Cloning and characterization of a human Mac-2-binding protein, a new member of the superfamily defined by the macrophage scavenger receptor cysteine-rich domain
We have purified and sequenced a secreted glycoprotein from both the human breast carcinoma cell line, SK-BR-3, and human breast milk. The native protein binds specifically to a human macrophage-associated lectin known as Mac-2. This Mac-2 binding protein (Mac-2-BP) has an apparent native molecular...
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| Veröffentlicht in: | The Journal of biological chemistry 1993-07, Vol.268 (19), p.14245-14249 |
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| container_title | The Journal of biological chemistry |
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| creator | KOTHS, K TAYLOR, E HALENBECK, R CASIPIT, C WANG, A |
| description | We have purified and sequenced a secreted glycoprotein from both the human breast carcinoma cell line, SK-BR-3, and human
breast milk. The native protein binds specifically to a human macrophage-associated lectin known as Mac-2. This Mac-2 binding
protein (Mac-2-BP) has an apparent native molecular mass of several million daltons and contains subunits of 85-97 kDa that
are very susceptible to proteolysis at a dibasic cleavage site. Western analysis suggests that Mac-2-BP is found in serum,
semen, saliva, urine, and tears, in addition to breast milk. The gene encoding Mac-2-BP was cloned from a cDNA bank of a human
monocytic cell line, using degenerate PCR primers based on the protein sequence. Recombinant Mac-2-BP was expressed in Cos
cells and secreted as a high molecular weight complex. The cDNA clone encodes a mature protein of 567 amino acids, preceded
by an 18-amino acid leader. The mature protein contains 16 cysteines and has seven potential N-linked glycosylation sites.
The first 106 amino acids represent a domain that is highly similar to an ancient protein superfamily defined by the macrophage
scavenger receptor cysteine-rich domain. |
| doi_str_mv | 10.1016/s0021-9258(19)85233-x |
| format | Article |
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breast milk. The native protein binds specifically to a human macrophage-associated lectin known as Mac-2. This Mac-2 binding
protein (Mac-2-BP) has an apparent native molecular mass of several million daltons and contains subunits of 85-97 kDa that
are very susceptible to proteolysis at a dibasic cleavage site. Western analysis suggests that Mac-2-BP is found in serum,
semen, saliva, urine, and tears, in addition to breast milk. The gene encoding Mac-2-BP was cloned from a cDNA bank of a human
monocytic cell line, using degenerate PCR primers based on the protein sequence. Recombinant Mac-2-BP was expressed in Cos
cells and secreted as a high molecular weight complex. The cDNA clone encodes a mature protein of 567 amino acids, preceded
by an 18-amino acid leader. The mature protein contains 16 cysteines and has seven potential N-linked glycosylation sites.
The first 106 amino acids represent a domain that is highly similar to an ancient protein superfamily defined by the macrophage
scavenger receptor cysteine-rich domain.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/s0021-9258(19)85233-x</identifier><identifier>PMID: 8390986</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>Amino Acid Sequence ; Analytical, structural and metabolic biochemistry ; Animals ; Antigens, Neoplasm ; Base Sequence ; Binding and carrier proteins ; Biological and medical sciences ; Biomarkers, Tumor ; Breast Neoplasms ; Carrier Proteins - biosynthesis ; Carrier Proteins - genetics ; Carrier Proteins - isolation & purification ; Cell Line ; Cloning, Molecular - methods ; Cysteine ; DNA ; Female ; Fundamental and applied biological sciences. Psychology ; Gene Library ; Glycoproteins - biosynthesis ; Glycoproteins - genetics ; Glycoproteins - isolation & purification ; Humans ; Milk, Human - metabolism ; Molecular Sequence Data ; Monocytes ; Multigene Family ; Oligodeoxyribonucleotides ; Proteins ; Receptors, Cell Surface - genetics ; Receptors, Immunologic ; Receptors, Scavenger ; Recombinant Proteins - biosynthesis ; Recombinant Proteins - isolation & purification ; Sequence Homology, Amino Acid ; Transfection ; Tumor Cells, Cultured</subject><ispartof>The Journal of biological chemistry, 1993-07, Vol.268 (19), p.14245-14249</ispartof><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c506t-7e5fc230470f7d09da38af158f9b5e591cec6c6c8a34a9e5fc18c50a65de29aa3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4839217$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8390986$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>KOTHS, K</creatorcontrib><creatorcontrib>TAYLOR, E</creatorcontrib><creatorcontrib>HALENBECK, R</creatorcontrib><creatorcontrib>CASIPIT, C</creatorcontrib><creatorcontrib>WANG, A</creatorcontrib><title>Cloning and characterization of a human Mac-2-binding protein, a new member of the superfamily defined by the macrophage scavenger receptor cysteine-rich domain</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>We have purified and sequenced a secreted glycoprotein from both the human breast carcinoma cell line, SK-BR-3, and human
breast milk. The native protein binds specifically to a human macrophage-associated lectin known as Mac-2. This Mac-2 binding
protein (Mac-2-BP) has an apparent native molecular mass of several million daltons and contains subunits of 85-97 kDa that
are very susceptible to proteolysis at a dibasic cleavage site. Western analysis suggests that Mac-2-BP is found in serum,
semen, saliva, urine, and tears, in addition to breast milk. The gene encoding Mac-2-BP was cloned from a cDNA bank of a human
monocytic cell line, using degenerate PCR primers based on the protein sequence. Recombinant Mac-2-BP was expressed in Cos
cells and secreted as a high molecular weight complex. The cDNA clone encodes a mature protein of 567 amino acids, preceded
by an 18-amino acid leader. The mature protein contains 16 cysteines and has seven potential N-linked glycosylation sites.
