Identification of Aminopeptidase Activity in the Secretory Granules of Mouse Mast Cells
Sonicates of mouse bone marrow-derived mast cells (BMMC) differentiated in vitro and of mouse serosal mast cells differentiated in vivo contained small but approximately equal amounts of aminopeptidase activity, as determined by cleavage of leucine-β-naphthylamide and resolution of the reaction prod...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1991-07, Vol.88 (14), p.5984-5988 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Serafin, William E. Guidry, Ursula A. Dayton, Elahe T. Kamada, Mika M. Stevens, Richard L. Austen, K. Frank |
| description | Sonicates of mouse bone marrow-derived mast cells (BMMC) differentiated in vitro and of mouse serosal mast cells differentiated in vivo contained small but approximately equal amounts of aminopeptidase activity, as determined by cleavage of leucine-β-naphthylamide and resolution of the reaction products by reverse-phase high-performance liquid chromatography. Aminopeptidase activity was exocytosed from antigen-activated, IgE-sensitized BMMC in proportion to the secretory granule enzyme β-hexosaminidase, thereby localizing ≈60% of the total cell-associated aminopeptidase activity to the secretory granules of the mast cells. A prominent secretory granule location for aminopeptidase was confirmed by activity measurement in subcellular fractions of disrupted BMMC. The secretory granule aminopeptidase had a pH optimum of 6.0-8.0 and a Kmof 0.36 ± 0.06 mM (mean ± SD; n = 3) for leucine-β-naphthylamide. When various amino acid β-naphthylamides were used as substrates, the preference of the secretory granule enzyme was Ala > Leu > Phe > > Arg > > Asp = Tyr. Most of the aminopeptidase activity that was exocytosed from calcium ionophore-activated BMMC was bound to35S-labeled proteoglycans in complexes of >1 x 107kDa as defined by exclusion during Sepharose CL-2B gel-filtration chromatography. We postulate that the aminopeptidase in the mast cell protease/proteoglycan complexes allows the removal of N-terminal amino acids from peptides that are generated by the action of mast cell endopeptidases. |
| doi_str_mv | 10.1073/pnas.88.14.5984 |
| format | Article |
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Frank</creator><creatorcontrib>Serafin, William E. ; Guidry, Ursula A. ; Dayton, Elahe T. ; Kamada, Mika M. ; Stevens, Richard L. ; Austen, K. Frank</creatorcontrib><description>Sonicates of mouse bone marrow-derived mast cells (BMMC) differentiated in vitro and of mouse serosal mast cells differentiated in vivo contained small but approximately equal amounts of aminopeptidase activity, as determined by cleavage of leucine-β-naphthylamide and resolution of the reaction products by reverse-phase high-performance liquid chromatography. Aminopeptidase activity was exocytosed from antigen-activated, IgE-sensitized BMMC in proportion to the secretory granule enzyme β-hexosaminidase, thereby localizing ≈60% of the total cell-associated aminopeptidase activity to the secretory granules of the mast cells. A prominent secretory granule location for aminopeptidase was confirmed by activity measurement in subcellular fractions of disrupted BMMC. The secretory granule aminopeptidase had a pH optimum of 6.0-8.0 and a Kmof 0.36 ± 0.06 mM (mean ± SD; n = 3) for leucine-β-naphthylamide. When various amino acid β-naphthylamides were used as substrates, the preference of the secretory granule enzyme was Ala > Leu > Phe > > Arg > > Asp = Tyr. Most of the aminopeptidase activity that was exocytosed from calcium ionophore-activated BMMC was bound to35S-labeled proteoglycans in complexes of >1 x 107kDa as defined by exclusion during Sepharose CL-2B gel-filtration chromatography. We postulate that the aminopeptidase in the mast cell protease/proteoglycan complexes allows the removal of N-terminal amino acids from peptides that are generated by the action of mast cell endopeptidases.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.88.14.5984</identifier><identifier>PMID: 2068074</identifier><identifier>CODEN: PNASA6</identifier><language>eng</language><publisher>Washington, DC: National Academy of Sciences of the United States of America</publisher><subject>Amino acids ; Aminopeptidases - isolation & purification ; Aminopeptidases - metabolism ; Analytical, structural and metabolic biochemistry ; Animals ; Biological and medical sciences ; Calcium ; Cell Fractionation ; Cells, Cultured ; Centrifugation, Density Gradient ; Chromatography, Gel ; Cytoplasmic Granules - enzymology ; Enzymes ; Enzymes and enzyme inhibitors ; Fibroblasts ; Fundamental and applied biological sciences. Psychology ; Histamines ; Hydrolases ; Kinetics ; Mast cells ; Mast Cells - enzymology ; Mice ; Mice, Inbred BALB C ; Proteoglycans ; Secretory vesicles ; Solvents ; Substrate Specificity</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1991-07, Vol.88 (14), p.5984-5988</ispartof><rights>Copyright 1991 The National Academy of Sciences of the United States of America</rights><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c523t-9b2da2dc4ad3f4935debd65567b6a97948eea57883e2f25099306fdcafba92f83</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/88/14.