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Fetal Globin Expression in New World Monkeys
Reverse phase chromatography of the globin chains of adult, newborn, and fetal erythrocytes from three species of New World monkeys ( Cebus apella, Aotus azarae, and Callithrix jacchus ) representing three of the seven platyrrhine clades showed that γ-globin expression was fetal in these animals. T...
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Published in: | The Journal of biological chemistry 1996-06, Vol.271 (25), p.14684-14691 |
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container_end_page | 14691 |
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container_start_page | 14684 |
container_title | The Journal of biological chemistry |
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creator | Johnson, R M Buck, S Chiu, C Schneider, H Sampaio, I Gage, D A Shen, T L Schneider, M P Muniz, J A Gumucio, D L Goodman, M |
description | Reverse phase chromatography of the globin chains of adult, newborn, and fetal erythrocytes from three species of New World
monkeys ( Cebus apella, Aotus azarae, and Callithrix jacchus ) representing three of the seven platyrrhine clades showed that γ-globin expression was fetal in these animals. The globins
were identified by a combination of chemical sequencing and mass spectrometric analysis. Since γ-globin expression is fetal
in the other major simian branch, the catarrhines, but embryonic in prosimian primates and nonprimate placental mammals, the
evolution of fetal recruitment can now be assigned to the period between the simian-prosimian divergence (55 million years
ago) and the platyrrhine-catarrhine divergence (35 million years ago). The γ-globin gene underwent tandem duplication during
the same evolutionary epoch, in accord with a model that suggests that the downstream duplicated γ-gene (γ2) was free to acquire
the mutations necessary for fetal recruitment. Mass spectrometric analysis of tryptic digests of the γ-globins verified the
amino acid sequences deduced from genomic sequencing. Detailed analysis of high performance liquid chromatography and matrix-assisted
laser desorption/ionization mass spectrometry data showed that γ2-globin in Cebus was expressed to a far greater extent than γ1-globin, supporting inferences drawn from a study of the promoter sequences.
A âpre-γâ-globin was observed in C. apella and shown to be primarily the glutathionyl adduct. The other species, A. azarae and C. jacchus, also express only one γ-globin polypeptide. This work provides biochemical evidence of an evolutionary trend in the platyrrhines
to alter the duplicated γ-globin gene locus so that only one γ-globin polypeptide is expressed. |
doi_str_mv | 10.1074/jbc.271.25.14684 |
format | article |
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monkeys ( Cebus apella, Aotus azarae, and Callithrix jacchus ) representing three of the seven platyrrhine clades showed that γ-globin expression was fetal in these animals. The globins
were identified by a combination of chemical sequencing and mass spectrometric analysis. Since γ-globin expression is fetal
in the other major simian branch, the catarrhines, but embryonic in prosimian primates and nonprimate placental mammals, the
evolution of fetal recruitment can now be assigned to the period between the simian-prosimian divergence (55 million years
ago) and the platyrrhine-catarrhine divergence (35 million years ago). The γ-globin gene underwent tandem duplication during
the same evolutionary epoch, in accord with a model that suggests that the downstream duplicated γ-gene (γ2) was free to acquire
the mutations necessary for fetal recruitment. Mass spectrometric analysis of tryptic digests of the γ-globins verified the
amino acid sequences deduced from genomic sequencing. Detailed analysis of high performance liquid chromatography and matrix-assisted
laser desorption/ionization mass spectrometry data showed that γ2-globin in Cebus was expressed to a far greater extent than γ1-globin, supporting inferences drawn from a study of the promoter sequences.
