Purified complement C3b triggers phagocytosis and activation of human neutrophils via complement receptor 1. [PDF]
AbstractThe complement system provides vital immune protection against infectious agents by labeling them with complement fragments that enhance phagocytosis by immune cells. Many details of complement-mediated phagocytosis remain elusive, partly because it is difficult to study the role of individual complement proteins on target surfaces.
Boero E+12 more
europepmc +7 more sources
Ficolin-3 Activates Complement and Triggers Necroptosis in Cholangiocarcinoma Cells via the RIPK1/RIPK3/MLKL Signaling Pathway. [PDF]
FCN3‐mediated activation of the lectin complement pathway via MASP2 binding induces necroptosis in cholangiocarcinoma cells through the RIPK1/RIPK3/MLKL axis. ABSTRACT Ficolin 3 (FCN3) is a pattern recognition molecule that activates the complement system via the lectin pathway.
Zhang Z+8 more
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Purification of the human complement control protein C3b inactivator [PDF]
An alternative method of isolation from human plasma is described for C3b inactivator, C3bINA, the proteinase that in conjunction with either beta 1H or C4b-binding protein will hydrolyse respectively C3b or C4b, the activation products of the third, C3 and fourth, C4, components of complement. The purification is by chromatography of plasma on columns
R R Porter, L G Crossley
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Inhibition of neutrophil function by fluid phase C3b of complement [PDF]
A high-molecular-weight fragment of C3 was isolated from normal human serum by column chromatography, was generated by incubation of serum at 37 degrees C with inulin, and was produced from highly purified C3 by limited digestion with trypsin. This product was shown to inhibit the antibacterial function of neutrophils by using Escherichia coli O75 as ...
Cora K. Ogle+2 more
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Effect of complement-protein-C3b density on the binding of complement factor H to surface-bound C3b [PDF]
Various amounts of the activation fragment C3b of the complement (C) protein C3 were coupled to Sepharose 4B by catalysis with the C3 convertase of the alternative pathway of C. The binding of radioactively labelled C proteins B and H (= factor H) to the C3b-carrying particles was assayed. It was found that the relative binding of H, but not of B, fell
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Structure of C3b reveals conformational changes that underlie complement activity [PDF]
Resistance to infection and clearance of cell debris in mammals depend on the activation of the complement system, which is an important component of innate and adaptive immunity. Central to the complement system is the activated form of C3, called C3b, which attaches covalently to target surfaces to amplify complement response, label cells for ...
Janssen, B.J.C.+4 more
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Disulfide bridges in human complement component C3b
The disulfide bridges of human complement component C3b, derived from C3 by removal of the 77‐residue C3a, have been determined. The 10 bridges are Cys537‐Cys794, Cys605‐Cys640, Cys851‐Cys1491, Cys1079‐Cys1169, Cys1336‐Cys1467, Cys1367‐Cys1436, Cys1448‐Cys1489, Cys1496‐Cys1568, Cys1515‐Cys1639, and Cys1615‐Cys1624.
Lars Sottrup-Jensen, Klavs Dolmer
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TWO DIFFERENT COMPLEMENT RECEPTORS ON HUMAN LYMPHOCYTES [PDF]
In the present study it was shown that normal peripheral lymphocytes have two different complement receptors: one for C3b (the immune adherence receptor) and one for C3b subsequent to its cleavage by C3b inactivator. The two receptors are not cross-reactive and were shown by tests with various antisera to be antigenically distinct.
Gordon D. Ross+3 more
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THE INTERACTION OF ARENICIN-1 WITH C3B COMPLEMENT PROTEIN
The complement system and antimicrobial peptides (AMPs) are known to be vital humoral factors of innate immunity. Earlier we showed the double-sided influence of arenicin-1 (Ar-1), the AMP from a sea polychaeta Arenicola marina, on the complement activation.
M. N. Berlov+7 more
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Retraction Note: The structure of complement C3b provides insights into complement activation and regulation [PDF]
This Letter is retracted by Nature. This follows an investigation by the University of Alabama at Birmingham, Alabama, USA, of structures deposited into the Protein Data Bank under accession 2HR0 by H. M. Krishna Murthy. Co-authors who agree with the Retraction.
A. Abdul Ajees+5 more
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