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In conclusion, we challenge the view of properdin as a pattern recognition molecule by providing evidence that it binds to different exogenous and endogenous molecular patterns in only a C3-dependent manner.
data indicate that properdin enhances platelet/granulocyte aggregates (PGAs) formation via increased production of C5a, and that inhibition of properdin function has therapeutic potential to limit thromboinflammation in diseases characterized by increased PGA formation
this study shows that RNA interference of properdin in dendritic cells decreased alloantigen-specific T-cell proliferation
studies demonstrate an essential role of properdin oligomerization in vivo while our monomers enable detailed structural insight paving the way for novel modulators of complement.
P serum level expression could be a reliable clinical biomarker to identify patients with underlying surface alternative pathway C5 convertase dysregulation.
can directly interact with neutrophil myeloperoxidase resulting in activation of alternative pathway of complement
In the pathogenesis of renal tubular damage, P can directly bind to PTECs and may accelerate AP activation by surpassing fH regulation
Our data show that physiological forms of human properdin bind directly to human platelets after activation by strong agonists in the absence of C3
Factor h and properdin recognize different epitopes on renal tubular epithelial heparan sulfate.
Properdin released from human polymorphonuclear cells does not bind to zymosan or E. coli, but when incubated in properdin-depleted serum this form of properdin binds efficiently to both substrates in a strictly complement C3-dependent manner.
Properdin and SC5b-9 may be novel biomarkers for future risk of type 2 diabetes in this high-risk population and warrant further investigation.
Immune human serum that contained bactericidal Abs directed against the 2C7 lipooligosaccharide epitope required functional properdin to kill C4BP-binding strains, but not C4BP-nonbinding strains.
report a large Finnish family with a novel mutation in the properdin gene. The mutation is located in exon 9 and changes guanine to adenine at nucleotide 1164 (c.1164G>A) that causes tryptophan to change to a premature stop codon (W388X).
tubular HS as a novel docking platform for alternative pathway activation via properdin, which might play a role in proteinuric renal damage.
levels of properdin are not associated with childhood wheezing and atopy
Human properdin can selectively recognize surfaces and enhance or promote alternative pathway of complement activation.
The conventional mechanism of properdin function is to bind to and stabilize alternative pathway C3 convertases on the surface of Neisseria meningitidis and N. gonorrhoeae.
Properdin presence is associated with increased SC5b-9 excretion and worse renal function.
CFP does not seem to confer any risk for age-related macular degeneration.
A splice site mutation in exon 10 (c.1487-2A>G) was found in the properdin gene and co segregated with biochemically measured properdin deficiency.
Properdin deficiency protects from 5-fluorouracil-induced small intestinal mucositis in a complement activation-independent, interleukin-10-dependent mechanism
We induced anti-myeloperoxidase vasculitis in mice and showed that neither MASP-2- nor properdin-deficient mice were protected, suggesting that alternative pathway activation does not require properdin or the lectin pathway.
The results show that Properdin plays a key role in allergen-induced airway inflammation and represents a potential therapeutic target for human asthma.
Authors conclude that properdin controls the strength of immune responses by affecting humoral as well as cellular phenotypes during acute bacterial infection and ensuing inflammation.
Properdin deficiency exacerbated renal injury in mice lacking complement factor H.
deficiency of properdin in mice with factor H mutation exacerbates C3 glomerulonephritis
Murine antigonococcal antiserum required functional properdin to kill C4BP-binding strains, but not C4BP-nonbinding strains.
properdin may be added to the list of complement proteins which influence lipid metabolism, energy storage and insulin resistance, and further support the hypothesis of a dual role of complement in adipose tissue
At the initial phase of local, zymosan-induced inflammation, properdin-deficient and wild-type mice showed bone erosion, proteoglycan loss and cell infiltration.
Properdin localizes to mast cells, has the ability to directly associate with Escherichia coli DH5alpha, and plays a significant role in the outcome of polymicrobial sepsis.
properdin deficiency attenuates zymosan-induced shock and exacerbates LPS-induced shock.
This gene encodes a plasma glycoprotein that positively regulates the alternative complement pathway of the innate immune system. This protein binds to many microbial surfaces and apoptotic cells and stabilizes the C3- and C5-convertase enzyme complexes in a feedback loop that ultimately leads to formation of the membrane attack complex and lysis of the target cell. Mutations in this gene result in two forms of properdin deficiency, which results in high susceptibility to meningococcal infections. Multiple alternatively spliced variants, encoding the same protein, have been identified.
complement factor P
, properdin P factor, complement
, properdin factor, complement
, Properdin P factor, complement