Evidence map›Paper›PMID 3138250›Full record

ArticleThe Journal of cell biology1988

Lateral segregation of neutrophil chemotactic receptors into actin- and fodrin-rich plasma membrane microdomains depleted in guanyl nucleotide regulatory proteins.

A J Jesaitis, G M Bokoch, J O Tolley, R A Allen

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1988. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
3.3field-weighted citation impact, top 8% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

22 citing papers in PubMed, 102 citations in OpenAlex.

  1. Actin dynamics rapidly reset chemoattractant receptor sensitivity following adaptation in neutrophils.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2013
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  11. Stimulus-induced dissociation of alpha subunits of heterotrimeric GTP-binding proteins from the cytoskeleton of human neutrophils.Proceedings of the National Academy of Sciences of the United States of America · 1993
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  16. Calmodulin and calcium-dependent protease I coordinately regulate the interaction of fodrin with actin.Proceedings of the National Academy of Sciences of the United States of America · 1990
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

A J JesaitisResearch Institute of Scripps Clinic, Department of Immunology, La Jolla, California 92037.
G M Bokoch
J O Tolley
R A Allen
Scripps Health · USScripps Clinic · US

Funding

VPA 985 IN LIVER CIRRHOSIS &ASCITESM01RR000833 · NCRR · SCRIPPS RESEARCH INSTITUTE · PI BABIOR, BERNARD M · 1985 to 2004
$14.0M
RREGULATION OF SUPEROXIDE PRODUCTION BY HUMAN NEUTROPHILR01AI022735 · NIAID · SCRIPPS CLINIC AND RESEARCH FOUNDATION · PI JESAITIS, ALGIRDAS JOSEPH · 1985 to 2003
$890k
STRUCTURE OF FACTOR H AND ITS HOMOLOG--THE C3B RECEPTORP01AI017354 · NIAID · SCRIPPS RESEARCH INSTITUTE · PI PETERSON, PER A · 1985 to 1991
–
NCRR NIH HHS RR00833NIAID NIH HHS AI17354NIAID NIH HHS R01 AI22735
6 · The paper itself

Abstract

Subcellular fractions were prepared from human neutrophils desensitized at 15 degrees C with stimulatory doses of the photoaffinity derivative F-Met-Leu-Phe-N epsilon-(2-(rho-azido[125I]salicylamido)ethyl-1,3'- dithio-propionyl)-Lys. The covalently labeled receptors were found in a membrane fraction of higher density than those from cells preexposed to ligand at 4 degrees C but not desensitized. The denser fraction (rho approximately equal to 1.155 g/cc) was the cellular locus of the membrane associated cytoskeletal proteins, actin, and fodrin, as detected immunologically on western blots. The light fraction (rho approximately equal to 1.135), cosedimented with neutrophil plasma membrane markers, plasma membrane guanyl nucleotide regulatory proteins, and several characteristic polypeptides identified by SDS-PAGE, including a major 72-kD species. The photoaffinity-labeled species in either case showed the same mobility on SDS-PAGE (Mr = 50,000-70,000) corresponding to previously reported values for N-formyl chemotactic receptors. These labeled receptors were sensitive to proteolysis after exposure of the intact photoaffinity-labeled cells to papain at 4 degrees C. We conclude that (a) the fractions isolated are probably derived from different lateral microdomains of the surface of human neutrophils; (b) the higher density fraction contains occupied N-formyl-chemotactic receptors previously shown to have been converted, to a high affinity, slowly dissociating form coisolating with neutrophil cytoskeleton and implicated in the termination of formyl peptide-induced neutrophil activation; and (c) the translocation of receptors to these microdomains may serve to compartmentalize receptors and perhaps regulate the interaction of the receptor/G-protein transduction pair.

Indexed as

ActinsAutoradiographyCarrier ProteinsCell FractionationCell MembraneCentrifugation, Density GradientCytoskeletonElectrophoresis, Polyacrylamide GelFemaleGTP-Binding ProteinsHumansImmunoassayLigandsMicrofilament ProteinsNeutrophilsN-Formylmethionine Leucyl-PhenylalanineActinsCarrier ProteinsGTP-Binding ProteinsLigandsMicrofilament ProteinsN-Formylmethionine Leucyl-PhenylalanineReceptors, Formyl PeptideReceptors, ImmunologicSpectrin

Identifiers

PMID3138250
PMCPMC2115286
OpenAlexW2108407309

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.