cDNA Cloning and Characterization of Human Monocyte/Macrophage Serine Esterase-1
Human monocyte/macrophage serine esterase (HMSE), commonly known as acid esterase or α-naphthylacetate esterase, comprises a group of five enzyme variants that can be distinguished by their isoelectric points from esterase variants of the other normal human blood cell populations. A cDNA for one of...
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| Veröffentlicht in: | Blood 1991-07, Vol.78 (2), p.506-512 |
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| creator | Zschunke, F. Salmassi, A. Kreipe, H. Buck, F. Parwaresch, M.R. Radzun, H.J. |
| description | Human monocyte/macrophage serine esterase (HMSE), commonly known as acid esterase or α-naphthylacetate esterase, comprises a group of five enzyme variants that can be distinguished by their isoelectric points from esterase variants of the other normal human blood cell populations. A cDNA for one of the monocytic enzyme variants (HMSE1) was cloned from a U-937 λgt11 cDNA library by screening with an oligonucleotide mixture designed according to amino acid sequence data of the purified enzyme. The cDNA contains 1,727 bp with an open reading frame of 1,512 bp coding for a protein of 503 amino acid residues. HMSE1 cDNA represents the first cloned monocyte/macrophage-specific serine esterase and its sequence shows up to 77% homology to other known serine esterases of different species. The amino acid composition of the putative active site of HMSE1 as deduced from the nucleotide sequence corresponds with the active sites of other serine esterases but not with the active sites of serine proteases. Hybridization of the cDNA with RNA of separated normal blood cell populations and hematopoietic cell lines shows restricted expression within the monocyte/macrophage lineage. |
| doi_str_mv | 10.1182/blood.V78.2.506.506 |
| format | Article |
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A cDNA for one of the monocytic enzyme variants (HMSE1) was cloned from a U-937 λgt11 cDNA library by screening with an oligonucleotide mixture designed according to amino acid sequence data of the purified enzyme. The cDNA contains 1,727 bp with an open reading frame of 1,512 bp coding for a protein of 503 amino acid residues. HMSE1 cDNA represents the first cloned monocyte/macrophage-specific serine esterase and its sequence shows up to 77% homology to other known serine esterases of different species. The amino acid composition of the putative active site of HMSE1 as deduced from the nucleotide sequence corresponds with the active sites of other serine esterases but not with the active sites of serine proteases. Hybridization of the cDNA with RNA of separated normal blood cell populations and hematopoietic cell lines shows restricted expression within the monocyte/macrophage lineage.</description><identifier>ISSN: 0006-4971</identifier><identifier>EISSN: 1528-0020</identifier><identifier>DOI: 10.1182/blood.V78.2.506.506</identifier><identifier>PMID: 2070086</identifier><language>eng</language><publisher>Washington, DC: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; Biological and medical sciences ; Blotting, Northern ; Cell Line ; Cloning, Molecular ; DNA - blood ; DNA - genetics ; DNA - isolation & purification ; Esterases - blood ; Esterases - genetics ; Fundamental and applied biological sciences. Psychology ; Gene Library ; Humans ; Leukocytes - enzymology ; Macrophages - enzymology ; Molecular and cellular biology ; Molecular genetics ; Molecular Sequence Data ; Monocytes - enzymology ; Nucleic Acid Hybridization ; Restriction Mapping ; RNA, Messenger - genetics ; Sequence Homology, Nucleic Acid ; Serine Endopeptidases - genetics</subject><ispartof>Blood, 1991-07, Vol.78 (2), p.506-512</ispartof><rights>1991 American Society of Hematology</rights><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c428t-e6f068eb06a6f1c4dc03a30222c7cafb5875c90ffb71267d0b60b8f922e424d3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27923,27924</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4684514$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2070086$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zschunke, F.