Evidence map›Paper›PMID 20843812›Full record

ArticleThe Journal of biological chemistry2010

Identification of acidic pH-dependent ligands of pentameric C-reactive protein.

David J Hammond, Sanjay K Singh, James A Thompson, Bradley W Beeler, Antonio E Rusiñol, Michael K Pangburn, Lawrence A Potempa, Alok Agrawal

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

58 citing papers in PubMed, 86 citations in OpenAlex.

  1. Review
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  9. Article
  10. The Role of Anti-mCRP Autoantibodies in Lupus Nephritis.Kidney diseases (Basel, Switzerland) · 2023
    Review
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  12. Article
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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

8 authors at 3 institutions in 1 country.

David J HammondDepartment of Pharmacology, Quillen College of Medicine, East Tennessee State University, Johnson City, Tennessee 37614, USA.
Sanjay K Singh
James A Thompson
Bradley W Beeler
Antonio E Rusiñol
Michael K Pangburn
Lawrence A Potempa
Alok Agrawal
East Tennessee State University · USDeerfield (United States) · USThe University of Texas Health Science Center at Tyler · US

Funding

Structure-Function Relationships of C-Reactive ProteinR01HL071233 · NHLBI · EAST TENNESSEE STATE UNIVERSITY · PI AGRAWAL, ALOK · 2002 to 2011
$2.6M
REGULATION OF COMPLEMENT BY MEMBRANE PROTEINSR01DK035081 · NIDDK · UNIVERSITY OF TEXAS HLTH CTR AT TYLER · PI PANGBURN, MICHAEL K. · 1986 to 2011
$2.5M
NHLBI NIH HHS R01 HL071233NHLBI NIH HHS R01HL071233NIDDK NIH HHS R01 DK035081NIDDK NIH HHS R01DK35081
6 · The paper itself

Abstract

C-reactive protein (CRP) is a phylogenetically conserved protein; in humans, it is present in the plasma and at sites of inflammation. At physiological pH, native pentameric CRP exhibits calcium-dependent binding specificity for phosphocholine. In this study, we determined the binding specificities of CRP at acidic pH, a characteristic of inflammatory sites. We investigated the binding of fluid-phase CRP to six immobilized proteins: complement factor H, oxidized low-density lipoprotein, complement C3b, IgG, amyloid β, and BSA immobilized on microtiter plates. At pH 7.0, CRP did not bind to any of these proteins, but, at pH ranging from 5.2 to 4.6, CRP bound to all six proteins. Acidic pH did not monomerize CRP but modified the pentameric structure, as determined by gel filtration, 1-anilinonaphthalene-8-sulfonic acid-binding fluorescence, and phosphocholine-binding assays. Some modifications in CRP were reversible at pH 7.0, for example, the phosphocholine-binding activity of CRP, which was reduced at acidic pH, was restored after pH neutralization. For efficient binding of acidic pH-treated CRP to immobilized proteins, it was necessary that the immobilized proteins, except factor H, were also exposed to acidic pH. Because immobilization of proteins on microtiter plates and exposure of immobilized proteins to acidic pH alter the conformation of immobilized proteins, our findings suggest that conformationally altered proteins form a CRP-ligand in acidic environment, regardless of the identity of the protein. This ligand binding specificity of CRP in its acidic pH-induced pentameric state has implications for toxic conditions involving protein misfolding in acidic environments and favors the conservation of CRP throughout evolution.

Indexed as

LigandsProtein MultimerizationAcidsAmino Acid SubstitutionAmyloid beta-PeptidesAnimalsBinding SitesCalciumCattleChlorocebus aethiopsComplement C3bComplement Factor HCOS CellsC-Reactive ProteinHumansHydrogen-Ion ConcentrationAcidsAmyloid beta-PeptidesCalciumComplement C3bComplement Factor HC-Reactive ProteinImmunoglobulin GLigandsLipoproteins, LDLoxidized low density lipoproteinSerum Albumin, Bovine

Identifiers

PMID20843812
PMCPMC2975246
OpenAlexW1986553067

What OpenQuestion holds

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Registered trials

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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.