Isozyme-selective stimulation of phospholipase C-β2 by G protein βγ-subunits

Camps, Montserrat; Carozzi, Amanda; Schnabel, Petra; Scheer, Alexander; Parker, Peter J.; Gierschik, Peter

doi:10.1038/360684a0

Cited by 605 publications

(329 citation statements)

References 21 publications

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“…The products were precipitated with ether, dissolved in PBS, and separated from the unreacted reagent by ultrafiltration with Microcon 10. The products were PEG/A-fMLF 4 and PEG/A-fMLF 4 -DIG 4 , and PEG/A-DIG 8 .…”

Section: Conjugation Of Peg-aspartate Copolymer With Fmlf and Digmentioning

confidence: 99%

“…These products are denoted B8-PEG-fMLF 8 , B8-PEG-fMLF 5.5 , and B8-PEG-fMLF 1.1 , respectively. Similarly, a 14-fold molar excess of fMLF was used for reactions with three-arm and four-arm branched amino-PEGs to achieve100% coupling, yielding B3-PEG-fMLF 3 and B4-PEG-fMLF 4 .…”

Section: Conjugation Of Fmlf With Branched (B) Pegmentioning

confidence: 99%

“…Cells were lysed, the membranes and cell debris were removed by centrifugation (5 min at 14000g), and the enzyme-linked immunosorbant assay (ELISA) for DIG was performed on the supernatant as described below. To study primary peritoneal cells, BALB/c mice were injected in the peritoneal cavity with 5 μg of PEG/A-DIG 4 -fMLF 4 (n = 3 mice), or PEG/A-DIG 8 (n=4 mice). After 1 h, the cavity was flushed with medium, and cells were collected and washed twice with cold PBS, as described above.…”

Section: Uptake By Hl-60 Jurkat and Peritoneal Cellsmentioning

confidence: 99%

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Conjugates Bearing Multiple Formyl-Methionyl Peptides Display Enhanced Binding to but Not Activation of Phagocytic Cells

et al. 2002

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N -Formyl-methionyl peptides can specifically bind to surface receptors on phagocytic cells. A single copy of N-formyl-methionine-leucine-phenylalanine (fMLF) covalently linked to a poly(ethylene glycol)-based polymer displayed reduced binding avidity (K d = 190 nM) for differentiated HL-60 cells relative to free fMLF (K d = 28 nM). Increasing the number of fMLF residues (up to eight) attached to a single polymer results in enhanced avidity for these cells (K d = 0.18 nM), which appears to be independent of whether the polymer backbone is linear or branched. However, no conjugate showed enhanced ability to activate phagocytic cells, relative to the free peptide (EC 50 = 5 nM), as measured by transient stimulation of release of calcium ions from intracellular stores into the cytoplasm. A polymer bearing four fMLF and four digoxigenin residues showed specific enhancement in binding to differentiated HL-60 cells and mouse peritoneal macrophages in situ relative to a polymer lacking fMLF; no such enhancement was seen in binding to receptor-negative lymphocytic Jurkat cells. These results suggest that multiple fMLF residues linked to a drug-delivery polymer can be used to target appended drugs to phagocytic cells with relatively little toxicity due to cellular activation.

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Section: Conjugation Of Peg-aspartate Copolymer With Fmlf and Digmentioning

confidence: 99%

Section: Conjugation Of Fmlf With Branched (B) Pegmentioning

confidence: 99%

Section: Uptake By Hl-60 Jurkat and Peritoneal Cellsmentioning

confidence: 99%

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Conjugates Bearing Multiple Formyl-Methionyl Peptides Display Enhanced Binding to but Not Activation of Phagocytic Cells

et al. 2002

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“…All PLC-β are strongly activated by GTPbound Gα q in the following order :β 1, β4 > β3 > β2 [8]. Additionally, PLC-β2 and PLC-β3 are activated by Gβγ subunits [9,10]. The mechanism of activation by G protein subunits is not well understood but the recent structure of PLC-β2 complexed with the small GTPase Rac2 may offer some clues [11], as discussed below.…”

Section: Introductionmentioning

confidence: 99%

Stimulation of phospholipase Cβ by membrane interactions, interdomain movement, and G protein binding — How many ways can you activate an enzyme?

Drin

Scarlata

2007

Cellular Signalling

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Signaling proteins are usually composed of one or more conserved structural domains. These domains are usually regulatory in nature by binding to specific activators or effectors, or species that regulate cellular location, etc. Inositol-specific mammalian phospholipase C (PLC) enzymes are multidomain proteins whose activities are controlled by regulators, such as G proteins, as well as membrane interactions. One of these domains has been found to bind membranes, regulators, and activate the catalytic region. The recently solved structure of a major region of PLC-β2 together with the structure of PLC-δ1 and a wealth of biochemical studies poises the system towards an understanding of the mechanism through which their regulations occurs.

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“…In addition to Gq/G11, it is well documented the  dimer of Gi proteins stimulate the activation of PLC (57,(67)(68)(69)(70)(71). PLC activated by the  dimer of Gi proteins has been demonstrated to mediate the activation of cPLA 2 and release of AA in response to ET-1 (57, 71).…”

Section: Discussionmentioning

confidence: 99%

Altered Endothelin-1 Signaling in Production of Thromboxane A2 in Kupffer Cells from Bile Duct Ligated Rats

Miller

Zhang

2009

Cell Mol Immunol

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Kupffer cells (KCs), the liver resident macrophages accounting for 80-90% of the total population of fixed tissue macrophages in the body, not only play a key role in host defense via removing particulate materials from the portal circulation, but may also contribute to the pathogenesis of various liver diseases. We have previously demonstrated that KCs play an important role in controlling portal hypertension and hepatocellular injury via releasing thromboxane A 2 (TXA 2 ) in early fibrosis induced by one-week bile duct ligation (BDL). Production of TXA 2 is controlled by cytosolic phospholipase A 2 (cPLA 2 ) that is activated by the interaction of entothelin-1 (ET-1) with its G-protein coupled ET receptor B (ETBR). However, the signaling pathways that contribute to the ET-1-induced activation of cPLA 2

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Isozyme-selective stimulation of phospholipase C-β2 by G protein βγ-subunits

Cited by 605 publications

References 21 publications

Conjugates Bearing Multiple Formyl-Methionyl Peptides Display Enhanced Binding to but Not Activation of Phagocytic Cells

Conjugates Bearing Multiple Formyl-Methionyl Peptides Display Enhanced Binding to but Not Activation of Phagocytic Cells

Stimulation of phospholipase Cβ by membrane interactions, interdomain movement, and G protein binding — How many ways can you activate an enzyme?

Altered Endothelin-1 Signaling in Production of Thromboxane A2 in Kupffer Cells from Bile Duct Ligated Rats

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