Identification and structural characterization of the 75-kDa rabbit zona pellucida protein

A cDNA (rc75) encoding a 75-kDa rabbit zona pellucida (ZP) glycoprotein (R75) has been cloned and sequenced. The predicted amino acid sequence consists of 676 amino acids including seven potential N-glycosylation sites. The cDNA hybridizes to a 2.4-kilobase mRNA in ovary that is not detectable in ot...

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Veröffentlicht in:The Journal of biological chemistry 1993-06, Vol.268 (17), p.12412-12417
Hauptverfasser: Lee, V H, Schwoebel, E, Prasad, S, Cheung, P, Timmons, T M, Cook, R, Dunbar, B S
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container_end_page 12417
container_issue 17
container_start_page 12412
container_title The Journal of biological chemistry
container_volume 268
creator Lee, V H
Schwoebel, E
Prasad, S
Cheung, P
Timmons, T M
Cook, R
Dunbar, B S
description A cDNA (rc75) encoding a 75-kDa rabbit zona pellucida (ZP) glycoprotein (R75) has been cloned and sequenced. The predicted amino acid sequence consists of 676 amino acids including seven potential N-glycosylation sites. The cDNA hybridizes to a 2.4-kilobase mRNA in ovary that is not detectable in other rabbit tissues. The R75 mRNA was also found to be expressed during the early stages of rabbit ovarian development (2-6 weeks of age) when the ovary contains primordial, primary, and early secondary follicles. The deduced amino acid sequence of rc75 has 77% similarity to the mouse ZP2 protein but no similarity to mouse ZP3. R75 also contains regions with 35-55% similarity to a previously cloned rabbit 55-kDa ZP protein. Monte Carlo simulation comparison confirmed that R75 has a significant probability of homology with mouse ZP2 and the rabbit 55-kDa ZP protein. Antibodies were developed against a fragment of R75 (rc75a cDNA) expressed in the pEX expression vector. These antibodies were used to confirm that the expressed protein contained epitopes found in the native rabbit ZP glycoprotein. These data suggest that some, but not all, ZP proteins may be conserved among different species and that within a species ZP proteins may share similar regions.
doi_str_mv 10.1016/s0021-9258(18)31405-4
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Schwoebel, E ; Prasad, S ; Cheung, P ; Timmons, T M ; Cook, R ; Dunbar, B S</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c477t-ee2df792e89e679e63f6b7e757eb9ec63d4492edd98fd287dc16e8baccfefdac3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Aging - metabolism</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>antigenic determinants</topic><topic>Base Sequence</topic><topic>Blotting, Northern</topic><topic>cDNA</topic><topic>Cloning, Molecular</topic><topic>DNA</topic><topic>Egg Proteins</topic><topic>Female</topic><topic>genes</topic><topic>Membrane Glycoproteins - chemistry</topic><topic>Membrane Glycoproteins - genetics</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>nucleotide sequence</topic><topic>Ovary - growth &amp; development</topic><topic>Ovary - metabolism</topic><topic>predictions</topic><topic>Protein Structure, Secondary</topic><topic>Rabbits</topic><topic>Receptors, Cell Surface</topic><topic>Recombinant Proteins - chemistry</topic><topic>RNA - metabolism</topic><topic>RNA, Messenger - analysis</topic><topic>RNA, Messenger - metabolism</topic><topic>Sequence Homology, Amino Acid</topic><topic>Zona Pellucida - chemistry</topic><topic>Zona Pellucida Glycoproteins</topic><topic>zona pellucida protein</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lee, V H</creatorcontrib><creatorcontrib>Schwoebel, E</creatorcontrib><creatorcontrib>Prasad, S</creatorcontrib><creatorcontrib>Cheung, P</creatorcontrib><creatorcontrib>Timmons, T M</creatorcontrib><creatorcontrib>Cook, R</creatorcontrib><creatorcontrib>Dunbar, B S</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lee, V H</au><au>Schwoebel, E</au><au>Prasad, S</au><au>Cheung, P</au><au>Timmons, T M</au><au>Cook, R</au><au>Dunbar, B S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification and structural characterization of the 75-kDa rabbit zona pellucida protein</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1993-06-15</date><risdate>1993</risdate><volume>268</volume><issue>17</issue><spage>12412</spage><epage>12417</epage><pages>12412-12417</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>A cDNA (rc75) encoding a 75-kDa rabbit zona pellucida (ZP) glycoprotein (R75) has been cloned and sequenced. The predicted amino acid sequence consists of 676 amino acids including seven potential N-glycosylation sites. The cDNA hybridizes to a 2.4-kilobase mRNA in ovary that is not detectable in other rabbit tissues. The R75 mRNA was also found to be expressed during the early stages of rabbit ovarian development (2-6 weeks of age) when the ovary contains primordial, primary, and early secondary follicles. The deduced amino acid sequence of rc75 has 77% similarity to the mouse ZP2 protein but no similarity to mouse ZP3. R75 also contains regions with 35-55% similarity to a previously cloned rabbit 55-kDa ZP protein. Monte Carlo simulation comparison confirmed that R75 has a significant probability of homology with mouse ZP2 and the rabbit 55-kDa ZP protein. Antibodies were developed against a fragment of R75 (rc75a cDNA) expressed in the pEX expression vector. These antibodies were used to confirm that the expressed protein contained epitopes found in the native rabbit ZP glycoprotein. 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source MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection
subjects Aging - metabolism
Amino Acid Sequence
Animals
antigenic determinants
Base Sequence
Blotting, Northern
cDNA
Cloning, Molecular
DNA
Egg Proteins
Female
genes
Membrane Glycoproteins - chemistry
Membrane Glycoproteins - genetics
Molecular Sequence Data
Molecular Weight
nucleotide sequence
Ovary - growth & development
Ovary - metabolism
predictions
Protein Structure, Secondary
Rabbits
Receptors, Cell Surface
Recombinant Proteins - chemistry
RNA - metabolism
RNA, Messenger - analysis
RNA, Messenger - metabolism
Sequence Homology, Amino Acid
Zona Pellucida - chemistry
Zona Pellucida Glycoproteins
zona pellucida protein
title Identification and structural characterization of the 75-kDa rabbit zona pellucida protein
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