Results 251 to 260 of about 40,238 (270)

Adsorption of Complement Proteins C3 and C1q

Journal of Colloid and Interface Science, 1996
Abstract Surface localization plays a key but ill defined role in activation of the serum complement system with or without related “opsonic” proteins. The adsorption of key complement components C3 and C1q and various opsonins, e.g., IgG, were therefore studied on different surfaces usingin situellipsometry.
Martin Malmsten, James M. Van Alstine, Ulf R. Nilsson, Bo Lassen   +3 more
openaire   +2 more sources

C1q component of complement binds to fibrinogen and fibrin

Biochemistry, 1988
The interaction of complement component C1q with fibrinogen and fibrin was studied by using a solid-phase direct binding assay. Scatchard analysis of radioiodinated fibrinogen binding to C1q indicated at least two high-affinity binding constants (Kd) calculated as 8.5 and 120 nM. In contrast, binding of radioiodinated fibrin to C1q showed only a single
Leo T. Furcht, Ruth A. Entwistle
openaire   +3 more sources

New insight into the autoimmunogenicity of the complement protein C1q

Molecular Immunology, 2011
C1q along with its physiological role in maintenance of homeostasis and normal function of the immune system is involved in pathological conditions associated with repetitive generation of anti-C1q autoantibodies. The time and events that cause their first appearance are still unknown.
Vishnya Stoyanova, Boriana Deliyska, Vasil Vasilev, Magdalena Tchorbadjieva, Svetla Petrova, Ivanka Tsacheva   +5 more
openaire   +3 more sources

Detection of complement C1q receptors on human spermatozoa

Journal of Reproductive Immunology, 1998
Clq, the first component of the classical complement pathway, is known to play roles in promoting phagocytic events, in addition to its role in activation of complement. Although the molecular events in fertilization leading to the entrance of the spermatozoan into the egg are not well understood, ultrastructural observations suggest that the process ...
Weibing Zhang, Richard Bronson, Berhane Ghebrehiwet, Lucila Oula, Susan Bronson   +4 more
openaire   +3 more sources

Regulation of the alternative pathway of human complement by C1q

Molecular Immunology, 1987
The interaction of C1q with C3b and its effect on C3b activities in the alternative pathway of complement (APC) have been studied. Purified C1q markedly inhibited C3b deposition on and lysis of rabbit erythrocytes by the isolated cytolytic APC. It also blocked formation of the C3 convertase, C3b, Bb as well as binding of Factors B and H to sheep ...
Zvi Fishelson, Hans J. Müller-Eberhard
openaire   +3 more sources

Structure-function studies of the receptors for complement C1q

Biochemical Society Transactions, 2002
C1q is an essential component of the phylo-genetically ancient innate complement (C) system and is crucial to our natural ability to ward off infection and clear toxic cell debris (e.g. amyloid fibrils, apoptotic cells). Several candidate C1q receptors [C1q receptor for phagocytosis enhancement (C1qRp), complement receptor (CR) 1, calreticulin (CRT ...
Philippe Gasque, Eamon Patrick McGreal
openaire   +3 more sources

Interaction of plasma fibronectin with gelatin and complement C1q

Molecular Immunology, 1983
A variety of techniques have been used to examine the interaction of human plasma fibronectin (Fn) with complement C1q in comparison to that with gelatin in phosphate buffered saline at pH 7.4. The precipitation of 3H-Fn by polyethylene glycol (PEG) was shifted to much lower concentrations of the polymer by addition of gelatin, and to a lesser extent ...
Shelesa A. Brew, Shirley I. Miekka, Kenneth C. Ingham   +2 more
openaire   +3 more sources

Roles of Complement C1q in Pneumococcus-Host Interactions

Critical Reviews in Immunology, 2015
The fight between a human host and a bacterial pathogen is highly complicated; each party tries to outshine the other in the race for survival. In humans, the innate immune system--in particular the complement system--functions as the first line of defence against invading pathogens.
Anna M. Blom, Vaibhav Agarwal
openaire   +2 more sources

The conformation of subcomponent C1q of the first component of human complement

Nature, 1980
xxx
John Turton Randall, J. Torbet, S. Gilmour, Raymond A. Dwek, K. J. Willan   +4 more
openaire   +4 more sources

Adiponectin binds C1q and activates the classical pathway of complement

Biochemical and Biophysical Research Communications, 2008
The adipose-specific protein adiponectin binds to a number of target molecules, including damaged endothelium and the surface of apoptotic cells. However, the significance of this binding remains unclear. This study demonstrates the binding of purified C1q to recombinant adiponectin under physiological conditions, and the dependence of this upon Ca(++)
Alexandra Walther, Philip W. Peake, John A. Charlesworth, Yvonne Shen   +3 more
openaire   +3 more sources