Alpha-1-antitrypsin-induced inhibition of complement-dependent phagocytosis
In a previous investigation, inhibition of complement-dependent rosette formation by alpha 1-antitrypsin (α 1-AT) was observed, and it was demonstrated that α 1-AT interacts through its carbohydrate portion with C3 and its fragments. In the present study, the effect of α 1-AT on the complement-recep...
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| Veröffentlicht in: | Immunobiology (1979) 1981-01, Vol.158 (4), p.338-346 |
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| container_title | Immunobiology (1979) |
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| creator | Mód, Anna Füst, Gyorgy Gergely, János Hollán, Susan R. Dierich, M.P. |
| description | In a previous investigation, inhibition of complement-dependent rosette formation by alpha
1-antitrypsin (α
1-AT) was observed, and it was demonstrated that α
1-AT interacts through its carbohydrate portion with C3 and its fragments. In the present study, the effect of α
1-AT on the complement-receptor-mediated phagocytosis by human peripheral blood monocytes was examined.
Purified α
1-AT inhibited in a dose-dependent manner phagocytosis of C3-carrying yeast particles. Inhibition was selective, concerned only C3-receptor-mediated phagocytosis, neither Fc-receptor-mediated phagocytosis nor uptake of untreated yeast particles was blocked by α
1-AT. It was demonstrated that α
1-AT exerted its inhibitory effect through binding to C3-carrying particles. The activity of α
1-AT towards C3 and fragments of C3 was not mediated by its antiprotease effect, but by its carbohydrate moiety. This finding suggests that α
1-AT may have an impact on various immune functions involving complement receptors. |
| doi_str_mv | 10.1016/S0171-2985(81)80005-8 |
| format | Article |
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1-antitrypsin (α
1-AT) was observed, and it was demonstrated that α
1-AT interacts through its carbohydrate portion with C3 and its fragments. In the present study, the effect of α
1-AT on the complement-receptor-mediated phagocytosis by human peripheral blood monocytes was examined.
Purified α
1-AT inhibited in a dose-dependent manner phagocytosis of C3-carrying yeast particles. Inhibition was selective, concerned only C3-receptor-mediated phagocytosis, neither Fc-receptor-mediated phagocytosis nor uptake of untreated yeast particles was blocked by α
1-AT. It was demonstrated that α
1-AT exerted its inhibitory effect through binding to C3-carrying particles. The activity of α
1-AT towards C3 and fragments of C3 was not mediated by its antiprotease effect, but by its carbohydrate moiety. This finding suggests that α
1-AT may have an impact on various immune functions involving complement receptors.</description><identifier>ISSN: 0171-2985</identifier><identifier>EISSN: 1878-3279</identifier><identifier>DOI: 10.1016/S0171-2985(81)80005-8</identifier><identifier>PMID: 7016739</identifier><language>eng</language><publisher>Netherlands: Elsevier GmbH</publisher><subject>alpha 1-Antitrypsin - pharmacology ; Blood Donors ; Complement C3 - metabolism ; Humans ; Leukemia - blood ; Monocytes - immunology ; Opsonin Proteins ; Phagocytosis ; Saccharomyces cerevisiae - metabolism</subject><ispartof>Immunobiology (1979), 1981-01, Vol.158 (4), p.338-346</ispartof><rights>1981 Gustav Fischer Verlag Stuttgart · New York</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c426t-ce964524b0a4afb78a08742bc57cfc6aca2296ecfd21a27504675eee75d88f013</citedby><cites>FETCH-LOGICAL-c426t-ce964524b0a4afb78a08742bc57cfc6aca2296ecfd21a27504675eee75d88f013</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0171-2985(81)80005-8$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>315,781,785,3551,27926,27927,45997</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7016739$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mód, Anna</creatorcontrib><creatorcontrib>Füst, Gyorgy</creatorcontrib><creatorcontrib>Gergely, János</creatorcontrib><creatorcontrib>Hollán, Susan R.</creatorcontrib><creatorcontrib>Dierich, M.P.</creatorcontrib><title>Alpha-1-antitrypsin-induced inhibition of complement-dependent phagocytosis</title><title>Immunobiology (1979)</title><addtitle>Immunobiology</addtitle><description>In a previous investigation, inhibition of complement-dependent rosette formation by alpha
1-antitrypsin (α
1-AT) was observed, and it was demonstrated that α
1-AT interacts through its carbohydrate portion with C3 and its fragments. In the present study, the effect of α
1-AT on the complement-receptor-mediated phagocytosis by human peripheral blood monocytes was examined.
