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Molecular Determinants of the Substrate Specificity of the Complement-initiating Protease, C1r [PDF]

Journal of Biological Chemistry, 2013
The serine protease, C1r, initiates activation of the classical pathway of complement, which is a crucial innate defense mechanism against pathogens and altered-self cells. C1r both autoactivates and subsequently cleaves and activates C1s. Because complement is implicated in many inflammatory diseases, an understanding of the interaction between C1r ...
Lakshmi C Wijeyewickrema, Robert Pike, Itamar Kass   +2 more
exaly   +3 more sources

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A polymorphism in the complement component C1r is not associated with sporadic Alzheimer's disease

Neuroscience Letters, 2003
A growing body of evidence suggests that Alzheimer's disease (AD) is associated with local inflammation processes. Complement activation is one of the cardinal pathological features of the inflammation. Intensive AD association studies investigating polymorphisms in inflammatory-related genes have been recently performed, mainly in cytokines, but much ...
Esther Kahana, Hanna Rosenmann, Zeev Meiner   +2 more
exaly   +5 more sources

Revisiting the mechanism of the autoactivation of the complement protease C1r in the C1 complex: Structure of the active catalytic region of C1r

Molecular Immunology, 2008
C1r is a modular serine protease which is the autoactivating component of the C1 complex of the classical pathway of the complement system. We have determined the first crystal structure of the entire active catalytic region of human C1r. This fragment contains the C-terminal serine protease (SP) domain and the preceding two complement control protein (
Peter Gal, Veronika Harmat, József Kardos   +2 more
exaly   +4 more sources

Clinical presentations and molecular basis of complement C1r deficiency in a male African–American patient with systemic lupus erythematosus

Lupus, 2011
Homozygous deficiencies of early components for complement activation are among the strongest genetic risk factors for human systemic lupus erythematosus (SLE).
F C Arnett, C Y Yu
exaly   +2 more sources

An Improved Method for Complement Subcomponent C1R Typing

Journal of Forensic Sciences, 1990
Abstract An improved method has been developed for the reliable classification of different C1R genetic variant forms from human serum or plasma. The method combines the use of neuraminidase-digested samples followed by monodimensional isoelectric focusing in the pH range 5 to 8 followed by immunoblotting.
M I, Kamboh, R E, Ferrell
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Characterization of the activation of the human C1r complement molecule

Molecular Immunology, 1982
The proenzyme form of C1r was isolated by sequential chromatography from the euglobulin fraction of human serum on DEAE-Sepharose 6B-CL, CM-Sepharose 6B-CL and Sepharose S-300-CL. This C1r had the tendency to spontaneously activate within 60-90 min of incubation at 37 degrees C in presence of EDTA and more slowly in the presence of Ca2+.
J, Bauer, G, Valet
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Nucleotide sequence of the cDNA coding for human complement C1r

Biochemistry, 1986
C1r is a zymogen of a serine protease that is involved in the activation of the first component of the classical pathway of the complement system. cDNAs coding for human C1r have been isolated from libraries prepared from poly(A) RNA from human liver and Hep G2 cells.
S P, Leytus, K, Kurachi, K S, Sakariassen, E W, Davie   +3 more
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A rapid and efficient method for the purification of the complement subcomponents C1r and C1s in zymogen form using fast protein chromatography

Journal of Immunological Methods, 1988
The purification of the subcomponents C1r and C1s of the first component of complement involves multiple steps and is time-consuming. This accounts for the frequently observed partial activation of the subcomponents.
Manuel Peitsch, H Isliker
exaly   +4 more sources

Blocking activation of the C1r zymogen defines a novel mode of complement inhibition

Journal of Biological Chemistry
Many hematophagous organisms secrete inhibitors of the coagulation and complement systems as constituents of their salivary fluid. Whereas previous studies on salivary gland extracts from the sandfly Lutzomyia longipalpis identified SALO (salivary anticomplement from L.
Brian Geisbrecht, Brandon Garcia, Samuel Bouyain   +2 more
exaly   +3 more sources

Physicochemical and Functional Characterization of the C1r Subunit of the First Complement Component

The Journal of Immunology, 1976
Abstract C1r was isolated from serum by an improved method and found to be a glycoprotein with a sedimentation coefficient of 7.0S. Under conditions of physiologic ionic strength and pH, C1r consists of two apparently identical noncovalently linked 95,000 dalton polypeptide chains.
R J, Ziccardi, N R, Cooper
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