The first 106 amino acids represent a domain that is highly similar to an ancient protein superfamily defined by the macrophage
scavenger receptor cysteine-rich domain.</description><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Antigens, Neoplasm</subject><subject>Base Sequence</subject><subject>Binding and carrier proteins</subject><subject>Biological and medical sciences</subject><subject>Biomarkers, Tumor</subject><subject>Breast Neoplasms</subject><subject>Carrier Proteins - biosynthesis</subject><subject>Carrier Proteins - genetics</subject><subject>Carrier Proteins - isolation & purification</subject><subject>Cell Line</subject><subject>Cloning, Molecular - methods</subject><subject>Cysteine</subject><subject>DNA</subject><subject>Female</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Library</subject><subject>Glycoproteins - biosynthesis</subject><subject>Glycoproteins - genetics</subject><subject>Glycoproteins - isolation & purification</subject><subject>Humans</subject><subject>Milk, Human - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Monocytes</subject><subject>Multigene Family</subject><subject>Oligodeoxyribonucleotides</subject><subject>Proteins</subject><subject>Receptors, Cell Surface - genetics</subject><subject>Receptors, Immunologic</subject><subject>Receptors, Scavenger</subject><subject>Recombinant Proteins - biosynthesis</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>Sequence Homology, Amino Acid</subject><subject>Transfection</subject><subject>Tumor Cells, Cultured</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc2O1DAQhCMEWoaFR1jJB4RAImDHcWIf0Yg_aREHQNqb1XHaE6PYGeyEZXgaHhVndjQcsQ8-1FfValdRXDH6ilHWvE6UVqxUlZDPmXohRcV5-etesWFU8pILdnO_2JyRh8WjlL7TfGrFLooLyRVVstkUf7bjFFzYEQg9MQNEMDNG9xtmNwUyWQJkWDwE8glMWZWdC_1K7-M0owsvsxzwlnj0HcYVnwckadljtODdeCA9WhewJ93hKHkwcdoPsMuUgZ8YdtkW0eB-niIxh7SmYhmdGUg_eXDhcfHAwpjwyem9LL69e_t1-6G8_vz-4_bNdWkEbeayRWFNxWndUtv2VPXAJVgmpFWdQKGYQdPkK4HXoFaYyeyERvRYKQB-WTy7y82r_Vgwzdq7ZHAcIeC0JN0KyXJc81-QNbKRirMMijswr5xSRKv30XmIB82oXivUX9Z-9NqPZkofK9Q32Xd1GrB0Hvuz69RZ1p-edMh_ONoIwbh0xurMVaz9hw1uN9y6iLpzkxnQ66o5zmN1VQv-F-jos1E</recordid><startdate>19930705</startdate><enddate>19930705</enddate><creator>KOTHS, K</creator><creator>TAYLOR, E</creator><creator>HALENBECK, R</creator><creator>CASIPIT, C</creator><creator>WANG, A</creator><general>American Society for Biochemistry and Molecular Biology</general><scope>IQODW</scope><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>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19930705</creationdate><title>Cloning and characterization of a human Mac-2-binding protein, a new member of the superfamily defined by the macrophage scavenger receptor cysteine-rich domain</title><author>KOTHS, K ; TAYLOR, E ; HALENBECK, R ; CASIPIT, C ; WANG, A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c506t-7e5fc230470f7d09da38af158f9b5e591cec6c6c8a34a9e5fc18c50a65de29aa3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Antigens, Neoplasm</topic><topic>Base Sequence</topic><topic>Binding and carrier proteins</topic><topic>Biological and medical sciences</topic><topic>Biomarkers, Tumor</topic><topic>Breast Neoplasms</topic><topic>Carrier Proteins - biosynthesis</topic><topic>Carrier Proteins - genetics</topic><topic>Carrier Proteins - isolation & purification</topic><topic>Cell Line</topic><topic>Cloning, Molecular - methods</topic><topic>Cysteine</topic><topic>DNA</topic><topic>Female</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Library</topic><topic>Glycoproteins - biosynthesis</topic><topic>Glycoproteins - genetics</topic><topic>Glycoproteins - isolation & purification</topic><topic>Humans</topic><topic>Milk, Human - metabolism</topic><topic>Molecular Sequence Data</topic><topic>Monocytes</topic><topic>Multigene Family</topic><topic>Oligodeoxyribonucleotides</topic><topic>Proteins</topic><topic>Receptors, Cell