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Neutrophil chemoattractant receptors and the membrane skeleton

Karl-Norbert Klotz, Algirdas J. Jesaitis
1994 Bioessays  
This binding is inhibited by added actin, with an ICso of about 0.1 J..IM.  ... 
doi:10.1002/bies.950160310 pmid:8166673 fatcat:37q5fr34nja4xdjpy4zpbhbzki

Filamentous Phage Display of Oligopeptide Libraries

James B. Burritt, Clifford W. Bond, Kimathi W. Doss, Algirdas J. Jesaitis
1996 Analytical Biochemistry  
J., Yang, M., O'Connell, M. P., Kelley, R. F., and Henner, D. J. (1991) BioTechnology 9, 1373-1377.  ...  Greenwood, J., Willis, Anne, E., and Perham, R. N. (1991) J. Center, the NSF EPSCOR Grant RII-891879, and the Council for Mol. Biol. 220, 821-827. Tobacco Research Grant 2918R2 (A.J.J.). 30.  ... 
doi:10.1006/abio.1996.0241 pmid:8660577 fatcat:xefu7acr7zcovl7ljuc5kjdnha

The interaction of N-formyl peptide chemoattractant receptors with the membrane skeleton is energy-dependent

Karl-Norbert Klotz, Algirdas J. Jesaitis
1994 Cellular Signalling  
Desensitization of N-fonnyl peptide chemoattractant receptors (FPR) in human neutrophils is thought to be achieved by lateral segregation of receptors and G proteins within the plane of the plasma membrane resulting in an interruption of the signalling cascade. Direct coupling of FPR to membrane skeletal actin appears to be the basis of this process~ however, the molecular mechanism is unknown. In this study we investigated the effect of energy depletion on formation of FPR-membrane skeleton
more » ... plexes. In addition the effect of the protein kinase C inhibitor stauroporine and the phosphatase inhibitor okadaic acid on coupling of FPR to the membrane skeletonwas studied. Human neutrophils were desensitized using the photoreactive agonist N-formy1-met-leu-phe-1ys-N'-[1251]2(p-azidosalicylamido)ethyl-1,3'-dithiopropionate (fMLFK-[ 125 l]ASD) after ATP depletion with NaF or after incubation with the respective inhibitors. The interaction of FPR with the membrane skeleton was studied by Sedimentation of the membrane skeleton-associated receptors in sucrose density gradients. Energy depletion of the cells markedly inhibited the formation of FPR-membrane skeleton complexes. This does not appear tobe related to inhibition of protein phosphorylation due to ATP depletion because inhibition of protein kinases and phosphatases bad no significant effect on coupling of FPR to the membrane skeleton. We conclude, therefore, that coupling of FPR to the membrane skeleton is an energy,dependent process which does not appear to require modification of the receptor protein by phosphorylation.
doi:10.1016/0898-6568(94)90027-2 pmid:7718413 fatcat:yelahrvjhnhapmmvvanmo2ek3y

Mutational Analysis Reveals Distinct Features of the Nox4-p22phoxComplex

Katharina von Löhneysen, Deborah Noack, Algirdas J. Jesaitis, Mary C. Dinauer, Ulla G. Knaus
2008 Journal of Biological Chemistry  
J. Jesaitis, M. C. Dinauer, and U. G. Knaus, unpublished observations. by guest on July 26, 2018 http://www.jbc.org/ Downloaded from  ...  2100 microscope (laser 405 nm, 488 nm, 543 nm) with a ϫ63 oil objective lens (Plan Apo, 1.4 numerical aperture) and were processed using Zeiss LSM Examiner, Bio-Rad LaserSharp 2000 (version 6.0), Image J  ... 
doi:10.1074/jbc.m804200200 pmid:18849343 pmcid:PMC2596391 fatcat:sa7vmcywpzbhhfszjyozasbfuu

Critical roles for p22phoxin the structural maturation and subcellular targeting of Nox3

Yoko Nakano, Botond Banfi, Algirdas J. Jesaitis, Mary C. Dinauer, Lee-Ann H. Allen, William M. Nauseef
2007 Biochemical Journal  
Monoclonal anti-p22 phox antibodies, CS9 (mouse IgG1) and 44.1 (mouse IgG2a), and monoclonal anti-gp91 phox antibody (54.1, mouse IgG1) were provided by Dr Algirdas Jesaitis.  ... 
doi:10.1042/bj20060819 pmid:17140397 pmcid:PMC1828898 fatcat:65lt4wab7bbozodf364x4uhr7u