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/2357422$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/2357422$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,727,780,784,803,885,27924,27925,53791,53793,58017,58250</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19837273$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2068074$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Serafin, William E.</creatorcontrib><creatorcontrib>Guidry, Ursula A.</creatorcontrib><creatorcontrib>Dayton, Elahe T.</creatorcontrib><creatorcontrib>Kamada, Mika M.</creatorcontrib><creatorcontrib>Stevens, Richard L.</creatorcontrib><creatorcontrib>Austen, K. Frank</creatorcontrib><title>Identification of Aminopeptidase Activity in the Secretory Granules of Mouse Mast Cells</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Sonicates of mouse bone marrow-derived mast cells (BMMC) differentiated in vitro and of mouse serosal mast cells differentiated in vivo contained small but approximately equal amounts of aminopeptidase activity, as determined by cleavage of leucine-β-naphthylamide and resolution of the reaction products by reverse-phase high-performance liquid chromatography. Aminopeptidase activity was exocytosed from antigen-activated, IgE-sensitized BMMC in proportion to the secretory granule enzyme β-hexosaminidase, thereby localizing ≈60% of the total cell-associated aminopeptidase activity to the secretory granules of the mast cells. A prominent secretory granule location for aminopeptidase was confirmed by activity measurement in subcellular fractions of disrupted BMMC. The secretory granule aminopeptidase had a pH optimum of 6.0-8.0 and a Kmof 0.36 ± 0.06 mM (mean ± SD; n = 3) for leucine-β-naphthylamide. When various amino acid β-naphthylamides were used as substrates, the preference of the secretory granule enzyme was Ala > Leu > Phe > > Arg > > Asp = Tyr. Most of the aminopeptidase activity that was exocytosed from calcium ionophore-activated BMMC was bound to35S-labeled proteoglycans in complexes of >1 x 107kDa as defined by exclusion during Sepharose CL-2B gel-filtration chromatography. We postulate that the aminopeptidase in the mast cell protease/proteoglycan complexes allows the removal of N-terminal amino acids from peptides that are generated by the action of mast cell endopeptidases.</description><subject>Amino acids</subject><subject>Aminopeptidases - isolation & purification</subject><subject>Aminopeptidases - metabolism</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Calcium</subject><subject>Cell Fractionation</subject><subject>Cells, Cultured</subject><subject>Centrifugation, Density Gradient</subject><subject>Chromatography, Gel</subject><subject>Cytoplasmic Granules - enzymology</subject><subject>Enzymes</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fibroblasts</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Histamines</subject><subject>Hydrolases</subject><subject>Kinetics</subject><subject>Mast cells</subject><subject>Mast Cells - enzymology</subject><subject>Mice</subject><subject>Mice, Inbred BALB C</subject><subject>Proteoglycans</subject><subject>Secretory vesicles</subject><subject>Solvents</subject><subject>Substrate Specificity</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1v1DAQxS0EKkvhzAVQLsAp24m_LXFZrUqp1IoDII6W49jUVTZJY6di__s62tDSC5x8eL834zcPodcVrCsQ5GToTFxLua7omilJn6BVBaoqOVXwFK0AsCglxfQ5ehHjNQAoJuEIHWHgEgRdoZ_njetS8MGaFPqu6H2x2YWuH9yQQmOiKzY2hduQ9kXoinTlim_Oji714744G003tS7Opst-yuylianYuraNL9Ezb9roXi3vMfrx-fT79kt58fXsfLu5KC3DJJWqxo3BjaWmIZ4qwhpXN5wxLmpulFBUOmeYkJI47DEDpQhw31jja6Owl-QYfTrMHaZ65xqbw4ym1cMYdmbc694E_VjpwpX-1d9qhgF4tn9Y7GN_M7mY9C5EmwOYzuVEWgIXFWD8X7DimOXLQwZPDqAd-xhH5-__UoGeK9NzZVpKXVE9V5Ydb_-OcM8vHWX9_aKbaE3r89VtiA9jlSQCC5K5dws3L_gjP1r08Z-A9lPbJvc7ZfLNgbyOuemHHxEmaD7GHZ22wsc</recordid><startdate>19910715</startdate><enddate>19910715</enddate><creator>Serafin, William E.</creator><creator>Guidry, Ursula A.</creator><creator>Dayton, Elahe T.</creator><creator>Kamada, Mika M.</creator><creator>Stevens, Richard L.