</creatorcontrib><creatorcontrib>Salmassi, A.</creatorcontrib><creatorcontrib>Kreipe, H.</creatorcontrib><creatorcontrib>Buck, F.</creatorcontrib><creatorcontrib>Parwaresch, M.R.</creatorcontrib><creatorcontrib>Radzun, H.J.</creatorcontrib><title>cDNA Cloning and Characterization of Human Monocyte/Macrophage Serine Esterase-1</title><title>Blood</title><addtitle>Blood</addtitle><description>Human monocyte/macrophage serine esterase (HMSE), commonly known as acid esterase or α-naphthylacetate esterase, comprises a group of five enzyme variants that can be distinguished by their isoelectric points from esterase variants of the other normal human blood cell populations. A cDNA for one of the monocytic enzyme variants (HMSE1) was cloned from a U-937 λgt11 cDNA library by screening with an oligonucleotide mixture designed according to amino acid sequence data of the purified enzyme. The cDNA contains 1,727 bp with an open reading frame of 1,512 bp coding for a protein of 503 amino acid residues. HMSE1 cDNA represents the first cloned monocyte/macrophage-specific serine esterase and its sequence shows up to 77% homology to other known serine esterases of different species. The amino acid composition of the putative active site of HMSE1 as deduced from the nucleotide sequence corresponds with the active sites of other serine esterases but not with the active sites of serine proteases. Hybridization of the cDNA with RNA of separated normal blood cell populations and hematopoietic cell lines shows restricted expression within the monocyte/macrophage lineage.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Binding Sites</subject><subject>Biological and medical sciences</subject><subject>Blotting, Northern</subject><subject>Cell Line</subject><subject>Cloning, Molecular</subject><subject>DNA - blood</subject><subject>DNA - genetics</subject><subject>DNA - isolation & purification</subject><subject>Esterases - blood</subject><subject>Esterases - genetics</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Library</subject><subject>Humans</subject><subject>Leukocytes - enzymology</subject><subject>Macrophages - enzymology</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>Molecular Sequence Data</subject><subject>Monocytes - enzymology</subject><subject>Nucleic Acid Hybridization</subject><subject>Restriction Mapping</subject><subject>RNA, Messenger - genetics</subject><subject>Sequence Homology, Nucleic Acid</subject><subject>Serine Endopeptidases - genetics</subject><issn>0006-4971</issn><issn>1528-0020</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1rGzEQhkVpSZ20v6AU9lByW2ek1WrlQw_BcT4gaQsNvYpZ7ShRWUuutC6kv75ybHLMYdBhnvfV8DD2icOccy3O-jHGYf6r03Mxb0Ht5g2b8VboGkDAWzYDAFXLRcffs-OcfwNw2Yj2iB0J6AC0mrEf9uLbebUcY_DhocIwVMtHTGgnSv4fTj6GKrrqervGUN3FEO3TRGd3aFPcPOIDVT8LF6ha5RLATDX_wN45HDN9PLwn7P5ydb-8rm-_X90sz29rK4WealIOlKYeFCrHrRwsNNiAEMJ2Fl3f6q61C3Cu77hQ3QC9gl67hRAkhRyaE3a6r92k-GdLeTJrny2NIwaK22x0aQetZQGbPVhOzjmRM5vk15ieDAez02ieNZqi0QhTFO6mpD4f6rf9moaXzMFb2X857DFbHF3CYH1-waTSsuW7z7_uMSom_npKJltPwdLgE9nJDNG_esZ_2ySQdQ</recordid><startdate>19910715</startdate><enddate>19910715</enddate><creator>Zschunke, F.</creator><creator>Salmassi, A.</creator><creator>Kreipe, H.</creator><creator>Buck, F.</creator><creator>Parwaresch, M.R.</creator><creator>Radzun, H.J.</creator><general>Elsevier Inc</general><general>The Americain Society of Hematology</general><scope>6I.