A Domain of p47phoxThat Interacts with Human Neutrophil Flavocytochromeb558

Frank R. DeLeo, William M. Nauseef, Algirdas J. Jesaitis, James B. Burritt, Robert A. Clark, Mark T. Quinn
1995 Journal of Biological Chemistry  
The NADPH-dependent oxidase of human neutrophils is a multicomponent system including cytosolic and membrane proteins. Activation requires translocation of cytosolic proteins p47 phox , p67 phox , and Rac2 to the plasma membrane and association with the membrane flavocytochrome b to assemble a functioning oxidase. We report the location of a region in p47 phox that mediates its interaction with flavocytochrome b. From a random peptide phage display library, we used biopanning with purified
more » ... cytochrome b to select phage peptides that mimicked potential p47 phox binding residues. Using this approach, we identified a region of p47 phox from residue 323 to 342 as a site of interaction with flavocytochrome b. Synthetic peptides 315 SRKRLSQD-AYRRNS 328 , 323 AYRRNSVRFL 332 , and 334 QRRRQARPG-PQSPG 347 inhibited superoxide (O 2 . ) production in the broken cell system with IC 50 of 18, 57, and 15 M, respectively. 323 AYRRNSVRFL 332 and its derivative peptides inhibited phosphorylation of p47 phox . However, the functional importance of this peptide was independent of its effects on phosphorylation, since 323 AYRRNA-VRFL 332 inhibited O 2 . production, but had no effect on phosphorylation. None of the peptides blocked O 2 . production when added after enzyme activation, suggesting that they inhibited the assembly, rather than the activity, of the oxidase. Furthermore these peptides inhibited membrane association of p47 phox in the broken cell translocation assay and O 2 . production by electropermeabilized neutrophils, thereby supporting the interpretation that this region of p47 phox interacts with flavocytochrome b. Human polymorphonuclear leukocytes (PMNs) 1 play an important role in host defense against invading microorganisms. PMNs possess an NADPH-dependent oxidase which is capable of generating superoxide anion (O 2 . ) and other microbicidal oxygen-derived species (e.g. H 2 O 2 , HOCl) when activated by various particulate and soluble stimuli (1, 2). The NADPH oxidase is a multicomponent enzyme system which is unassembled in resting PMNs but assembles on the plasma membrane in activated PMNs (3, 4) . The critical importance of the PMN NADPH oxidase in normal host defense is most dramatically illustrated by the frequent and severe infections seen in patients with chronic granulomatous disease (5, 6). The PMNs from such patients lack a functionally competent oxidase and, when stimulated, fail to generate O 2 . . Essential components of the NADPH oxidase include plasma membrane and cytosolic proteins. The key plasma membrane component is a heterodimeric flavocytochrome b which is composed of a 91-kDa glycoprotein (gp91 phox ) and a 22-kDa protein (p22 phox ) (7-10). Flavocytochrome b serves to transfer electrons from NADPH to molecular oxygen, resulting in the generation of O 2 . . In PMN membranes, a low molecular weight GTP-binding protein, Rap1A, is associated with flavocytochrome b and plays an important role in NADPH oxidase regulation in vivo (11) (12) (13) . Cytosolic proteins p47 phox , p67 phox , and a second low molecular weight GTP-binding protein, Rac2, are absolutely required for NADPH oxidase activity (14 -18), and these three proteins associate with flavocytochrome b to form the functional NADPH oxidase (19 -21). Additionally, a cytosolic protein, p40 phox , has recently been identified, but its role in oxidase function is not completely defined (22) . According to the current model of NADPH oxidase assembly, p47 phox and p67 phox translocate en bloc to associate with flavocytochrome b during PMN activation (23, 24). Rac2 translocates simultaneously but independently of the other two cytosolic components to associate with the membrane-bound NADPH oxidase (25, 26) . Studies of oxidase assembly in PMNs of patients with various forms of chronic granulomatous disease suggest that p47 phox binds directly to flavocytochrome b (20), and at least six regions of flavocytochrome b have been identified as potential sites for interaction with p47 phox , including four sites on gp91 phox and two sites on p22 phox (27) (28) (29) (30) (31) (32) (33) (34) . In contrast, the complementary sites of interaction presented on p47 phox have not been fully characterized (29, 33, 34) . In previous studies, peptides mimicking p47 phox residues 323 AYR-RNSVRFL 332 inhibited phosphorylation of p47 phox , O 2 . production, and translocation of cytosolic components in the broken cell system (35), suggesting that this might be a possible site of interaction between p47 phox and flavocytochrome b. In the present work, we used an approach combining the screening of a random peptide phage display library with the functional analysis of synthetic peptides to define residues in p47 phox which interact with flavocytochrome b. Our data indicate that the region encompassing amino acids 323-342 comprises a functionally important domain in the association of p47 phox with flavocytochrome b.
doi:10.1074/jbc.270.44.26246 pmid:7592831 fatcat:26nrc7wqerhrvmzdms43lvt2ai

Antibody Imprint of a Membrane Protein Surface

James B. Burritt, Scott C. Busse, Dawit Gizachew, Daniel W. Siemsen, Mark T. Quinn, Clifford W. Bond, Edward A. Dratz, Algirdas J. Jesaitis
1998 Journal of Biological Chemistry  
doi:10.1074/jbc.273.38.24847 pmid:9733789 fatcat:jvm7tyt7rzgindgavl5m6t6mry

Cytoskeletal regulation of chemotactic receptors: Molecular complexation of N-formyl peptide receptors with G proteins and actin

