription of the gp43 and gp37 genes in Xenopus.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Blotting, Northern</subject><subject>Cloning, Molecular</subject><subject>DNA Primers - chemistry</subject><subject>DNA, Complementary - genetics</subject><subject>egg envelope</subject><subject>Egg Proteins - genetics</subject><subject>Egg Proteins - metabolism</subject><subject>Female</subject><subject>glycoprotein gp37</subject><subject>gp37</subject><subject>In Situ Hybridization</subject><subject>Mammals</subject><subject>Membrane Glycoproteins - genetics</subject><subject>Membrane Glycoproteins - metabolism</subject><subject>Microscopy, Electron</subject><subject>Molecular Sequence Data</subject><subject>Ovary - metabolism</subject><subject>Ovary - ultrastructure</subject><subject>Receptors, Cell Surface</subject><subject>Reverse Transcriptase Polymerase Chain Reaction</subject><subject>RNA, Messenger - metabolism</subject><subject>Sequence Homology, Amino Acid</subject><subject>Vitelline Membrane - metabolism</subject><subject>Xenopus laevis</subject><subject>Xenopus laevis - genetics</subject><subject>Xenopus laevis - metabolism</subject><subject>Xenopus oocytes</subject><subject>Zona Pellucida Glycoproteins</subject><subject>ZP1 homolog</subject><subject>ZP1 protein</subject><issn>0012-1592</issn><issn>1440-169X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><recordid>eNqNkE1LxDAQhoMoun78BcnJk62ZNGm24EVcv0DUg4LoIaTptHZJm9rs6u6_t-sqePQ0A_PMzMtDCAUWAxPpyTQGIVgEabaIOWMsZkzyNF5skNHv4HmTjBgDHoHM-A7ZDWE6gEIA3yY7wLI0U4KPyOtFVVFsP9D5DmnlltZ3vZ9h3dKqSxQ1gRr6jK3v5oG--cY7X1Ff0sY0jXG1aenLAxzT3AQsqG-pndydUet8W7fVPtkqjQt48FP3yNPlxeP5dXR7f3VzfnYb2SFNGkFSmgIkyrJIuJI5lhlyxpVlCgqmhDI5joUY53xsIZNWFgISqaQoMpnmUCZ75Gh9d0j-Pscw000dLDpnWvTzoEEpASD4AI7XoO19CD2WuuvrxvRLDUyvxOqpXvnTK7F6JVZ_i9WLYfXw58c8b7D4s7g2OQCna-Czdrj892E9uZoMTfIFwfOFoA</recordid><startdate>200008</startdate><enddate>200008</enddate><creator>Kubo, Hideo</creator><creator>Kawano, Takehiro</creator><creator>Tsubuki, Satoshi</creator><creator>Kotani, Masaharu</creator><creator>Kawasaki, Hiroshi</creator><creator>Kawashima, Seiichi</creator><general>Blackwell Science Pty</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>7TM</scope></search><sort><creationdate>200008</creationdate><title>Egg envelope glycoprotein gp37 as a Xenopus homolog of mammalian ZP1, based on cDNA cloning</title><author>Kubo, Hideo ; Kawano, Takehiro ; Tsubuki, Satoshi ; Kotani, Masaharu ; Kawasaki, Hiroshi ; Kawashima, Seiichi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4126-13fad15e5fd3275bef9e2027c071d0747abe8448b28c195c5d4135754d956b1f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Blotting, Northern</topic><topic>Cloning, Molecular</topic><topic>DNA Primers - chemistry</topic><topic>DNA, Complementary - genetics</topic><topic>egg envelope</topic><topic>Egg Proteins - genetics</topic><topic>Egg Proteins - metabolism</topic><topic>Female</topic><topic>glycoprotein gp37</topic><topic>gp37</topic><topic>In Situ Hybridization</topic><topic>Mammals</topic><topic>Membrane Glycoproteins - genetics</topic><topic>Membrane Glycoproteins - metabolism</topic><topic>Microscopy, Electron</topic><topic>Molecular Sequence Data</topic><topic>Ovary - metabolism</topic><topic>Ovary - ultrastructure</topic><topic>Receptors, Cell Surface</topic><topic>Reverse Transcriptase Polymerase Chain Reaction</topic><topic>RNA, Messenger - metabolism</topic><topic>Sequence Homology, Amino Acid</topic><topic>Vitelline Membrane - metabolism</topic><topic>Xenopus laevis</topic><topic>Xenopus laevis - genetics</topic><topic>Xenopus laevis - metabolism</topic><topic>Xenopus oocytes</topic><topic>Zona Pellucida Glycoproteins</topic><topic>ZP1 homolog</topic><topic>ZP1 protein</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kubo, Hideo</creatorcontrib><creatorcontrib>Kawano, Takehiro</creatorcontrib><creatorcontrib>Tsubuki, Satoshi</creatorcontrib><creatorcontrib>Kotani, Masaharu</creatorcontrib><creatorcontrib>Kawasaki, Hiroshi</creatorcontrib><creatorcontrib>Kawashima, Seiichi</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><jtitle>Development, growth & differentiation</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kubo, Hideo</au><au>Kawano, Takehiro</au><au>Tsubuki, Satoshi</au><au>Kotani, Masaharu</au><au>Kawasaki, Hiroshi</au><au>Kawashima, Seiichi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Egg envelope glycoprotein gp37 as a Xenopus homolog of mammalian ZP1, based on cDNA cloning</atitle><jtitle>Development, growth & differentiation</jtitle><addtitle>Dev Growth Differ</addtitle><date>2000-08</date><risdate>2000</risdate><volume>42</volume><issue>4</issue><spage>419</spage><epage>427</epage><pages>419-427</pages><issn>0012-1592</issn><eissn>1440-169X</eissn><abstract>The egg envelope is a kind of extracellular matrix, which surrounds growing oocytes, ovulated eggs and early embryos. Among the glycoprotein components of the Xenopus laevis egg envelope, gp43/gp41 and gp69/64 have already been shown to be frog homologs of the mammalian zona pellucida components ZP3 and ZP2, respectively. To determine the structure of another major component of egg envelope, gp37, the peptides isolated from the lysyl endopeptidase digests of gp37 were sequenced for amino acids to design degenerate primers for polymerase chain reaction. By reverse transcription–polymerase chain reaction with a poly(A)+ RNA from the ovary of a postovulated female Xenopus, a specifically amplified band was obtained and sequenced. The upstream and downstream sequences of the sequenced region were completed by 5′‐ and 3′‐rapid amplification of cDNA ends, respectively. The gp37 cDNA comprises 1674 bp and contains one open reading frame encoding a polypeptide with 543 amino acids. The predicted amino acid sequence of the gp37 cDNA has a close similarity to that of mammalian ZP1. Northern blot and in situ hybridization studies indicated that the transcript (1.8 kb) is exclusively expressed in the oocytes, particularly in the previtellogenic young oocytes, just like the expression pattern of gp43 mRNA, suggesting a coordinate transcription of the gp43 and gp37 genes in Xenopus.</abstract><cop>Melbourne, Australia</cop><pub>Blackwell Science Pty</pub><pmid>10969742</pmid><doi>10.1046/j.1440-169x.2000.00526.x</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Amino Acid Sequence Animals Base Sequence Blotting, Northern Cloning, Molecular DNA Primers - chemistry DNA, Complementary - genetics egg envelope Egg Proteins - genetics Egg Proteins - metabolism Female glycoprotein gp37 gp37 In Situ Hybridization Mammals Membrane Glycoproteins - genetics Membrane Glycoproteins - metabolism Microscopy, Electron Molecular Sequence Data Ovary - metabolism Ovary - ultrastructure Receptors, Cell Surface Reverse Transcriptase Polymerase Chain Reaction RNA, Messenger - metabolism Sequence Homology, Amino Acid Vitelline Membrane - metabolism Xenopus laevis Xenopus laevis - genetics Xenopus laevis - metabolism Xenopus oocytes Zona Pellucida Glycoproteins ZP1 homolog ZP1 protein |
title | Egg envelope glycoprotein gp37 as a Xenopus homolog of mammalian ZP1, based on cDNA cloning |
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