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The binding of tissue prokallikrein to isolated human neutrophils
Author(s) -
Anders Jonas,
Kemme Michael
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00598-2
Subject(s) - kallikrein , chemistry , endocytosis , in vitro , binding site , biochemistry , microbiology and biotechnology , receptor , enzyme , biology
We have investigated the binding of human tissue kallikrein and the corresponding proenzyme to isolated human lymphocytes and neutrophils, respectively, by the means of steady‐state binding assays. It was demonstrated that only prokallikrein bound to washed neutrophils in a time‐dependent, specific and saturable manner, whereas in vitro binding of activated kallikrein to neutrophils or lymphocytes could be excluded. Our data provide strong evidence for the specific interaction of prokallikrein with intact human neutrophils and indicate a neutrophil surface binding site for the tissue kallikrein precursor which could be involved in kallikrein endocytosis and selective prokallikrein‐to‐kallikrein conversion.