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In Vitro Release of Lysozyme From Monocytes and Granulocytes
Author(s) -
Haneberg Bjørn,
Glette Johan,
Talstad Ingebrigt,
Sørnes Steinar,
Solberg Claus Ola
Publication year - 1984
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1002/jlb.35.6.573
Subject(s) - lysozyme , zymosan , lysis , monocyte , granulocyte , biology , enzyme , lactate dehydrogenase , myeloperoxidase , in vitro , biochemistry , microbiology and biotechnology , immunology , inflammation
When exposed to zymosan or latex particles or heat‐inactivated staphylococci, freshly prepared human blood monocytes and granulocytes rapidly released a large fraction of their lysozyme content. Within 24 hours the total lysozyme activity in the monocyte suspensions tripled, while it doubled in the granulocyte suspensions, indicating synthesis of the enzyme following release. The monocytes in particular seemed to release and synthesize lysozyme without any other stimulus than contact with lymphocytes and the tube walls. Potassium caseinate in solution did not influence the lysozyme release. Myeloperoxidase and β‐glucuronidase, which in the granulocytes are kept in lysosomal fractions separate from most of the lysozyme, were neither released nor synthesized to a significant degree. Moreover, the minute amount of lactate dehydrogenase released indicated that the lysozyme release was not the result of cell lysis. Accordingly, the monocytes, which are not already stimulated by adherence to nonphagocytosable surfaces, are capable of selective enzyme release similar to that of the granulocytes.

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