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alpha-Kallikrein was prepared using an improved purification protocol (Burger, D., Schleuning, W.-D. and Schapira, M. (1986) J. Biol. Chem. 261, 324-327) and was employed to reevaluate our previous observations indicating that kallikrein activates blood neutrophils by a mechanism requiring an uncleaved Mr 52,000 NH2-terminal heavy chain. Cellular activation was evaluated by measuring neutrophil aggregation, release of both vitamin B12 binding capacity and myeloperoxidase, and generation of superoxide anion. Whereas all these indicators were evoked by exposing neutrophils to f-Met-Leu-Phe, phorbol myristate acetate, zymosan activated serum, or the calcium ionophore A 23187, we show here that neutrophils incubated with alpha-kallikrein remained unactivated. Moreover, we demonstrate that this lack of activation is accompanied by an inability of neutrophils to specifically bind alpha-kallikrein.
D Burger, and
P Maechler, and
M Schapira
January 1971,
Progress in hematology,
D Burger, and
P Maechler, and
M Schapira
July 2011,
Biological chemistry,
D Burger, and
P Maechler, and
M Schapira
June 1973,
The American journal of physiology,
D Burger, and
P Maechler, and
M Schapira
January 1981,
Sovetskaia meditsina,
D Burger, and
P Maechler, and
M Schapira
May 1982,
The Journal of clinical investigation,
D Burger, and
P Maechler, and
M Schapira
July 2009,
Cardiovascular & hematological agents in medicinal chemistry,
D Burger, and
P Maechler, and
M Schapira
January 1988,
Sovetskaia meditsina,
D Burger, and
P Maechler, and
M Schapira
September 2010,
Biological chemistry,
D Burger, and
P Maechler, and
M Schapira
March 1983,
Archives of surgery (Chicago, Ill. : 1960),
D Burger, and
P Maechler, and
M Schapira
February 1985,
Chirurgia e patologia sperimentale,
