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MECHANISMS OF LYSOSOMAL ENZYME RELEASE FROM LEUKOCYTES EXPOSED TO IMMUNE COMPLEXES AND OTHER PARTICLES
Human PMN release lysosomal enzymes (β-glucuronidase, acid phosphatase) when exposed to immune complexes, but do not release cytoplasmic LDH. The cells remain viable, and failure of LDH to appear in supernatants is not due to selective absorption or inactivation. Release of enzymes is not due to pla...
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
1971
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2139061/ https://www.ncbi.nlm.nih.gov/pubmed/19867363 |
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author | Weissmann, Gerald Zurier, Robert B. Spieler, Paul J. Goldstein, Ira M. |
author_facet | Weissmann, Gerald Zurier, Robert B. Spieler, Paul J. Goldstein, Ira M. |
author_sort | Weissmann, Gerald |
collection | PubMed |
description | Human PMN release lysosomal enzymes (β-glucuronidase, acid phosphatase) when exposed to immune complexes, but do not release cytoplasmic LDH. The cells remain viable, and failure of LDH to appear in supernatants is not due to selective absorption or inactivation. Release of enzymes is not due to platelet contamination and is only partially enhanced by fresh serum. The selective release of lysosomal enzymes after uptake of complexes resembles that induced by inert particles of zymosan, and can be distinguished from the concurrent release of all enzymes after cell death induced by membrane-lytic crystals of MSU. Uptake of complexes, zymosan, or MSU particles is accompanied by concomitant increases in C-1 oxidation of glucose. Although MSU-induced damage can be retarded by the presence of Tris buffer, immune complexes and zymosan selectively release lysosomal hydrolases in the presence or absence of Tris buffer. Agents which elevate the level, within cells, of cAMP (PGE(1), theophylline, 2-CA) and cAMP itself inhibit the selective extrusion of acid hydrolases from leukocytes without affecting the viability of cells. Leukocytes may respond to immune particles by regurgitating a portion of their lysosomal hydrolases during phagocytosis. |
format | Text |
id | pubmed-2139061 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1971 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21390612008-04-17 MECHANISMS OF LYSOSOMAL ENZYME RELEASE FROM LEUKOCYTES EXPOSED TO IMMUNE COMPLEXES AND OTHER PARTICLES Weissmann, Gerald Zurier, Robert B. Spieler, Paul J. Goldstein, Ira M. J Exp Med Mediation of Immunological Injury Human PMN release lysosomal enzymes (β-glucuronidase, acid phosphatase) when exposed to immune complexes, but do not release cytoplasmic LDH. The cells remain viable, and failure of LDH to appear in supernatants is not due to selective absorption or inactivation. Release of enzymes is not due to platelet contamination and is only partially enhanced by fresh serum. The selective release of lysosomal enzymes after uptake of complexes resembles that induced by inert particles of zymosan, and can be distinguished from the concurrent release of all enzymes after cell death induced by membrane-lytic crystals of MSU. Uptake of complexes, zymosan, or MSU particles is accompanied by concomitant increases in C-1 oxidation of glucose. Although MSU-induced damage can be retarded by the presence of Tris buffer, immune complexes and zymosan selectively release lysosomal hydrolases in the presence or absence of Tris buffer. Agents which elevate the level, within cells, of cAMP (PGE(1), theophylline, 2-CA) and cAMP itself inhibit the selective extrusion of acid hydrolases from leukocytes without affecting the viability of cells. Leukocytes may respond to immune particles by regurgitating a portion of their lysosomal hydrolases during phagocytosis. The Rockefeller University Press 1971-09-01 /pmc/articles/PMC2139061/ /pubmed/19867363 Text en Copyright © 1971 by The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Mediation of Immunological Injury Weissmann, Gerald Zurier, Robert B. Spieler, Paul J. Goldstein, Ira M. MECHANISMS OF LYSOSOMAL ENZYME RELEASE FROM LEUKOCYTES EXPOSED TO IMMUNE COMPLEXES AND OTHER PARTICLES |
title | MECHANISMS OF LYSOSOMAL ENZYME RELEASE FROM LEUKOCYTES EXPOSED TO IMMUNE COMPLEXES AND OTHER PARTICLES |
title_full | MECHANISMS OF LYSOSOMAL ENZYME RELEASE FROM LEUKOCYTES EXPOSED TO IMMUNE COMPLEXES AND OTHER PARTICLES |
title_fullStr | MECHANISMS OF LYSOSOMAL ENZYME RELEASE FROM LEUKOCYTES EXPOSED TO IMMUNE COMPLEXES AND OTHER PARTICLES |
title_full_unstemmed | MECHANISMS OF LYSOSOMAL ENZYME RELEASE FROM LEUKOCYTES EXPOSED TO IMMUNE COMPLEXES AND OTHER PARTICLES |
title_short | MECHANISMS OF LYSOSOMAL ENZYME RELEASE FROM LEUKOCYTES EXPOSED TO IMMUNE COMPLEXES AND OTHER PARTICLES |
title_sort | mechanisms of lysosomal enzyme release from leukocytes exposed to immune complexes and other particles |
topic | Mediation of Immunological Injury |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2139061/ https://www.ncbi.nlm.nih.gov/pubmed/19867363 |
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