ERGIC-53, a Membrane Protein of the Endoplasmic Reticulum-Golgi Intermediate Compartment, Is Identical to MR60, an Intracellular Mannose-specific Lectin of Myelomonocytic Cells
A mannose-specific membrane lectin (MR60) isolated from human myelomonocytic HL60 cells by affinity chromatography is expressed in intracellular organelles of immature monocytes (Pimpaneau, V., Midoux, P., Monsigny, M., and Roche, A. C. (1991) Carbohydr. Res. 213, 95-108). It is not present at the c...
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creator | Arar, C Carpentier, V Le Caer, J P Monsigny, M Legrand, A Roche, A C |
description | A mannose-specific membrane lectin (MR60) isolated from human myelomonocytic HL60 cells by affinity chromatography is expressed
in intracellular organelles of immature monocytes (Pimpaneau, V., Midoux, P., Monsigny, M., and Roche, A. C. (1991) Carbohydr. Res. 213, 95-108). It is not present at the cell surface and is immunochemically and structurally distinct from the M r 175,000 mannose receptor of mature macrophages. MR60 cDNA was isolated and characterized; on the basis of its sequence, MR60
is not related to any known mammalian lectins. Surprisingly, MR60 was found to be identical to ERGIC-53 (Schindler, R., Itin,
C., Zerial, M., Lottspeich, F., and Hauri, H. P.(1993) Eur. J. Cell Biol. 61, 1-9), a type I integral membrane protein, defined as a marker of the intermediate compartment that recycles between the
Golgi apparatus and endoplasmic reticulum; MR60/ERGIC-53 shares with VIP-36 significant homologies with leguminous plant lectins
(Fiedler, K., and Simmons, K.(1994) Cell 77, 625-626). We extend these findings in evidencing a structural homology between MR60/ERGIC-53 and mammalian galectins
(soluble β galactose binding proteins). MR60/ERGIC-53 is the first lectin characterized as an endoplasmic reticulum-Golgi
protein. Accordingly, this intracellular mannose binding protein could be involved in the traffic of glycoproteins between
endoplasmic reticulum and the Golgi apparatus. |
doi_str_mv | 10.1074/jbc.270.8.3551 |
format | Article |
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in intracellular organelles of immature monocytes (Pimpaneau, V., Midoux, P., Monsigny, M., and Roche, A. C. (1991) Carbohydr. Res. 213, 95-108). It is not present at the cell surface and is immunochemically and structurally distinct from the M r 175,000 mannose receptor of mature macrophages. MR60 cDNA was isolated and characterized; on the basis of its sequence, MR60
is not related to any known mammalian lectins. Surprisingly, MR60 was found to be identical to ERGIC-53 (Schindler, R., Itin,
C., Zerial, M., Lottspeich, F., and Hauri, H. P.(1993) Eur. J. Cell Biol. 61, 1-9), a type I integral membrane protein, defined as a marker of the intermediate compartment that recycles between the
Golgi apparatus and endoplasmic reticulum; MR60/ERGIC-53 shares with VIP-36 significant homologies with leguminous plant lectins
(Fiedler, K., and Simmons, K.(1994) Cell 77, 625-626). We extend these findings in evidencing a structural homology between MR60/ERGIC-53 and mammalian galectins
(soluble β galactose binding proteins). MR60/ERGIC-53 is the first lectin characterized as an endoplasmic reticulum-Golgi
protein. Accordingly, this intracellular mannose binding protein could be involved in the traffic of glycoproteins between
endoplasmic reticulum and the Golgi apparatus.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.270.8.3551</identifier><identifier>PMID: 7876089</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Amino Acid Sequence ; Base Sequence ; Cell Compartmentation ; Cell Line ; Cloning, Molecular ; DNA, Complementary ; Endoplasmic Reticulum - metabolism ; Golgi Apparatus - metabolism ; Hematopoietic Stem Cells - metabolism ; Humans ; Lectins - genetics ; Lectins - metabolism ; Life Sciences ; Mannose-Binding Lectins ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Molecular Sequence Data ; Sequence Homology, Amino Acid</subject><ispartof>The Journal of biological chemistry, 1995-02, Vol.270 (8), p.3551-3553</ispartof><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c488t-18815df7c1b9deeeae8768630399c2df7832e5294102185d042e953ebcf4630b3</citedby><cites>FETCH-LOGICAL-c488t-18815df7c1b9deeeae8768630399c2df7832e5294102185d042e953ebcf4630b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7876089$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-02138409$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Arar, C</creatorcontrib><creatorcontrib>Carpentier, V</creatorcontrib><creatorcontrib>Le Caer, J P</creatorcontrib><creatorcontrib>Monsigny, M</creatorcontrib><creatorcontrib>Legrand, A</creatorcontrib><creatorcontrib>Roche, A C</creatorcontrib><title>ERGIC-53, a Membrane Protein of the Endoplasmic Reticulum-Golgi Intermediate Compartment, Is Identical to MR60, an Intracellular Mannose-specific Lectin of Myelomonocytic Cells</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>A mannose-specific membrane lectin (MR60) isolated from human myelomonocytic HL60 cells by affinity chromatography is expressed
in intracellular organelles of immature monocytes (Pimpaneau, V., Midoux, P., Monsigny, M., and Roche, A. C. (1991) Carbohydr. Res. 213, 95-108). It is not present at the cell surface and is immunochemically and structurally distinct from the M r 175,000 mannose receptor of mature macrophages. MR60 cDNA was isolated and characterized; on the basis of its sequence, MR60
is not related to any known mammalian lectins. Surprisingly, MR60 was found to be identical to ERGIC-53 (Schindler, R., Itin,
C., Zerial, M., Lottspeich, F., and Hauri, H. P.(1993) Eur. J. Cell Biol. 61, 1-9), a type I integral membrane protein, defined as a marker of the intermediate compartment that recycles between the
Golgi apparatus and endoplasmic reticulum; MR60/ERGIC-53 shares with VIP-36 significant homologies with leguminous plant lectins
(Fiedler, K., and Simmons, K.(1994) Cell 77, 625-626). We extend these findings in evidencing a structural homology between MR60/ERGIC-53 and mammalian galectins
(soluble β galactose binding proteins). MR60/ERGIC-53 is the first lectin characterized as an endoplasmic reticulum-Golgi
protein. Accordingly, this intracellular mannose binding protein could be involved in the traffic of glycoproteins between
endoplasmic reticulum and the Golgi apparatus.</description><subject>Amino Acid Sequence</subject><subject>Base Sequence</subject><subject>Cell Compartmentation</subject><subject>Cell Line</subject><subject>Cloning, Molecular</subject><subject>DNA, Complementary</subject><subject>Endoplasmic Reticulum - metabolism</subject><subject>Golgi Apparatus - metabolism</subject><subject>Hematopoietic Stem Cells - metabolism</subject><subject>Humans</subject><subject>Lectins - genetics</subject><subject>Lectins - metabolism</subject><subject>Life Sciences</subject><subject>Mannose-Binding Lectins</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Sequence Homology, Amino Acid</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFUV2LEzEUDaKsdfXVNyH4IAg7Yz4mneRxKXW30KIUBd9CJnNnm2VmUpOM0n_lTzRDy-KbeUm495xzc-5B6C0lJSV19emxsSWrSSlLLgR9hhaUSF5wQX88RwtCGC0UE_IlehXjI8mnUvQKXdWyXhKpFujPen-3WRWC32CDdzA0wYyAvwafwI3YdzgdAK_H1h97Ewdn8R6Ss1M_DcWd7x8c3owJwgCtMwnwyg9HE9IAY7rBm4g3bX45a3qcPN7tlyRPGWdKMBb6fupNwDszjj5CEY9gXZcnbMGm8-zdCXo_-NHbU1bBq0yJr9GLzvQR3lzua_T98_rb6r7YfslGbreFraRMBZWSirarLW1UCwAGsmO55IQrZVluSM5AMFXRvCIpWlIxUIJDY7sqoxp-jT6edQ-m18fgBhNO2hun72-3eq5lHpcVUb9oxn44Y4_B_5wgJj24OBvMu_RT1HVNhaoY-y-QLmtGieAZWJ6BNvgYA3RPX6BEz7nrnLvOuWup59wz4d1FeWpyGk_wS9C5__5ixz0cfrsAunHeHmD4V-QvCDqz7Q</recordid><startdate>19950224</startdate><enddate>19950224</enddate><creator>Arar, C</creator><creator>Carpentier, V</creator><creator>Le Caer, J P</creator><creator>Monsigny, M</creator><creator>Legrand, A</creator><creator>Roche, A C</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>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>1XC</scope></search><sort><creationdate>19950224</creationdate><title>ERGIC-53, a Membrane Protein of the Endoplasmic Reticulum-Golgi Intermediate Compartment, Is Identical to MR60, an Intracellular Mannose-specific Lectin of Myelomonocytic Cells</title><author>Arar, C ; Carpentier, V ; Le Caer, J P ; Monsigny, M ; Legrand, A ; Roche, A C</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c488t-18815df7c1b9deeeae8768630399c2df7832e5294102185d042e953ebcf4630b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Amino Acid Sequence</topic><topic>Base Sequence</topic><topic>Cell Compartmentation</topic><topic>Cell Line</topic><topic>Cloning, Molecular</topic><topic>DNA, Complementary</topic><topic>Endoplasmic Reticulum - metabolism</topic><topic>Golgi Apparatus - metabolism</topic><topic>Hematopoietic Stem Cells - metabolism</topic><topic>Humans</topic><topic>Lectins - genetics</topic><topic>Lectins - metabolism</topic><topic>Life Sciences</topic><topic>Mannose-Binding Lectins</topic><topic>Membrane Proteins - genetics</topic><topic>Membrane Proteins - metabolism</topic><topic>Molecular Sequence Data</topic><topic>Sequence Homology, Amino Acid</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Arar, C</creatorcontrib><creatorcontrib>Carpentier, V</creatorcontrib><creatorcontrib>Le Caer, J P</creatorcontrib><creatorcontrib>Monsigny, M</creatorcontrib><creatorcontrib>Legrand, A</creatorcontrib><creatorcontrib>Roche, A C</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>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Arar, C</au><au>Carpentier, V</au><au>Le Caer, J P</au><au>Monsigny, M</au><au>Legrand, A</au><au>Roche, A C</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>ERGIC-53, a Membrane Protein of the Endoplasmic Reticulum-Golgi Intermediate Compartment, Is Identical to MR60, an Intracellular Mannose-specific Lectin of Myelomonocytic Cells</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1995-02-24</date><risdate>1995</risdate><volume>270</volume><issue>8</issue><spage>3551</spage><epage>3553</epage><pages>3551-3553</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>A mannose-specific membrane lectin (MR60) isolated from human myelomonocytic HL60 cells by affinity chromatography is expressed
in intracellular organelles of immature monocytes (Pimpaneau, V., Midoux, P., Monsigny, M., and Roche, A. C. (1991) Carbohydr. Res. 213, 95-108). It is not present at the cell surface and is immunochemically and structurally distinct from the M r 175,000 mannose receptor of mature macrophages. MR60 cDNA was isolated and characterized; on the basis of its sequence, MR60
is not related to any known mammalian lectins. Surprisingly, MR60 was found to be identical to ERGIC-53 (Schindler, R., Itin,
C., Zerial, M., Lottspeich, F., and Hauri, H. P.(1993) Eur. J. Cell Biol. 61, 1-9), a type I integral membrane protein, defined as a marker of the intermediate compartment that recycles between the
Golgi apparatus and endoplasmic reticulum; MR60/ERGIC-53 shares with VIP-36 significant homologies with leguminous plant lectins
(Fiedler, K., and Simmons, K.(1994) Cell 77, 625-626). We extend these findings in evidencing a structural homology between MR60/ERGIC-53 and mammalian galectins
(soluble β galactose binding proteins). MR60/ERGIC-53 is the first lectin characterized as an endoplasmic reticulum-Golgi
protein. Accordingly, this intracellular mannose binding protein could be involved in the traffic of glycoproteins between
endoplasmic reticulum and the Golgi apparatus.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>7876089</pmid><doi>10.1074/jbc.270.8.3551</doi><tpages>3</tpages><oa>free_for_read</oa></addata></record> |
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source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
subjects | Amino Acid Sequence Base Sequence Cell Compartmentation Cell Line Cloning, Molecular DNA, Complementary Endoplasmic Reticulum - metabolism Golgi Apparatus - metabolism Hematopoietic Stem Cells - metabolism Humans Lectins - genetics Lectins - metabolism Life Sciences Mannose-Binding Lectins Membrane Proteins - genetics Membrane Proteins - metabolism Molecular Sequence Data Sequence Homology, Amino Acid |
title | ERGIC-53, a Membrane Protein of the Endoplasmic Reticulum-Golgi Intermediate Compartment, Is Identical to MR60, an Intracellular Mannose-specific Lectin of Myelomonocytic Cells |
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