Inhibition of homologous complement activation by the heat-stable antigen
The murlne heat-stable antigen (HSAg) Is of particular Interest due to Its unique tissuedistribution. HSAg Is expressed on most thymocytes, bone marrow cells, immature B cells, and erythrocytes, but not on peripheral T and mature B cells. Although HSAg has been thought to be a differentiation antige...
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| Veröffentlicht in: | International immunology 1993-07, Vol.5 (7), p.805-808 |
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| creator | Hitsumoto, Yasuo Ohnishi, Hiroshi Nakano, Akihiro Hamada, Fumihiko Saheki, Shuichi Takeuchi, Nozomu |
| description | The murlne heat-stable antigen (HSAg) Is of particular Interest due to Its unique tissuedistribution. HSAg Is expressed on most thymocytes, bone marrow cells, immature B cells, and erythrocytes, but not on peripheral T and mature B cells. Although HSAg has been thought to be a differentiation antigen, its actual biological significance remains unknown except for the HSAg on antigen presenting cells. Recently, a new rat antl-HSAg mAb, R13, has been developed. Here It has been found that the mouse complement activation on mouse erythrocytes, but not the human, guinea pig or rabbit complement activations, was enhanced In the presence of the Fab fragment of R13. Afflnlty-purlfled HSAg derived from mouse erythrocytes could be passively Incorporated Into rabbit erythrocytes because of Its molecular characteristic of glycosylphosphatidyl Inosltol-anchored protein. Mouse complement activation, but not guinea pig complement activation, was partially suppressed on the HSAg-incorporated rabbiterythrocytes.These findings suggest that HSAg has a homologous complement regulating activity. |
| doi_str_mv | 10.1093/intimm/5.7.805 |
| format | Article |
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HSAg Is expressed on most thymocytes, bone marrow cells, immature B cells, and erythrocytes, but not on peripheral T and mature B cells. Although HSAg has been thought to be a differentiation antigen, its actual biological significance remains unknown except for the HSAg on antigen presenting cells. Recently, a new rat antl-HSAg mAb, R13, has been developed. Here It has been found that the mouse complement activation on mouse erythrocytes, but not the human, guinea pig or rabbit complement activations, was enhanced In the presence of the Fab fragment of R13. Afflnlty-purlfled HSAg derived from mouse erythrocytes could be passively Incorporated Into rabbit erythrocytes because of Its molecular characteristic of glycosylphosphatidyl Inosltol-anchored protein. Mouse complement activation, but not guinea pig complement activation, was partially suppressed on the HSAg-incorporated rabbiterythrocytes.These findings suggest that HSAg has a homologous complement regulating activity.</description><identifier>ISSN: 0953-8178</identifier><identifier>EISSN: 1460-2377</identifier><identifier>DOI: 10.1093/intimm/5.7.805</identifier><identifier>PMID: 7690245</identifier><language>eng</language><publisher>Oxford: Oxford University Press</publisher><subject>Animals ; Antigens, CD - physiology ; Antigens, Differentiation - physiology ; Biological and medical sciences ; CD59 Antigens ; Complement Activation ; Fundamental and applied biological sciences. 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HSAg Is expressed on most thymocytes, bone marrow cells, immature B cells, and erythrocytes, but not on peripheral T and mature B cells. Although HSAg has been thought to be a differentiation antigen, its actual biological significance remains unknown except for the HSAg on antigen presenting cells. Recently, a new rat antl-HSAg mAb, R13, has been developed. Here It has been found that the mouse complement activation on mouse erythrocytes, but not the human, guinea pig or rabbit complement activations, was enhanced In the presence of the Fab fragment of R13. Afflnlty-purlfled HSAg derived from mouse erythrocytes could be passively Incorporated Into rabbit erythrocytes because of Its molecular characteristic of glycosylphosphatidyl Inosltol-anchored protein. Mouse complement activation, but not guinea pig complement activation, was partially suppressed on the HSAg-incorporated rabbiterythrocytes.These findings suggest that HSAg has a homologous complement regulating activity.