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  • 1
    Electronic Resource
    Electronic Resource
    Extensive Contact between Gi2 and N-Formyl Peptide Receptor of Human Neutrophils: Mapping of Binding Sites Using Receptor-Mimetic Peptides (1995)
    s.l. : American Chemical Society
    Biochemistry 34 (1995), S. 6720-6728 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00020a017
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  • 2
    Electronic Resource
    Electronic Resource
    Association of a Ras-related protein with cytochrome b of human neutrophils (1989)
    [s.l.] : Nature Publishing Group
    Nature 342 (1989), S. 198-200 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Stimulation of human neutrophils with a variety of agents induces microbicidal responses which include the generation of superoxide anion at the cell surface1'3. The plasma membrane superoxide-generating system consists of a flavoprotein NADPH-oxidase4, which oxidizes intracellular NADPH, thereby ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/342198a0
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  • 3
    Electronic Resource
    Electronic Resource
    The glycoprotein encoded by the X-linked chronic granulomatous disease locus is a component of the neutrophil cytochrome b complex (1987)
    [s.l.] : Nature Publishing Group
    Nature 327 (1987), S. 717-720 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Fig. 1 Translation of in vitro synthesized RNAs. a, cDNA constructions used to generate RNAs and the polypeptide products anticipated from initiation of translation at the indicated AUGs. The full-length X-CGD restriction map is indicated in the middle with the two in-frame AUGs indicated by upward ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/327717a0
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  • 4
    Electronic Resource
    Electronic Resource
    In vitro binding of riboflavin to subcellular particles from maize coleoptiles and Cucurbita hypocotyls (1980)
    Springer
    Planta 147 (1980), S. 312-319 
    Details
    ISSN: 1432-2048
    Keywords: Cucurbita ; Endoplasmic reticulum ; Light (blue) receptor ; Plasmalemma ; Riboflavin binding ; Zea
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Saturable and reversible in vitro binding of [14C]riboflavin was found to occur on subcellular, sedimentable particles from maize coleoptiles and Cucurbita hypocotyls. The KD was ca. 6 μM, the pH optimum was near 6.0, and the number of binding sites amounted to 0.1–0.5 μM on a fresh-weight basis. When the reducing agent dithionite was present, riboflavin binding increased-the KD was 2.5 μM, and the pH optimum above 8.0. The binding was specific: flavin mononucleotide (FMN) and flavin adenosine-dinucleotide (FAD) bound less tightly to these sites than riboflavin and another major soluble flavin, the previously described riboflavin-analog “FX”, occurring in grass coleoptiles. These flavin-binding sites were localized on vesicles derived from plasmalemma and endoplasmic reticulum by analyzing sucrose and metrizamide density gradients and marker enzymes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00379839
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  • 5
    Electronic Resource
    Electronic Resource
    Photoaffinity labeling of the N-formyl peptide receptor of human polymorphonuclear leukocytes (1982)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 20 (1982), S. 203-214 
    Details
    ISSN: 0730-2312
    Keywords: N-formyl peptide receptor ; photoaffinity labeling ; polymorphonuclear leukocytes ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Quantitative analysis of ligand-occupied receptor interactions with elements of the cytoskeleton and with intracellular compartments requires a sensitive and simple method of identifying the receptor-ligand complex in living cells. Toward this goal, we have prepared a photoactivatable arylazide derivative of the chemotactic peptide N-formyl-Nle-Leu-Phe-Nle-Tyr-Lys, which can be radiolabeled to high specific activity with 125I. This derivative was biologically active as judged by its ability to elicit superoxide anion production by human PMNL at nanomolar concentrations (ED50 ∼ 0.7 nM). When incubated at 0°C with whole PMNL, radioactive ligand became specifically and saturably associated with a 60-70,000-dalton species (as assessed by SDS-PAGE) after exposure to UV light. Addition of 10-100-fold excess of unlabeled parent or unlabeled azidopeptide derivative completely blocked uptake into this species. Approximately 20-40% of the available surface receptor-binding sites were covalently labeled under these conditions. Subcellular fractionation of the labeled cells on sucrose gradients after homogenization showed that the labeled species was primarily associated with plasma membrane-rich fractions. The labeled receptor could be completely solubilized with Triton X-100 in a form which eluted as a single species with a Stoke's radius of less than 50 Å on Sepharose 4B columns. In addition, the solubilized receptor-ligand complex bound specifically to wheat germ agglutinin, indicating that it is probably a glycoprotein. The ability to label the receptor in living PMNL with a high efficiency should facilitate the study of receptor dynamics and receptor physiochemical properties in this system.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240200211