</creator><creator>Austen, K. Frank</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</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>7T5</scope><scope>H94</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19910715</creationdate><title>Identification of Aminopeptidase Activity in the Secretory Granules of Mouse Mast Cells</title><author>Serafin, William E. ; Guidry, Ursula A. ; Dayton, Elahe T. ; Kamada, Mika M. ; Stevens, Richard L. ; Austen, K. Frank</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c523t-9b2da2dc4ad3f4935debd65567b6a97948eea57883e2f25099306fdcafba92f83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>Amino acids</topic><topic>Aminopeptidases - isolation & purification</topic><topic>Aminopeptidases - metabolism</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Calcium</topic><topic>Cell Fractionation</topic><topic>Cells, Cultured</topic><topic>Centrifugation, Density Gradient</topic><topic>Chromatography, Gel</topic><topic>Cytoplasmic Granules - enzymology</topic><topic>Enzymes</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fibroblasts</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Histamines</topic><topic>Hydrolases</topic><topic>Kinetics</topic><topic>Mast cells</topic><topic>Mast Cells - enzymology</topic><topic>Mice</topic><topic>Mice, Inbred BALB C</topic><topic>Proteoglycans</topic><topic>Secretory vesicles</topic><topic>Solvents</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Serafin, William E.</creatorcontrib><creatorcontrib>Guidry, Ursula A.</creatorcontrib><creatorcontrib>Dayton, Elahe T.</creatorcontrib><creatorcontrib>Kamada, Mika M.</creatorcontrib><creatorcontrib>Stevens, Richard L.</creatorcontrib><creatorcontrib>Austen, K. 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Frank</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification of Aminopeptidase Activity in the Secretory Granules of Mouse Mast Cells</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1991-07-15</date><risdate>1991</risdate><volume>88</volume><issue>14</issue><spage>5984</spage><epage>5988</epage><pages>5984-5988</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><coden>PNASA6</coden><abstract>Sonicates of mouse bone marrow-derived mast cells (BMMC) differentiated in vitro and of mouse serosal mast cells differentiated in vivo contained small but approximately equal amounts of aminopeptidase activity, as determined by cleavage of leucine-β-naphthylamide and resolution of the reaction products by reverse-phase high-performance liquid chromatography. Aminopeptidase activity was exocytosed from antigen-activated, IgE-sensitized BMMC in proportion to the secretory granule enzyme β-hexosaminidase, thereby localizing ≈60% of the total cell-associated aminopeptidase activity to the secretory granules of the mast cells. A prominent secretory granule location for aminopeptidase was confirmed by activity measurement in subcellular fractions of disrupted BMMC. The secretory granule aminopeptidase had a pH optimum of 6.0-8.0 and a Kmof 0.36 ± 0.06 mM (mean ± SD; n = 3) for leucine-β-naphthylamide. When various amino acid β-naphthylamides were used as substrates, the preference of the secretory granule enzyme was Ala > Leu > Phe > > Arg > > Asp = Tyr. Most of the aminopeptidase activity that was exocytosed from calcium ionophore-activated BMMC was bound to35S-labeled proteoglycans in complexes of >1 x 107kDa as defined by exclusion during Sepharose CL-2B gel-filtration chromatography. We postulate that the aminopeptidase in the mast cell protease/proteoglycan complexes allows the removal of N-terminal amino acids from peptides that are generated by the action of mast cell endopeptidases.</abstract><cop>Washington, DC</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>2068074</pmid><doi>10.1073/pnas.88.14.5984</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1991-07, Vol.88 (14), p.5984-5988 |
| issn | 0027-8424 1091-6490 |
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| source | MEDLINE; JSTOR Archive Collection A-Z Listing; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Amino acids Aminopeptidases - isolation & purification Aminopeptidases - metabolism Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Calcium Cell Fractionation Cells, Cultured Centrifugation, Density Gradient Chromatography, Gel Cytoplasmic Granules - enzymology Enzymes Enzymes and enzyme inhibitors Fibroblasts Fundamental and applied biological sciences. Psychology Histamines Hydrolases Kinetics Mast cells Mast Cells - enzymology Mice Mice, Inbred BALB C Proteoglycans Secretory vesicles Solvents Substrate Specificity |
| title | Identification of Aminopeptidase Activity in the Secretory Granules of Mouse Mast Cells |
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