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lower DEFA1/DEFA3 copy number (CNV < 7) is associated with higher susceptibility to hospital-acquired infections (HAIs) in critically ill patients, indicating that host genetic factors are involved in the development of HAIs
Human Neutrophil Peptide 1 directly binds and neutralizes Exotoxin A of Pseudomonas aeruginosa.
Pretreatment of component b with human alpha-defensin-1 prior to addition of component a of Clostridium perfringens iota toxin prevented intoxication implicating that alpha-defensin-1 interacts with the toxin b component to prevent the formation of biologically active iota toxin on cells.
DEFA1, DEFA3, and PPBP expression was significantly increased in hyperlipidemia and coronary heart disease patients compared with controls.
HNP1 upregulation of cytokine expression in pDCs was inhibited by blockade of NF-kappaB activation or knockdown of IRF1, demonstrating the importance of these two signaling events in HNP1-induced pDC activation.
these results demonstrate that HNPs1-3 may be potent inhibitors of ADAMTS13 activity, likely by binding to the central A2 domain of VWF and physically blocking ADAMTS13 binding.
Increased alpha-defensin expression is associated with risk of coronary heart disease in hyperlipidemia patients.
Levels in sera and CSF were elevated in Alzheimer disease patients compared with controls.
the decreased HNP-1 production in the polymorphonuclear phagocytes form elderly individuals might have an important participation in the increased susceptibility to infectious diseases.
Increased levels of neutrophil defensin 1, apolipoprotein E, clusterin, and zinc-alpha-2-glycoprotein are present in carotid atherosclerotic plaque secretomes.
HNP1 functions as a "molecular brake" on macrophage-driven inflammation, ensuring both pathogen clearance and the resolution of inflammation with minimal bystander tissue damage.
HP1 binding to the chromosomal passenger complex becomes particularly important when Aurora B phosphorylates kinetochore targets to eliminate erroneous microtubule attachments
data demonstrate that HNP-1 induces IL-8 production not only through P2Y6, but also through additional P2 receptors via an ERK1/2-dependent mechanism in intestinal epithelial cells.
Results showed that NO and NaNO2 can be considered as factors regulating the chemoattractant properties of defensin HNP1 in neutrophils
Overexpression of DEFA1 retained independent prognostic significance for B-ALL outcome.
The expression of alpha-defensins 1, 2 and 3 is up-regulated in hypercholesteremia.
Defensins promote the differentiation into activated CD91(bright) dendritic cells.
Elevated DEFA1 levels in diabetes are independent of DEFA1 copy numbers.
The AD-1 assay offers another test with high sensitivity and specificity for diagnosing a prosthetic joint infection.
The concentrations of LL37, alpha-1, beta-1 and beta-2 defensins were determined by ELISA. Serum AMPs did not change during attacks and did not correlate with acute phase reactants.
we engineered a monoclonal antibody against HNP-1 to block the interaction with P2X7 and found that the blocking antibody protected mice carrying high copy number of DEFA1/DEFA3 from lethal sepsis. We thus demonstrate that DEFA1/DEFA3 copy number variation strongly modulates sepsis development in vivo and explore a paradigm for the precision treatment of sepsis tailored by individual genetic information.
Mouse adenovirus 2 infection was enhanced by enteric alpha-defensins.
Decreased alpha-defensin is associated with intestinal inflammation in a model of inflammatory bowel disease.
cryptdin-1 and cryptdin-4 exhibit circadian oscillation
the Arg5-Glu13 salt bridge in alpha-defensin is conserved for defensin in vivo stability
MMP-7 activates mouse paneth cell pro-alpha-defensins
Defensins are a family of microbicidal and cytotoxic peptides thought to be involved in host defense. They are abundant in the granules of neutrophils and also found in the epithelia of mucosal surfaces such as those of the intestine, respiratory tract, urinary tract, and vagina. Members of the defensin family are highly similar in protein sequence and distinguished by a conserved cysteine motif. The protein encoded by this gene, defensin, alpha 1, is found in the microbicidal granules of neutrophils and likely plays a role in phagocyte-mediated host defense. Several alpha defensin genes are clustered on chromosome 8. This gene differs from defensin, alpha 3 by only one amino acid. This gene and the gene encoding defensin, alpha 3 are both subject to copy number variation.
defensin, alpha 1, myeloid-related sequence
, defensin, alpha 2
, myeloid-related sequence
, neutrophil defensin 1
, alpha-defensin 1
, defensin related cryptdin peptide 1
, defensin-related cryptdin peptide
, defensin alpha 1
, Paneth cell-specific alpha-defensin 2
, alpha-defensin 5, Paneth cell-specific
, defensin NP-2
, neutrophil antibiotic peptide NP-1
, neutrophil antibiotic peptide NP-2
, neutrophil defensin 2
, Neutrophil defensin 1
, Neutrophil defensin 3
, neutrophil defensin 8