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  • 6
    Electronic Resource
    Electronic Resource
    Ligand/receptor internalization: a spectroscopic analysis and a comparison of ligand binding, cellular response, and internalization by human neutrophils (1982)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 20 (1982), S. 193-202 
    Details
    ISSN: 0730-2312
    Keywords: ligand-receptor interaction ; neutrophils ; cellular response ; fluorescein, peptides ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: We have compared the kinetics of the responses of neutrophils to the kinetics of ligand-receptor interaction and internalization, using as a model ligand the fluorcsceinated hexapeptide N-CHO-Nle-Leu-Phe-Nle-Tyr-Lys-Fluorescein (Nle, norleucine). Cellular responses, ie, membrane depolarization, enzyme (elastase) secretion, and superoxide anion (O2-) generation, are all initiated within 10 sec of the exposure of cells to stimulus. In the cases of membrane depolarization and secretion (in cytochalasin B-treated cells), full responses are elicited by binding which occurs within 15 sec of peptide addition. Ligand binding and internalization have been analyzed over the same time frame with new spectroscopic techniques. The association of ligand and receptor is monitored using an antibody to fluorcscein. The antibody to fluorescein specifically quenches the ligand which is in solution, but receptor-bound ligand is inaccessible to the antibody. The internalization of the receptor-bound ligand is monitored by the accessibility of the fluoresceinated peptide to quenching by an external pH change (7.4 → 4.0). Ligand which is either outside or on the cell surface is instantaneously quenched while intracellular peptide (or intracellular fluorescein derived from fluorescein diacetate) is only slowly quenched. No internalization is observed until 1 min after binding begins and internalization proceeds at a rate of up to 5,000 receptors/min/cell following a near optimal stimulatory ligand concentration (∼ 1 nM) while the occupied receptors are being cleared from the surface. A comparison of the kinetics of internalization and the cellular responses suggests that internalization of the ligand is too slow to be involved in the triggering of the cellular responses.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240200210
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  • 7
    Electronic Resource
    Electronic Resource
    The fate of the N-formyl-chemotactic peptide receptor in stimulated human granulocytes: subcellular fractionation studies (1982)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 20 (1982), S. 177-191 
    Details
    ISSN: 0730-2312
    Keywords: N-formyl-chemotactic peptide ; granulocytes ; subcellular fractionation ; peptide receptors ; endocytosis ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Experiments were performed to examine how human granulocytes, stimulated by N-formyl-chemotactic peptides, process the N-formyl peptide receptor. One percent of the surface N-formyl-chemotactic peptide receptors of purified human granulocytes were covalently, specifically, and radioactively labeled at 4°C using the photochemically reactive N-formyl-chemotactic hexapeptide CHO-Nle-Leu-Phe-Nle-[l25I] Tyr-N°(6-(4′-azido-2′-nitrophenyl-amino)hexanoyl)-Lys. After incubation in the presence of 500 nM of N-formyl-Met-Leu-Phe at 37°C, the cells were lysed and fractionated by isopycnic surcrose density gradient sedimentation. Receptor-associated radioactivity cosedimented with plasma membrane in fractions from cells kept at 4°C or incubated at 37°C for 2 min or less. Fractionation of cells incubated at 37°C for longer times revealed that the radioactivity sedi-mented to lower densities coincident with Golgi markers and the site of noncovalently bound and internalized formyl-chemotactic peptide. To follow the redistribution of unoccupied receptors, human granulocytes were stimulated with 500 nM N-formyl-Met-Leu-Phe at 37°C for 5 min, washed, lysed by N2 cavitation, and fractionated by rate zonal sucrose density gradient