Purified α
1-AT inhibited in a dose-dependent manner phagocytosis of C3-carrying yeast particles. Inhibition was selective, concerned only C3-receptor-mediated phagocytosis, neither Fc-receptor-mediated phagocytosis nor uptake of untreated yeast particles was blocked by α
1-AT. It was demonstrated that α
1-AT exerted its inhibitory effect through binding to C3-carrying particles. The activity of α
1-AT towards C3 and fragments of C3 was not mediated by its antiprotease effect, but by its carbohydrate moiety. This finding suggests that α
1-AT may have an impact on various immune functions involving complement receptors.</description><subject>alpha 1-Antitrypsin - pharmacology</subject><subject>Blood Donors</subject><subject>Complement C3 - metabolism</subject><subject>Humans</subject><subject>Leukemia - blood</subject><subject>Monocytes - immunology</subject><subject>Opsonin Proteins</subject><subject>Phagocytosis</subject><subject>Saccharomyces cerevisiae - metabolism</subject><issn>0171-2985</issn><issn>1878-3279</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1981</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkEtLxDAQx4Mo67r6ERZ6Ej1Ek7Rp0pPI4gsXPKjnkKZTN9ImtUmF_fZ2H-zV0wzM_8H8EJpTckMJzW_fCRUUs0LyK0mvJSGEY3mEplQKiVMmimM0PUhO0VkI34TQggk5QRMxJoi0mKLX-6ZbaUyxdtHGft0F67B11WCgSqxb2dJG613i68T4tmugBRdxBR24atyS0fzlzTr6YMM5Oql1E-BiP2fo8_HhY_GMl29PL4v7JTYZyyM2UOQZZ1lJdKbrUkhNpMhYabgwtcm10YwVOZi6YlQzwUmWCw4AgldS1oSmM3S5y-16_zNAiKq1wUDTaAd-CErwXDBO0lHId0LT-xB6qFXX21b3a0WJ2kBUW4hqQ0hJqrYQlRx9833BULZQHVx7auP9bneH8ctfC70KxoIbkdkeTFSVt_80_AFCWIJ7</recordid><startdate>19810101</startdate><enddate>19810101</enddate><creator>Mód, Anna</creator><creator>Füst, Gyorgy</creator><creator>Gergely, János</creator><creator>Hollán, Susan R.</creator><creator>Dierich, M.P.</creator><general>Elsevier GmbH</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>7X8</scope></search><sort><creationdate>19810101</creationdate><title>Alpha-1-antitrypsin-induced inhibition of complement-dependent phagocytosis</title><author>Mód, Anna ; Füst, Gyorgy ; Gergely, János ; Hollán, Susan R. ; Dierich, M.P.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c426t-ce964524b0a4afb78a08742bc57cfc6aca2296ecfd21a27504675eee75d88f013</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1981</creationdate><topic>alpha 1-Antitrypsin - pharmacology</topic><topic>Blood Donors</topic><topic>Complement C3 - metabolism</topic><topic>Humans</topic><topic>Leukemia - blood</topic><topic>Monocytes - immunology</topic><topic>Opsonin Proteins</topic><topic>Phagocytosis</topic><topic>Saccharomyces cerevisiae - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mód, Anna</creatorcontrib><creatorcontrib>Füst, Gyorgy</creatorcontrib><creatorcontrib>Gergely, János</creatorcontrib><creatorcontrib>Hollán, Susan R.</creatorcontrib><creatorcontrib>Dierich, M.P.</creatorcontrib><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>Immunobiology (1979)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mód, Anna</au><au>Füst, Gyorgy</au><au>Gergely, János</au><au>Hollán, Susan R.</au><au>Dierich, M.P.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Alpha-1-antitrypsin-induced inhibition of complement-dependent phagocytosis</atitle><jtitle>Immunobiology (1979)</jtitle><addtitle>Immunobiology</addtitle><date>1981-01-01</date><risdate>1981</risdate><volume>158</volume><issue>4</issue><spage>338</spage><epage>346</epage><pages>338-346</pages><issn>0171-2985</issn><eissn>1878-3279</eissn><abstract>In a previous investigation, inhibition of complement-dependent rosette formation by alpha
1-antitrypsin (α
1-AT) was observed, and it was demonstrated that α
1-AT interacts through its carbohydrate portion with C3 and its fragments. In the present study, the effect of α
1-AT on the complement-receptor-mediated phagocytosis by human peripheral blood monocytes was examined.
Purified α
1-AT inhibited in a dose-dependent manner phagocytosis of C3-carrying yeast particles. Inhibition was selective, concerned only C3-receptor-mediated phagocytosis, neither Fc-receptor-mediated phagocytosis nor uptake of untreated yeast particles was blocked by α
1-AT. It was demonstrated that α
1-AT exerted its inhibitory effect through binding to C3-carrying particles. The activity of α
1-AT towards C3 and fragments of C3 was not mediated by its antiprotease effect, but by its carbohydrate moiety. This finding suggests that α
1-AT may have an impact on various immune functions involving complement receptors.</abstract><cop>Netherlands</cop><pub>Elsevier GmbH</pub><pmid>7016739</pmid><doi>10.1016/S0171-2985(81)80005-8</doi><tpages>9</tpages></addata></record> |
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| identifier | ISSN: 0171-2985 |
| ispartof | Immunobiology (1979), 1981-01, Vol.158 (4), p.338-346 |
| issn | 0171-2985 1878-3279 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | alpha 1-Antitrypsin - pharmacology Blood Donors Complement C3 - metabolism Humans Leukemia - blood Monocytes - immunology Opsonin Proteins Phagocytosis Saccharomyces cerevisiae - metabolism |
| title | Alpha-1-antitrypsin-induced inhibition of complement-dependent phagocytosis |
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