Algirdas J. Jesaitis, Karl-Norbert Klotz
2009 European Journal of Haematology  
Recently a report by J ohansson and co-workers confirmed the existence of regulated lateral diffusion of FPR, which at least qualitatively supports immobilization of FPR by the membrane skeleton under  ... 
doi:10.1111/j.1600-0609.1993.tb01610.x fatcat:uakpl23tlnanpigruq72wlt3se

Phosphorylation of p22phoxIs Mediated by Phospholipase D-dependent and -independent Mechanisms

Debra S. Regier, Dianne G. Greene, Susan Sergeant, Algirdas J. Jesaitis, Linda C. McPhail
2000 Journal of Biological Chemistry  
C. (1999) J. Biol. Chem. 274, 36601-36608).  ... 
doi:10.1074/jbc.m004703200 pmid:10893420 fatcat:ittnqtmrtfbqfcuh7r4m64bxte

Evidence forN-formyl chemotactic peptide-stimulated GTPase activity in human neutrophil homogenates

Paul A. Hyslop, Zenaida G. Oades, Algirdas J. Jesaitis, Richard G. Painter, Charles G. Cochrane, Larry A. Sklar
1984 FEBS Letters  
doi:10.1016/0014-5793(84)80065-4 pmid:6141069 fatcat:xusz25moxncdvekt2n6hpmi2fq

Preparation of Secretory Vesicle-Free Plasma Membranes by Isopycnic Sucrose Gradient Fractionation of Neutrophils Purified by the Gelatin Method

Jamal Stie, Algirdas J. Jesaitis
2004 Cytotechnology (Dordrecht)  
; Jesaitis et al. 1993; Jesaitis et al. 1989; Jesaitis et al. 1988 ), since the 'unstimulated' neutrophil populations employed in these latter studies were isolated by the gelatin method.  ...  Immunoblotting is performed at 22°C as previously described (Jesaitis et al. 1988 ).  ... 
doi:10.1007/s10616-005-0300-6 pmid:19003266 pmcid:PMC3449717 fatcat:g6glyfxh5zau7mfbhuy7nvpm4y

Phosphatidic Acid and Diacylglycerol Directly Activate NADPH Oxidase by Interacting with Enzyme Components

Anita Palicz, Thomas R. Foubert, Algirdas J. Jesaitis, Laszlo Marodi, Linda C. McPhail
2000 Journal of Biological Chemistry  
Zhang, J. B. Nixon, T. L. Leto, and L. C. McPhail, manuscript in preparation.  ... 
doi:10.1074/jbc.m007759200 pmid:11060300 fatcat:7pxf7ybeufct7ppzenaq2pn22y

Phage Display Epitope Mapping of Human Neutrophil Flavocytochromeb558

James B. Burritt, Frank R. DeLeo, Connie L. McDonald, Justin R. Prigge, Mary C. Dinauer, Michio Nakamura, William M. Nauseef, Algirdas J. Jesaitis
2000 Journal of Biological Chemistry  
characterization could provide information about Cyt b structure beyond localization of YKNPWIRGM B 3 LKNPWQRGD C 9 LPNPWVRGD D 1 LNKAWVRGS E 1 NANPWSRGF F 3 VNNKWARGD G 1 LTNKWMRGD H 1 IGGPWRRGF I 1 INKAWVRGM J  ... 
doi:10.1074/jbc.m006236200 pmid:11027685 fatcat:lnqckvtc5jesfhucc7ax2dre3e

Deletion Mutagenesis of p22phoxSubunit of Flavocytochromeb558

Yanmin Zhu, Christophe C. Marchal, Amy-Jo Casbon, Natalie Stull, Katharina von Löhneysen, Ulla G. Knaus, Algirdas J. Jesaitis, Sally McCormick, William M. Nauseef, Mary C. Dinauer
2006 Journal of Biological Chemistry  
Jesaitis, unpublished observations. to transfection of wild-type p22 phox , except for consistently modestly lower levels of mature gp91 phox in cells expressing p22 phox -(1-5, 172-195) (Ϸ30% lower, after  ... 
doi:10.1074/jbc.m607191200 pmid:16895900 fatcat:wrccj3agjng3npbtavug665zsi

Processing and Maturation of Flavocytochromeb558Include Incorporation of Heme as a Prerequisite for Heterodimer Assembly

Frank R. DeLeo, James B. Burritt, Lixin Yu, Algirdas J. Jesaitis, Mary C. Dinauer, William M. Nauseef
2000 Journal of Biological Chemistry  
In contrast to earlier studies by Jesaitis and co-workers (69) that demonstrated that gp91 phox and p22 phox each bound heme, Dinauer and co-workers (20) observed that p22 phox alone did not produce a  ...  Alternatively, if one heme bound exclusively to gp91 phox , whereas the other heme was shared between gp91 phox and p22 phox , as suggested by Jesaitis and co-workers (70) , then one would anticipate  ... 
doi:10.1074/jbc.275.18.13986 pmid:10788525 fatcat:vtuncpdygbcnzouodvmy4ncqgi
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