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anaphylaxis/phosphatase

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Página 1 a partir de 59 resultados

Glutamine Prevents Late-Phase Anaphylaxis via MAPK Phosphatase 1-Dependent Cytosolic Phospholipase A2 Deactivation.

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BACKGROUND Cytosolic phospholipase A2 (cPLA2) plays a key role in the development of late-phase anaphylaxis. L-Glutamine (Gln), a nonessential amino acid, has anti-inflammatory activity via inhibiting cPLA2. METHODS We used a penicillin-induced murine model of anaphylaxis, and late-phase anaphylaxis
Dual specificity phosphatase DUSP1 (otherwise known as mitogen-activated phosphatase 1 or MKP-1) dephosphorylates MAPKs, particularly p38, and negatively regulates innate immunity. Recent studies have shown that the DUSP1 gene is transcriptionally up-regulated by glucocorticoids (GCs) and that the

PEST-domain-enriched tyrosine phosphatase and glucocorticoids as regulators of anaphylaxis in mice.

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BACKGROUND PEST-domain-enriched tyrosine phosphatase (PEP) is a protein tyrosine phosphatase exclusively expressed in hematopoietic cells. It is a potent negative regulator of T-cell receptor signalling that acts on receptor-coupled protein tyrosine kinases. PEST-domain-enriched tyrosine phosphatase

PLASMA PHOSPHATASE, CHOLINESTERASE AND PEPTONASE IN ANAPHYLACTIC SHOCK.

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[Alkaline phosphatase activity of rat serum after anaphylactoid shock].

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The ability of food proteins to resist digestion in simulated gastric fluid (SGF) correlates with allergenic potential. The purpose of the current investigations was to determine whether this association is due solely to the failure of unstable proteins to elicit an immune response when administered
Several known antiallergic agents, including cromolyn sodium and a series of pyrido[2,1-b]quinazolines, inhibit human alkaline phosphatase (ALP), a membranal enzyme associated with calcium uptake in certain tissues. A comparison of ALP and rat passive cutaneous anaphylaxis (PCA) inhibition indicates
BACKGROUND CD45, receptor-type protein tyrosine phosphatases (PTPases) are essential components of signaling through both the T cell receptor and the B cell antigen receptor. However, the functional significance of CD45 in the signaling pathway through the high-affinity immunoglobulin (Ig) E

Cytoenzymatic investigations of parathyroid glands in acute anaphylactic shock of guinea pig.

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50 guinea pigs were allergized three times in 3 days intervals by subcutaneous injection of 25% solution of egg-white in physiological saline in a dose of 0-1 ml/100 g of body weight. On the 21 day after the last injection the animals were exposed to aerosol of antigen of egg-white. 11 animals died

SHP-1 regulation of mast cell function in allergic inflammation and anaphylaxis.

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Allergic inflammation and severe allergic reactions (anaphylaxis) are important in allergen induced diseases. Bacterial products such as lipopolysaccharide (LPS) are ubiquitous and can facilitate allergen induced Th2 immune responses. Phosphatase SHP-1 is critical in regulating immunological

Protein kinase CK2/PTEN pathway plays a key role in platelet-activating factor-mediated murine anaphylactic shock.

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Platelet-activating factor (PAF) is a major mediator in the induction of fatal hypovolemic shock in murine anaphylaxis. This PAF-mediated effect has been reported to be associated with PI3K/Akt-dependent eNOS-derived NO. The phosphatase and tensin homolog deleted on chromosome 10 (PTEN) is
Assessment of the allergenic potency of enzymes involves the use of a guinea pig model in which specific IgG1 antibody titers are used as the endpoint. The in vivo passive cutaneous anaphylaxis (PCA) assay is used to measure specific IgG1 antibody. This report describes the development and

Comparison of clinical findings between dogs with suspected anaphylaxis and dogs with confirmed sepsis.

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OBJECTIVE To compare clinical signs, laboratory test results, and imaging findings between dogs with suspected anaphylaxis and dogs with sepsis. DESIGN Retrospective case-case study. ANIMALS 10 dogs with suspected anaphylaxis and 22 dogs with confirmed sepsis that met the criteria for systemic

Protein tyrosine phosphatase 1B (PTP1B) is dispensable for IgE-mediated cutaneous reaction in vivo.

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Mast cells play a critical role in allergic reactions. The cross-linking of FcεRI-bound IgE with multivalent antigen initiates a cascade of signaling events leading to mast cell activation. It has been well-recognized that cross linking of FcεRI mediates tyrosine phosphorylation. However, the
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