A âpre-γâ-globin was observed in C. apella and shown to be primarily the glutathionyl adduct. The other species, A. azarae and C. jacchus, also express only one γ-globin polypeptide. This work provides biochemical evidence of an evolutionary trend in the platyrrhines
to alter the duplicated γ-globin gene locus so that only one γ-globin polypeptide is expressed.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.271.25.14684</identifier><identifier>PMID: 8663037</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Abortion, Veterinary ; Amino Acid Sequence ; Animals ; Animals, Newborn ; Aotus trivirgatus ; Biological Evolution ; Callithrix ; Callithrix jacchus ; Cebus ; Cebus apella ; Cercopithecidae ; Chromatography, High Pressure Liquid ; Cyanogen Bromide ; Female ; Fetus ; Globins - biosynthesis ; Globins - chemistry ; Humans ; Molecular Sequence Data ; Peptide Fragments - chemistry ; Pregnancy ; Sequence Homology, Amino Acid ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Strepsirhini ; Trypsin</subject><ispartof>The Journal of biological chemistry, 1996-06, Vol.271 (25), p.14684-14691</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c398t-698380e42670e1c84d200280c14525eacbc6769fab8e63a100fdd2209b5e90723</citedby><cites>FETCH-LOGICAL-c398t-698380e42670e1c84d200280c14525eacbc6769fab8e63a100fdd2209b5e90723</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,27905,27906</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8663037$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Johnson, R M</creatorcontrib><creatorcontrib>Buck, S</creatorcontrib><creatorcontrib>Chiu, C</creatorcontrib><creatorcontrib>Schneider, H</creatorcontrib><creatorcontrib>Sampaio, I</creatorcontrib><creatorcontrib>Gage, D A</creatorcontrib><creatorcontrib>Shen, T L</creatorcontrib><creatorcontrib>Schneider, M P</creatorcontrib><creatorcontrib>Muniz, J A</creatorcontrib><creatorcontrib>Gumucio, D L</creatorcontrib><creatorcontrib>Goodman, M</creatorcontrib><title>Fetal Globin Expression in New World Monkeys</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Reverse phase chromatography of the globin chains of adult, newborn, and fetal erythrocytes from three species of New World
monkeys ( Cebus apella, Aotus azarae, and Callithrix jacchus ) representing three of the seven platyrrhine clades showed that γ-globin expression was fetal in these animals. The globins
were identified by a combination of chemical sequencing and mass spectrometric analysis. Since γ-globin expression is fetal
in the other major simian branch, the catarrhines, but embryonic in prosimian primates and nonprimate placental mammals, the
evolution of fetal recruitment can now be assigned to the period between the simian-prosimian divergence (55 million years
ago) and the platyrrhine-catarrhine divergence (35 million years ago). The γ-globin gene underwent tandem duplication during
the same evolutionary epoch, in accord with a model that suggests that the downstream duplicated γ-gene (γ2) was free to acquire
the mutations necessary for fetal recruitment. Mass spectrometric analysis of tryptic digests of the γ-globins verified the
amino acid sequences deduced from genomic sequencing. Detailed analysis of high performance liquid chromatography and matrix-assisted
laser desorption/ionization mass spectrometry data showed that γ2-globin in Cebus was expressed to a far greater extent than γ1-globin, supporting inferences drawn from a study of the promoter sequences.
A âpre-γâ-globin was observed in C. apella and shown to be primarily the glutathionyl adduct. The other species, A. azarae and C. jacchus, also express only one γ-globin polypeptide. This work provides biochemical evidence of an evolutionary trend in the platyrrhines
to alter the duplicated γ-globin gene locus so that only one γ-globin polypeptide is expressed.</description><subject>Abortion, Veterinary</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Animals, Newborn</subject><subject>Aotus trivirgatus</subject><subject>Biological Evolution</subject><subject>Callithrix</subject><subject>Callithrix jacchus</subject><subject>Cebus</subject><subject>Cebus apella</subject><subject>Cercopithecidae</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Cyanogen Bromide</subject><subject>Female</subject><subject>Fetus</subject><subject>Globins - biosynthesis</subject><subject>Globins - chemistry</subject><subject>Humans</subject><subject>Molecular Sequence Data</subject><subject>Peptide Fragments - chemistry</subject><subject>Pregnancy</subject><subject>Sequence Homology, Amino Acid</subject><subject>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</subject><subject>Strepsirhini</subject><subject>Trypsin</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><recordid>eNqFkD1PwzAQhi0EKuVjZ0HKgJhIONuxY4-oagtSgQUEm5U4F5qSNMVuVfrvMbRCYuKW0-n90Okh5IxCQiFLr2eFTVhGEyYSmkqV7pE-BcVjLujrPukDMBprJtQhOfJ-BmFSTXukp6TkwLM-uRrhMm-icdMV9Twafi4cel938yhcD7iOXjrXlNF9N3_HjT8hB1XeeDzd7WPyPBo-DW7jyeP4bnAziS3XahlLrbgCTJnMAKlVacnCIwosTQUTmNvCykzqKi8USp5TgKosGQNdCNSQMX5MLre9C9d9rNAvTVt7i02Tz7FbeZMpypnO6L9GKoTWMoVghK3Rus57h5VZuLrN3cZQMN8kTSBpAknDhPkhGSLnu-5V0WL5G9ihC_rFVp_Wb9N17dAUdWen2P6t-QKAOHgZ</recordid><startdate>19960621</startdate><enddate>19960621</enddate><creator>Johnson, R