</scope><scope>AAFTH</scope><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>7X8</scope></search><sort><creationdate>19910715</creationdate><title>cDNA Cloning and Characterization of Human Monocyte/Macrophage Serine Esterase-1</title><author>Zschunke, F. ; Salmassi, A. ; Kreipe, H. ; Buck, F. ; Parwaresch, M.R. ; Radzun, H.J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c428t-e6f068eb06a6f1c4dc03a30222c7cafb5875c90ffb71267d0b60b8f922e424d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Binding Sites</topic><topic>Biological and medical sciences</topic><topic>Blotting, Northern</topic><topic>Cell Line</topic><topic>Cloning, Molecular</topic><topic>DNA - blood</topic><topic>DNA - genetics</topic><topic>DNA - isolation & purification</topic><topic>Esterases - blood</topic><topic>Esterases - genetics</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Library</topic><topic>Humans</topic><topic>Leukocytes - enzymology</topic><topic>Macrophages - enzymology</topic><topic>Molecular and cellular biology</topic><topic>Molecular genetics</topic><topic>Molecular Sequence Data</topic><topic>Monocytes - enzymology</topic><topic>Nucleic Acid Hybridization</topic><topic>Restriction Mapping</topic><topic>RNA, Messenger - genetics</topic><topic>Sequence Homology, Nucleic Acid</topic><topic>Serine Endopeptidases - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zschunke, F.</creatorcontrib><creatorcontrib>Salmassi, A.</creatorcontrib><creatorcontrib>Kreipe, H.</creatorcontrib><creatorcontrib>Buck, F.</creatorcontrib><creatorcontrib>Parwaresch, M.R.</creatorcontrib><creatorcontrib>Radzun, H.J.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><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>MEDLINE - Academic</collection><jtitle>Blood</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zschunke, F.</au><au>Salmassi, A.</au><au>Kreipe, H.</au><au>Buck, F.</au><au>Parwaresch, M.R.</au><au>Radzun, H.J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>cDNA Cloning and Characterization of Human Monocyte/Macrophage Serine Esterase-1</atitle><jtitle>Blood</jtitle><addtitle>Blood</addtitle><date>1991-07-15</date><risdate>1991</risdate><volume>78</volume><issue>2</issue><spage>506</spage><epage>512</epage><pages>506-512</pages><issn>0006-4971</issn><eissn>1528-0020</eissn><abstract>Human monocyte/macrophage serine esterase (HMSE), commonly known as acid esterase or α-naphthylacetate esterase, comprises a group of five enzyme variants that can be distinguished by their isoelectric points from esterase variants of the other normal human blood cell populations. A cDNA for one of the monocytic enzyme variants (HMSE1) was cloned from a U-937 λgt11 cDNA library by screening with an oligonucleotide mixture designed according to amino acid sequence data of the purified enzyme. The cDNA contains 1,727 bp with an open reading frame of 1,512 bp coding for a protein of 503 amino acid residues. HMSE1 cDNA represents the first cloned monocyte/macrophage-specific serine esterase and its sequence shows up to 77% homology to other known serine esterases of different species. The amino acid composition of the putative active site of HMSE1 as deduced from the nucleotide sequence corresponds with the active sites of other serine esterases but not with the active sites of serine proteases. 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| ispartof | Blood, 1991-07, Vol.78 (2), p.506-512 |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Animals Base Sequence Binding Sites Biological and medical sciences Blotting, Northern Cell Line Cloning, Molecular DNA - blood DNA - genetics DNA - isolation & purification Esterases - blood Esterases - genetics Fundamental and applied biological sciences. Psychology Gene Library Humans Leukocytes - enzymology Macrophages - enzymology Molecular and cellular biology Molecular genetics Molecular Sequence Data Monocytes - enzymology Nucleic Acid Hybridization Restriction Mapping RNA, Messenger - genetics Sequence Homology, Nucleic Acid Serine Endopeptidases - genetics |
| title | cDNA Cloning and Characterization of Human Monocyte/Macrophage Serine Esterase-1 |
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