Lysosomal alpha-mannosidases of mouse tissues: characteristics of the isoenzymes, and cloning and expression of a full-length cDNA
Lysosomal alpha-d-mannosidase from mouse tissues was separated into its constituent isoenzymes by DEAE-cellulose chromatography. Forms corresponding to the human isoenzymes B and A were present in testis, brain, spleen and kidney, whereas in epididymis and liver only the B form was present. Murine a...
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| Veröffentlicht in: | Biochemical journal 1997-10, Vol.327 ( Pt 1) (1), p.45-49 |
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| container_title | Biochemical journal |
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| creator | Beccari, T Appolloni, M G Costanzi, E Stinchi, S Stirling, J L Della Fazia, M A Servillo, G Viola, M P Orlacchio, A |
| description | Lysosomal alpha-d-mannosidase from mouse tissues was separated into its constituent isoenzymes by DEAE-cellulose chromatography. Forms corresponding to the human isoenzymes B and A were present in testis, brain, spleen and kidney, whereas in epididymis and liver only the B form was present. Murine alpha-mannosidases A and B are glycoproteins and have pH optima, thermal stabilities and molecular masses similar to those of the human isoenzymes. A full-length cDNA (3.1 kb) containing the complete coding sequence for alpha-mannosidase was isolated from a mouse macrophage cDNA library. Comparison of the deduced amino acid sequences of human and mouse alpha-mannosidases showed that they had 75% identity and 83% similarity. Expression of this cDNA in COS cells showed that both the A and the B isoenzymes can arise from a single transcript. Northern blotting analysis showed a 10-fold range in the abundance of alpha-mannosidase mRNA in mouse tissues, with the highest levels found in epididymis, and the lowest in liver. |
| doi_str_mv | 10.1042/bj3270045 |
| format | Article |
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Forms corresponding to the human isoenzymes B and A were present in testis, brain, spleen and kidney, whereas in epididymis and liver only the B form was present. Murine alpha-mannosidases A and B are glycoproteins and have pH optima, thermal stabilities and molecular masses similar to those of the human isoenzymes. A full-length cDNA (3.1 kb) containing the complete coding sequence for alpha-mannosidase was isolated from a mouse macrophage cDNA library. Comparison of the deduced amino acid sequences of human and mouse alpha-mannosidases showed that they had 75% identity and 83% similarity. Expression of this cDNA in COS cells showed that both the A and the B isoenzymes can arise from a single transcript. Northern blotting analysis showed a 10-fold range in the abundance of alpha-mannosidase mRNA in mouse tissues, with the highest levels found in epididymis, and the lowest in liver.</description><identifier>ISSN: 0264-6021</identifier><identifier>EISSN: 1470-8728</identifier><identifier>DOI: 10.1042/bj3270045</identifier><identifier>PMID: 9355733</identifier><language>eng</language><publisher>England</publisher><subject>alpha-Mannosidase ; Amino Acid Sequence ; Animals ; Blotting, Northern ; Chromatography, DEAE-Cellulose ; Chromosome Mapping ; Cloning, Molecular ; COS Cells ; DNA, Complementary - genetics ; Gene Expression ; Humans ; Isoenzymes - chemistry ; Isoenzymes - genetics ; Isoenzymes - isolation & purification ; Isoenzymes - metabolism ; Lysosomes - enzymology ; Mannosidases - chemistry ; Mannosidases - genetics ; Mannosidases - isolation & purification ; Mannosidases - metabolism ; Mice ; Molecular Sequence Data ; RNA, Messenger - genetics ; RNA, Messenger - metabolism ; Sequence Homology, Amino Acid</subject><ispartof>Biochemical journal, 1997-10, Vol.327 ( Pt 1) (1), p.45-49</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c401t-5958b928f6f0d1eee269f3ca5550cf454080e00f231ebbd5f299a1b6b7676a1d3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1218761/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1218761/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9355733$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Beccari, T</creatorcontrib><creatorcontrib>Appolloni, M