</description><subject>Animals</subject><subject>Antigens, CD - physiology</subject><subject>Antigens, Differentiation - physiology</subject><subject>Biological and medical sciences</subject><subject>CD59 Antigens</subject><subject>Complement Activation</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fundamental immunology</subject><subject>glycosyl-phosphatidylinositol-anchored protein</subject><subject>Glycosylphosphatidylinositols - physiology</subject><subject>Hot Temperature</subject><subject>Immunohematology</subject><subject>Membrane Glycoproteins - physiology</subject><subject>Mice</subject><subject>mouse erythrocyte</subject><subject>Rats</subject><subject>Red blood cell immunology</subject><issn>0953-8178</issn><issn>1460-2377</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkEFP2zAYhi3ExDrgym1SDmi3FNtfHNtHVNG1EtIuAyEulu3YrSGJS-xO49-TkarXyQcf3ud79epB6IrgOcESbkKfQ9fdsDmfC8xO0IxUNS4pcH6KZlgyKAXh4iv6ltILxhiohDN0xmuJacVmaL3ut8GEHGJfRF9sYxfbuIn7VNjY7VrXuT4X2ubwR38y5r3IW1dsnc5lytq0rtDjgo3rL9AXr9vkLg__OXpY3v1erMr7Xz_Xi9v70oIQuawa4ihIAiA8wY03WBgwhnkqNICvqG4wY5a6qpGyppw5YYwEzI31ta85nKMfU-9uiG97l7LqQrKubXXvxt2KMwnjw_8FSV1TIJ-N8wm0Q0xpcF7thtDp4V0RrP5JVpNkxRRXo-Tx4PuheW861xzxg9Uxvz7kOlnd-kH3NqQjVglRV5yMWDlhIWX39xjr4VWNqzhTq6dnxR4fmZTLlZLwATnwlU8</recordid><startdate>19930701</startdate><enddate>19930701</enddate><creator>Hitsumoto, Yasuo</creator><creator>Ohnishi, Hiroshi</creator><creator>Nakano, Akihiro</creator><creator>Hamada, Fumihiko</creator><creator>Saheki, Shuichi</creator><creator>Takeuchi, Nozomu</creator><general>Oxford University Press</general><scope>BSCLL</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>7T5</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>19930701</creationdate><title>Inhibition of homologous complement activation by the heat-stable antigen</title><author>Hitsumoto, Yasuo ; Ohnishi, Hiroshi ; Nakano, Akihiro ; Hamada, Fumihiko ; Saheki, Shuichi ; Takeuchi, Nozomu</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c388t-4d1e2391338f10dfb08b3bb5f28a33f42ad055c2e4d996275e8bb9307bcf6f673</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Animals</topic><topic>Antigens, CD - physiology</topic><topic>Antigens, Differentiation - physiology</topic><topic>Biological and medical sciences</topic><topic>CD59 Antigens</topic><topic>Complement Activation</topic><topic>Fundamental and applied biological sciences. 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HSAg Is expressed on most thymocytes, bone marrow cells, immature B cells, and erythrocytes, but not on peripheral T and mature B cells. Although HSAg has been thought to be a differentiation antigen, its actual biological significance remains unknown except for the HSAg on antigen presenting cells. Recently, a new rat antl-HSAg mAb, R13, has been developed. Here It has been found that the mouse complement activation on mouse erythrocytes, but not the human, guinea pig or rabbit complement activations, was enhanced In the presence of the Fab fragment of R13. Afflnlty-purlfled HSAg derived from mouse erythrocytes could be passively Incorporated Into rabbit erythrocytes because of Its molecular characteristic of glycosylphosphatidyl Inosltol-anchored protein. 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| ispartof | International immunology, 1993-07, Vol.5 (7), p.805-808 |
| issn | 0953-8178 1460-2377 |
| language | eng |
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| source | MEDLINE; Oxford University Press Journals Digital Archive Legacy |
| subjects | Animals Antigens, CD - physiology Antigens, Differentiation - physiology Biological and medical sciences CD59 Antigens Complement Activation Fundamental and applied biological sciences. Psychology Fundamental immunology glycosyl-phosphatidylinositol-anchored protein Glycosylphosphatidylinositols - physiology Hot Temperature Immunohematology Membrane Glycoproteins - physiology Mice mouse erythrocyte Rats Red blood cell immunology |
| title | Inhibition of homologous complement activation by the heat-stable antigen |
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