Studies on the human plasma kallikrein-kinin system: alpha-kallikrein does not directly activate blood neutrophils.
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.
Burger
D
D
Rheumatology Division, Hôpital Cantonal Universitaire, Geneva, Switzerland.
Maechler
P
P
Schapira
M
M
D001667:Binding, Competitive; D002449:Cell Aggregation; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007610:Kallikreins / Q000502:physiology*; D007705:Kinins / Q000502:physiology*; D009504:Neutrophils / Q000502:physiology*; D013481:Superoxides / Q000378:metabolism; D015054:Zymosan / Q000494:pharmacology
D007705:Kinins; D013481:Superoxides; D015054:Zymosan; D007610:Kallikreins