sedimentation. Compared to unstimulated controls the specific binding of N-formyl-Met-Leu-[3H]Phe decreased 76% ± 9% in plasma membrane fractions. N-formyl-Met-Leu-[3H]Phe-binding activity associated with an intracellular pool cosedimenting with specific granules remained unchanged. Approximately 20% of the activity lost in the plasma membrane could be accounted for by a redistribution of specific N-formyl-Met-Leu-Phe binding to fractions enriched in azurophil granules. We conclude that the receptor is the carrier in the internalization of the N-formyl-chemotactic peptides to a Golgi-enriched fraction and hypothesize that after a short residency in this fraction, the receptor may dissociate from the ligand and pass onto a fraction consedimenting with dense granules.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240200209
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  • 8
    Electronic Resource
    Electronic Resource
    Membrane-cytoskeleton interactions and the regulation of chemotactic peptide-induced activation of human granulocytes: The effects of dihydrocytochalasin B (1985)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 27 (1985), S. 241-253 
    Details
    ISSN: 0730-2312
    Keywords: superoxide generation ; chemotactic peptide receptor ; cytoskeleton ; cell activation ; polymorphonuclear leukocytes ; granulocytes ; neutrophils ; dihydrocytochalasin B ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: When N-formyl chemotaclic peptides bind to granulocyte receptors at 37°C they rapidly form a high-affinity ligand-receptor complex whose coisolation with cyto-skeletal residues of Triton X-100-extracted cells is under cellular control [Jesaitis et al: J Cell Biol 98:1378, 1984]. Experiments were performed to investigate the significance of this coisolation. When the granulocytes were preincubated with dihydrocytochalasin B (dhCB) for 10 min at 37°C and then stimulated with 50 nM N-formyl-Met-Leu-[3H]Phe, the rate of uptake of the radioligand by the cells was inhibited. Colocalization of the retained peptide with the Triton X-100 fraction of these cells was also reduced relative to this fraction of the untreated cells. This inhibition was apparent before the onset of FMLP endocytosis. The inhibition was 50% effective at 0.25 μg dhCB/ml. Maximal inhibition (80-90%) occurred at doses of dhCB 〉 1 μg/ml. The 90% retention of two plasma membrane markers by the cytoskeleton was marginally affected. These results support the hypothesis that coisolation of the high-affinity receptor-peptide complexes with granulocyte cytoskeletons occurs because of specific association of the complexes with the cytoskeleton at the cell surface. In addition, since these events precede internalization, they suggest that formation of the association between the ligand-receptor complex and cytoskeleton may be necessary for ligand-receptor endocytosis. Experiments were also performed to evaluate other functional consequences of cytoskeletal disruption on chemotactic peptide-stimulated functions. f-Met-Leu-Phe stimulation of O2- production was potentiated due to prolongation of and increase in the rate of O2- production. This potentiation has the same dose dependency as the inhibition of receptor modulation. The possible relationship of these various functions is discussed.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240270306
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  • 9
    Electronic Resource
    Electronic Resource
    Neutrophil chemoattractant receptors and the membrane skeleton (1994)
    New York, NY : Wiley-Blackwell
    BioEssays 16 (1994), S. 193-198 
    Details
    ISSN: 0265-9247
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Signal transduction via receptors for N-formylmethionyl peptide chemoattractants (FPR) on human neutrophils is a highly regulated process which involves participation of cytoskeletal elements. Evidence exists suggesting that the cytoskeleton and/or the membrane skeleton controls the distribution of FPR in the plane of the plasma membrane, thus controlling the accessibility of FPR to different proteins in functionally distinct domains. In desensitized cells, FPR are restricted to domains which are depleted of G proteins but enriched in cytoskeletal proteins such as actin and fodrin. Thus, the G protein signal transduction partners of FPR become inaccessible to the agonist-occupied receptor, preventing cell activation. The mechanism of interaction of FPR with the membrane skeleton is poorly understood but evidence is accumulating that suggests a direct binding of FPR (and other receptors) to cytoskeletal proteins such as actin.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bies.950160310
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