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Assembly of contact-phase factors on the surface of the human neutrophil
membrane
LM Henderson, CD Figueroa, W Muller-Esterl and KD Bhoola
Department of Biochemistry, University of Bristol, UK.
H-kininogen (HK), a major factor involved in contact-phase activation, was
recently immunolocalized on the external surface of human neutrophils.
Experiments were, therefore, designed to consider the question of whether
the complete assembly of contact factors occurs on the outer surface of the
neutrophil membrane. By immunolocalization techniques, and using specific
antibodies directed against the various contact factors, we now demonstrate
that plasma prekallikrein (PK), factor XI (FXI), and factor XII (FXII) are
present on the exterior face of the human neutrophil. Failure to localize
HK, PK, or FXI by monoclonal antibodies directed to their reciprocal
binding sites, and displacement of PK/FXI by peptide HK31, which mimics the
relevant binding site(s) of HK, suggested that prekallikrein and FXI are
anchored to the neutrophil membrane through attachment to the kininogen
molecule. Probing of the kinin moiety by a specific antibody showed that
kininogen molecules bound to the neutrophil cell membrane contain the kinin
sequence, which can be released by plasma kallikrein or by tissue
kallikrein. Our results led us to the novel conclusion that neutrophils
provide a circulating platform for the components of the contact-phase
system.
Volume 84,
Issue 2,
pp. 474-482,
07/15/1994
Copyright © 1994 by The American Society of Hematology
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