Immunovisualisation of plasma prekallikrein and H-kininogen on human neutrophils and in human hepatocytes.
Both plasma prekallikrein and H-kininogen were immunolocalised in human hepatocytes by the use of immunocytochemical techniques in conjunction with the confocal optical scanning microscopy. In contrast, both proteins were demonstrated on the external surface of human blood neutrophils. However, detection of H-kininogen on non-fixed but not on fixed neutrophils with the anti-domain 6 antibody (directed at the prekallikrein binding site on H-kininogen), suggested that access to the epitope was blocked by the presence of the bound plasma prekallikrein. Therefore, we prepose that H-kininogen provides the binding site for plasma prekallikrein on circulating neutrophils.
Henderson
L M
LM
Department of Biochemistry, University of Bristol, U.K.
Figueroa
C D
CD
Muller-Esterl
W
W
Stain
A
A
Bhoola
K D
KD
D000328:Adult; D001665:Binding Sites; D002462:Cell Membrane / Q000378:metabolism; D006801:Humans; D007150:Immunohistochemistry; D066298:In Vitro Techniques; D007704:Kininogens / Q000378:metabolism*; D008099:Liver / Q000378:metabolism; D009504:Neutrophils / Q000378:metabolism; D011288:Prekallikrein / Q000378:metabolism*
D007704:Kininogens; D011288:Prekallikrein