G</creatorcontrib><creatorcontrib>Costanzi, E</creatorcontrib><creatorcontrib>Stinchi, S</creatorcontrib><creatorcontrib>Stirling, J L</creatorcontrib><creatorcontrib>Della Fazia, M A</creatorcontrib><creatorcontrib>Servillo, G</creatorcontrib><creatorcontrib>Viola, M P</creatorcontrib><creatorcontrib>Orlacchio, A</creatorcontrib><title>Lysosomal alpha-mannosidases of mouse tissues: characteristics of the isoenzymes, and cloning and expression of a full-length cDNA</title><title>Biochemical journal</title><addtitle>Biochem J</addtitle><description>Lysosomal alpha-d-mannosidase from mouse tissues was separated into its constituent isoenzymes by DEAE-cellulose chromatography. Forms corresponding to the human isoenzymes B and A were present in testis, brain, spleen and kidney, whereas in epididymis and liver only the B form was present. Murine alpha-mannosidases A and B are glycoproteins and have pH optima, thermal stabilities and molecular masses similar to those of the human isoenzymes. A full-length cDNA (3.1 kb) containing the complete coding sequence for alpha-mannosidase was isolated from a mouse macrophage cDNA library. Comparison of the deduced amino acid sequences of human and mouse alpha-mannosidases showed that they had 75% identity and 83% similarity. Expression of this cDNA in COS cells showed that both the A and the B isoenzymes can arise from a single transcript. Northern blotting analysis showed a 10-fold range in the abundance of alpha-mannosidase mRNA in mouse tissues, with the highest levels found in epididymis, and the lowest in liver.</description><subject>alpha-Mannosidase</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Blotting, Northern</subject><subject>Chromatography, DEAE-Cellulose</subject><subject>Chromosome Mapping</subject><subject>Cloning, Molecular</subject><subject>COS Cells</subject><subject>DNA, Complementary - genetics</subject><subject>Gene Expression</subject><subject>Humans</subject><subject>Isoenzymes - chemistry</subject><subject>Isoenzymes - genetics</subject><subject>Isoenzymes - isolation & purification</subject><subject>Isoenzymes - metabolism</subject><subject>Lysosomes - enzymology</subject><subject>Mannosidases - chemistry</subject><subject>Mannosidases - genetics</subject><subject>Mannosidases - isolation & purification</subject><subject>Mannosidases - metabolism</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>RNA, Messenger - genetics</subject><subject>RNA, Messenger - metabolism</subject><subject>Sequence Homology, Amino Acid</subject><issn>0264-6021</issn><issn>1470-8728</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUuLFDEUhYMoYzu68AcIWQmCNd4klXq4GBjGxwiNbnRdpFI3XRlSSZtbLfYs55dbM9M0unJ1D9yPw-Ecxl4KOBNQynf9tZI1QKkfsZUoayiaWjaP2QpkVRYVSPGUPSO6BhAllHDCTlqlda3Uit2u95QoTSZwE7ajKSYTYyI_GELiyfEp7Qj57Il2SO-5HU02dsbsafb2nphH5J4Sxpv9hPSWmzhwG1L0cXOv8fc2I5FP8Y423O1CKALGzTxy--HrxXP2xJlA-OJwT9mPTx-_X14V62-fv1xerAtbgpgL3eqmb2XjKgeDQERZtU5Zo7UG60pdQgMI4KQS2PeDdrJtjeirvq7qyohBnbLzB9_trp9wsBjnbEK3zX4yed8l47t_P9GP3Sb96oQUTV2JxeD1wSCnn0sbczd5shiCibi01NWtgla18r-gqJRQuqkX8M0DaHMiyuiOaQR0d8t2x2UX9tXf8Y_kYUr1B-SvoUc</recordid><startdate>19971001</startdate><enddate>19971001</enddate><creator>Beccari, T</creator><creator>Appolloni, M G</creator><creator>Costanzi, E</creator><creator>Stinchi, S</creator><creator>Stirling, J L</creator><creator>Della Fazia, M A</creator><creator>Servillo, G</creator><creator>Viola, M P</creator><creator>Orlacchio, A</creator><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>5PM</scope></search><sort><creationdate>19971001</creationdate><title>Lysosomal alpha-mannosidases of mouse tissues: characteristics of the isoenzymes, and cloning and expression of a full-length cDNA</title><author>Beccari, T ; Appolloni, M G ; Costanzi, E ; Stinchi, S ; Stirling, J L ; Della Fazia, M A ; Servillo, G ; Viola, M P ; Orlacchio, A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c401t-5958b928f6f0d1eee269f3ca5550cf454080e00f231ebbd5f299a1b6b7676a1d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>alpha-Mannosidase</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Blotting, Northern</topic><topic>Chromatography, DEAE-Cellulose</topic><topic>Chromosome Mapping</topic><topic>Cloning, Molecular</topic><topic>COS Cells</topic><topic>DNA, Complementary - genetics</topic><topic>Gene Expression</topic><topic>Humans</topic><topic>Isoenzymes - chemistry</topic><topic>Isoenzymes - genetics</topic><topic>Isoenzymes - isolation & purification</topic><topic>Isoenzymes - metabolism</topic><topic>Lysosomes - enzymology</topic><topic>Mannosidases - chemistry</topic><topic>Mannosidases - genetics</topic><topic>Mannosidases - isolation & purification</topic><topic>Mannosidases - metabolism</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>RNA, Messenger - genetics</topic><topic>RNA, Messenger - metabolism</topic><topic>Sequence Homology, Amino Acid</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Beccari, T</creatorcontrib><creatorcontrib>Appolloni, M G</creatorcontrib><creatorcontrib>Costanzi, E</creatorcontrib><creatorcontrib>Stinchi, S</creatorcontrib><creatorcontrib>Stirling, J L</creatorcontrib><creatorcontrib>Della Fazia, M A</creatorcontrib><creatorcontrib>Servillo, G</creatorcontrib><creatorcontrib>Viola, M P</creatorcontrib><creatorcontrib>Orlacchio, A</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>PubMed Central (Full Participant titles)</collection><jtitle>Biochemical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Beccari, T</au><au>Appolloni, M G</au><au>Costanzi, E</au><au>Stinchi, S</au><au>Stirling, J L</au><au>Della Fazia, M A</au><au>Servillo, G</au><au>Viola, M P</au><au>Orlacchio, A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Lysosomal alpha-mannosidases of mouse tissues: characteristics of the isoenzymes, and cloning and expression of a full-length cDNA</atitle><jtitle>Biochemical journal</jtitle><addtitle>Biochem J</addtitle><date>1997-10-01</date><risdate>1997</risdate><volume>327 ( Pt 1)</volume><issue>1</issue><spage>45</spage><epage>49</epage><pages>45-49</pages><issn>0264-6021</issn><eissn>1470-8728</eissn><abstract>Lysosomal alpha-d-mannosidase from mouse tissues was separated into its constituent isoenzymes by DEAE-cellulose chromatography. Forms corresponding to the human isoenzymes B and A were present in testis, brain, spleen and kidney, whereas in epididymis and liver only the B form was present. Murine alpha-mannosidases A and B are glycoproteins and have pH optima, thermal stabilities and molecular masses similar to those of the human isoenzymes. A full-length cDNA (3.1 kb) containing the complete coding sequence for alpha-mannosidase was isolated from a mouse macrophage cDNA library. Comparison of the deduced amino acid sequences of human and mouse alpha-mannosidases showed that they had 75% identity and 83% similarity. Expression of this cDNA in COS cells showed that both the A and the B isoenzymes can arise from a single transcript. Northern blotting analysis showed a 10-fold range in the abundance of alpha-mannosidase mRNA in mouse tissues, with the highest levels found in epididymis, and the lowest in liver.</abstract><cop>England</cop><pmid>9355733</pmid><doi>10.1042/bj3270045</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | alpha-Mannosidase Amino Acid Sequence Animals Blotting, Northern Chromatography, DEAE-Cellulose Chromosome Mapping Cloning, Molecular COS Cells DNA, Complementary - genetics Gene Expression Humans Isoenzymes - chemistry Isoenzymes - genetics Isoenzymes - isolation & purification Isoenzymes - metabolism Lysosomes - enzymology Mannosidases - chemistry Mannosidases - genetics Mannosidases - isolation & purification Mannosidases - metabolism Mice Molecular Sequence Data RNA, Messenger - genetics RNA, Messenger - metabolism Sequence Homology, Amino Acid |
| title | Lysosomal alpha-mannosidases of mouse tissues: characteristics of the isoenzymes, and cloning and expression of a full-length cDNA |
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