Surface - genetics</topic><topic>Receptors, Immunologic</topic><topic>Receptors, Scavenger</topic><topic>Recombinant Proteins - biosynthesis</topic><topic>Recombinant Proteins - isolation & purification</topic><topic>Sequence Homology, Amino Acid</topic><topic>Transfection</topic><topic>Tumor Cells, Cultured</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>KOTHS, K</creatorcontrib><creatorcontrib>TAYLOR, E</creatorcontrib><creatorcontrib>HALENBECK, R</creatorcontrib><creatorcontrib>CASIPIT, C</creatorcontrib><creatorcontrib>WANG, A</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>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</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>KOTHS, K</au><au>TAYLOR, E</au><au>HALENBECK, R</au><au>CASIPIT, C</au><au>WANG, A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cloning and characterization of a human Mac-2-binding protein, a new member of the superfamily defined by the macrophage scavenger receptor cysteine-rich domain</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1993-07-05</date><risdate>1993</risdate><volume>268</volume><issue>19</issue><spage>14245</spage><epage>14249</epage><pages>14245-14249</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>We have purified and sequenced a secreted glycoprotein from both the human breast carcinoma cell line, SK-BR-3, and human
breast milk. The native protein binds specifically to a human macrophage-associated lectin known as Mac-2. This Mac-2 binding
protein (Mac-2-BP) has an apparent native molecular mass of several million daltons and contains subunits of 85-97 kDa that
are very susceptible to proteolysis at a dibasic cleavage site. Western analysis suggests that Mac-2-BP is found in serum,
semen, saliva, urine, and tears, in addition to breast milk. The gene encoding Mac-2-BP was cloned from a cDNA bank of a human
monocytic cell line, using degenerate PCR primers based on the protein sequence. Recombinant Mac-2-BP was expressed in Cos
cells and secreted as a high molecular weight complex. The cDNA clone encodes a mature protein of 567 amino acids, preceded
by an 18-amino acid leader. The mature protein contains 16 cysteines and has seven potential N-linked glycosylation sites.
The first 106 amino acids represent a domain that is highly similar to an ancient protein superfamily defined by the macrophage
scavenger receptor cysteine-rich domain.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>8390986</pmid><doi>10.1016/s0021-9258(19)85233-x</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1993-07, Vol.268 (19), p.14245-14249 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_75811586 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Analytical, structural and metabolic biochemistry Animals Antigens, Neoplasm Base Sequence Binding and carrier proteins Biological and medical sciences Biomarkers, Tumor Breast Neoplasms Carrier Proteins - biosynthesis Carrier Proteins - genetics Carrier Proteins - isolation & purification Cell Line Cloning, Molecular - methods Cysteine DNA Female Fundamental and applied biological sciences. Psychology Gene Library Glycoproteins - biosynthesis Glycoproteins - genetics Glycoproteins - isolation & purification Humans Milk, Human - metabolism Molecular Sequence Data Monocytes Multigene Family Oligodeoxyribonucleotides Proteins Receptors, Cell Surface - genetics Receptors, Immunologic Receptors, Scavenger Recombinant Proteins - biosynthesis Recombinant Proteins - isolation & purification Sequence Homology, Amino Acid Transfection Tumor Cells, Cultured |
| title | Cloning and characterization of a human Mac-2-binding protein, a new member of the superfamily defined by the macrophage scavenger receptor cysteine-rich domain |
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