scholarly journals Activation and function of human Hageman factor. The role of high molecular weight kininogen and prekallikrein.

1977 ◽  
Vol 60 (1) ◽  
pp. 18-31 ◽  
Author(s):  
H L Meier ◽  
J V Pierce ◽  
R W Colman ◽  
A P Kaplan
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
High Molecular Weight Kininogen ◽  
Hageman Factor ◽  
And Function

scholarly journals The Role of High Molecular Weight Kininogen and Prothrombin as Cofactors in the Binding of Factor XI A3 Domain to the Platelet Surface

2000 ◽  
Vol 275 (33) ◽  
pp. 25139-25145 ◽  
Author(s):  
David H. Ho ◽  
Karen Badellino ◽  
Frank A. Baglia ◽  
Mao-Fu Sun ◽  
Ming-Ming Zhao ◽  
...  
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
High Molecular Weight Kininogen ◽  
Factor Xi ◽  
Platelet Surface

scholarly journals Hageman factor, high molecular weight kininogen, and prekallikrein in chronic liver disease.

1986 ◽  
Vol 39 (9) ◽  
pp. 1003-1005 ◽  
Author(s):  
C Cordova ◽  
F Violi ◽  
C Alessandri ◽  
D Ferro ◽  
M Saliola ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Liver Disease ◽  
Chronic Liver Disease ◽  
High Molecular Weight ◽  
Chronic Liver ◽  
High Molecular Weight Kininogen ◽  
Hageman Factor

The Role of Urokinase Receptor (uPAR) In Efferocytosis: uPAR Engulfs Apoptotic Cells via a Phosphatidylserine Pathway Mediated by Plasma High Molecular Weight Kininogen

Blood ◽  
2010 ◽  
Vol 116 (21) ◽  
pp. 929-929 ◽  
Author(s):  
Aizhen Yang ◽  
Jihong Dai ◽  
Raymond B. Birge ◽  
Yi Wu
Keyword(s):  
Molecular Weight ◽  
Flow Cytometry ◽  
Cell Surface ◽  
High Molecular Weight ◽  
Apoptotic Cell ◽  
Annexin V ◽  
Apoptotic Cells ◽  
High Molecular Weight Kininogen ◽  
Viable Cells

Abstract Abstract 929 Phagocytosis of apoptotic cells by phagocytes, also known as efferocytosis, is essential for maintaining normal tissue homeostasis and regulating immune responses. Defects in rapid clearance of apoptotic cells lead to the release of immunogenic cellular contents, which may cause tissue damage and autoimmune disease. Phagocytic receptors differentiate apoptotic cells from viable cells by recognizing ‘don't eat- or eat-me’ signals on the cell surface. Recently, we and others have reported the role of uPAR in mediating efferocytosis. In this study, we examined the mechanism by which uPAR recognizes and internalizes apoptotic cells. By flow cytometry-based in vivo and in vitro phagocytosis assay, we found that in knockout mice the lack of uPAR expression on macrophages decreased their apoptotic cell engulfing activity by >35%. Conversely, soluble uPAR and polyclonal anti-uPAR antibodies (Ab) suppressed the internalization of apoptotic cells by macrophages. However, there was no defect in uPAR-/- macrophage uptake of viable cells, suggesting that uPAR plays a specific role in phagocytosis of apoptotic cells. We established a HEK 293 cell line expressing human full-length uPAR (293-uPAR). In these cells, uPAR-mediated phagocytosis of apoptotic cells was completely blocked by annexin V in the presence of calcium. The effect of annexin V was not observed in the absence of calcium, indicating that uPAR internalizes apoptotic cells through a phosphatidylserine pathway. We also found that uPAR-mediated uptake of apoptotic cells was completely prevented under serum-free conditions. To identify plasma proteins that may opsonize the uPAR function, we used immunodepletion method to test three known uPAR-binding proteins, vitronectin, uPA and high molecular weight kininogen (HK). Depletion of HK from serum by a polyclonal anti-HK Ab significantly reduced the engulfment of apoptotic cells by either macrophages or 293-uPAR cells in a co-culture system. In contrast, depletion of vitronectin or uPA from serum had little effect. uPAR is a GPI-anchored protein. Upon sucrose gradient ultracentrifugation, the majority of uPAR molecules were co-localized with membrane-bound HK in lipid rafts. The binding capacity of HK to apoptotic cell surface was further analyzed by flow cytometry. Phycoerythrin-labeled HK bound to apoptotic cells in a concentration-dependent manner, saturating at 300 nM. In contrast, HK did not bind to viable cells at concentrations up to 1200 nM. It is known that HK is a key component of the plasma contact system and that apoptotic cells potentiate factor Xa formation. Our new findings of the uPAR-HK-phosphatidylserine axis in efferocytosis suggest that this pathway may modulate the coagulation cascade on the surface of apoptotic cells. This pathway may also play a role in the pathogenesis of autoimmune and thrombotic disease. Disclosures: No relevant conflicts of interest to declare.

Prekallikrein, hageman factor, and high molecular weight kininogen in liver cirrhosis

1986 ◽  
Vol 41 ◽  
pp. 41
Author(s):  
C. Cordova ◽  
F. Violi ◽  
C. Alessandri ◽  
D. Ferro ◽  
M. Saliola ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Liver Cirrhosis ◽  
High Molecular Weight ◽  
High Molecular Weight Kininogen ◽  
Hageman Factor

scholarly journals An essential role of high-molecular-weight kininogen in endotoxemia

2017 ◽  
Vol 214 (9) ◽  
pp. 2649-2670 ◽  
Author(s):  
Aizhen Yang ◽  
Zhanli Xie ◽  
Bo Wang ◽  
Robert W. Colman ◽  
Jihong Dai ◽  
...  
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Light Chain ◽  
Essential Role ◽  
High Molecular Weight Kininogen ◽  
Core Oligosaccharide ◽  
E Coli ◽  
Chain Form ◽  
Deficient Mice

In this study, we show that mice lacking high-molecular-weight kininogen (HK) were resistant to lipopolysaccharide (LPS)-induced mortality and had significantly reduced circulating LPS levels. Replenishment of HK-deficient mice with human HK recovered the LPS levels and rendered the mice susceptible to LPS-induced mortality. Binding of HK to LPS occurred through the O-polysaccharide/core oligosaccharide, consistent with the ability to bind LPS from K. pneumoniae, P. aeruginosa, S. minnesota, and different E. coli strains. Binding of LPS induced plasma HK cleavage to the two-chain form (HKa, containing a heavy chain [HC] and a light chain [LC]) and bradykinin. Both HKa and the LC, but not the HC, could disaggregate LPS. The light chain bound LPS with high affinity (Kd = 1.52 × 10−9 M) through a binding site in domain 5 (DHG15). A monoclonal antibody against D5 significantly reduced LPS-induced mortality and circulating LPS levels in wild-type mice. Thus, HK, as a major LPS carrier in circulation, plays an essential role in endotoxemia.

Possible physiological role of new peptide fragments released from bovine high molecular weight kininogen by plasma kallikrein

1977 ◽  
Vol 26 (2) ◽  
pp. 115-120 ◽  
Author(s):  
Oh-ishi Sachiko ◽  
Katori Makoto ◽  
Yong Nam Han ◽  
Iwanaga Sadaaki ◽  
Kato Hisao ◽  
...  
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Physiological Role ◽  
Plasma Kallikrein ◽  
Peptide Fragments ◽  
High Molecular Weight Kininogen
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