M</creator><creator>Buck, S</creator><creator>Chiu, C</creator><creator>Schneider, H</creator><creator>Sampaio, I</creator><creator>Gage, D A</creator><creator>Shen, T L</creator><creator>Schneider, M P</creator><creator>Muniz, J A</creator><creator>Gumucio, D L</creator><creator>Goodman, M</creator><general>American Society for Biochemistry and Molecular Biology</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><scope>7X8</scope></search><sort><creationdate>19960621</creationdate><title>Fetal Globin Expression in New World Monkeys</title><author>Johnson, R M ; Buck, S ; Chiu, C ; Schneider, H ; Sampaio, I ; Gage, D A ; Shen, T L ; Schneider, M P ; Muniz, J A ; Gumucio, D L ; Goodman, M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c398t-698380e42670e1c84d200280c14525eacbc6769fab8e63a100fdd2209b5e90723</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Abortion, Veterinary</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Animals, Newborn</topic><topic>Aotus trivirgatus</topic><topic>Biological Evolution</topic><topic>Callithrix</topic><topic>Callithrix jacchus</topic><topic>Cebus</topic><topic>Cebus apella</topic><topic>Cercopithecidae</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Cyanogen Bromide</topic><topic>Female</topic><topic>Fetus</topic><topic>Globins - biosynthesis</topic><topic>Globins - chemistry</topic><topic>Humans</topic><topic>Molecular Sequence Data</topic><topic>Peptide Fragments - chemistry</topic><topic>Pregnancy</topic><topic>Sequence Homology, Amino Acid</topic><topic>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</topic><topic>Strepsirhini</topic><topic>Trypsin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Johnson, R M</creatorcontrib><creatorcontrib>Buck, S</creatorcontrib><creatorcontrib>Chiu, C</creatorcontrib><creatorcontrib>Schneider, H</creatorcontrib><creatorcontrib>Sampaio, I</creatorcontrib><creatorcontrib>Gage, D A</creatorcontrib><creatorcontrib>Shen, T L</creatorcontrib><creatorcontrib>Schneider, M P</creatorcontrib><creatorcontrib>Muniz, J A</creatorcontrib><creatorcontrib>Gumucio, D L</creatorcontrib><creatorcontrib>Goodman, M</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><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Johnson, R M</au><au>Buck, S</au><au>Chiu, C</au><au>Schneider, H</au><au>Sampaio, I</au><au>Gage, D A</au><au>Shen, T L</au><au>Schneider, M P</au><au>Muniz, J A</au><au>Gumucio, D L</au><au>Goodman, M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Fetal Globin Expression in New World Monkeys</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1996-06-21</date><risdate>1996</risdate><volume>271</volume><issue>25</issue><spage>14684</spage><epage>14691</epage><pages>14684-14691</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Reverse phase chromatography of the globin chains of adult, newborn, and fetal erythrocytes from three species of New World
monkeys ( Cebus apella, Aotus azarae, and Callithrix jacchus ) representing three of the seven platyrrhine clades showed that γ-globin expression was fetal in these animals. The globins
were identified by a combination of chemical sequencing and mass spectrometric analysis. Since γ-globin expression is fetal
in the other major simian branch, the catarrhines, but embryonic in prosimian primates and nonprimate placental mammals, the
evolution of fetal recruitment can now be assigned to the period between the simian-prosimian divergence (55 million years
ago) and the platyrrhine-catarrhine divergence (35 million years ago). The γ-globin gene underwent tandem duplication during
the same evolutionary epoch, in accord with a model that suggests that the downstream duplicated γ-gene (γ2) was free to acquire
the mutations necessary for fetal recruitment. Mass spectrometric analysis of tryptic digests of the γ-globins verified the
amino acid sequences deduced from genomic sequencing. Detailed analysis of high performance liquid chromatography and matrix-assisted
laser desorption/ionization mass spectrometry data showed that γ2-globin in Cebus was expressed to a far greater extent than γ1-globin, supporting inferences drawn from a study of the promoter sequences.
A âpre-γâ-globin was observed in C. apella and shown to be primarily the glutathionyl adduct. The other species, A. azarae and C. jacchus, also express only one γ-globin polypeptide. This work provides biochemical evidence of an evolutionary trend in the platyrrhines
to alter the duplicated γ-globin gene locus so that only one γ-globin polypeptide is expressed.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>8663037</pmid><doi>10.1074/jbc.271.25.14684</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Abortion, Veterinary Amino Acid Sequence Animals Animals, Newborn Aotus trivirgatus Biological Evolution Callithrix Callithrix jacchus Cebus Cebus apella Cercopithecidae Chromatography, High Pressure Liquid Cyanogen Bromide Female Fetus Globins - biosynthesis Globins - chemistry Humans Molecular Sequence Data Peptide Fragments - chemistry Pregnancy Sequence Homology, Amino Acid Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Strepsirhini Trypsin |
title | Fetal Globin Expression in New World Monkeys |
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