Fig. 2.
Fig. 2. Model of chemokine receptor activation and signal transduction for IL-8 and neutrophils. / IL-8 binding to CXCR1 or CXCR2 causes guanosine triphosphate displacement of guanosine diphosphate in the Gαi2subunit, which allows dissociation of Gαi2 from Gβγ. Gβ activates phospholipase C (PLCβ), which cleaves PIP2 into the second messengers DAG and IP3. DAG activates PKCβ, whereas IP3 causes the release of calcium from intracellular stores. The rapid rise in intracellular calcium activates PLD. Meanwhile Gαi2directly activates PTK. These activate MAP kinases and phosphorylate serine and threonine residues on the C-termini of CXCR1 and CXCR2, leading to receptor inactivation. MAP kinases activate phospholipase A2. DAG, intracellular calcium, PKC, and phospholipase A2 (PLA2) all interact with specific cell activation mechanisms, leading to cell motility, degranulation, release of superoxide anions, and modification of integrin avidity.

Model of chemokine receptor activation and signal transduction for IL-8 and neutrophils.

IL-8 binding to CXCR1 or CXCR2 causes guanosine triphosphate displacement of guanosine diphosphate in the Gαi2subunit, which allows dissociation of Gαi2 from Gβγ. Gβ activates phospholipase C (PLCβ), which cleaves PIP2 into the second messengers DAG and IP3. DAG activates PKCβ, whereas IP3 causes the release of calcium from intracellular stores. The rapid rise in intracellular calcium activates PLD. Meanwhile Gαi2directly activates PTK. These activate MAP kinases and phosphorylate serine and threonine residues on the C-termini of CXCR1 and CXCR2, leading to receptor inactivation. MAP kinases activate phospholipase A2. DAG, intracellular calcium, PKC, and phospholipase A2 (PLA2) all interact with specific cell activation mechanisms, leading to cell motility, degranulation, release of superoxide anions, and modification of integrin avidity.

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