Phylogenetic Aspects of C‐reactive Protein and Related Proteins*

Baltz, M L; Beer, Frederick C. de; Feinstein, A.; Munn, E. A.; Milstein, C.; Fletcher, Thelma C.; March, John F.; Taylor, Jacqueline; Bruton, Chris J.; Clamp, John R.; Davies, A. J. S.; Pepys, Mark B.

doi:10.1111/j.1749-6632.1982.tb22125.x

Cited by 154 publications

(80 citation statements)

References 56 publications

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“…There are only minor differences in binding properties between human and rabbit CRP; both bind strongly to phosphocholine (12). In contrast, some of the C-reactive proteins described in other species are glycoproteins, some are hexamers, and most do not demonstrate marked acute phase reactivity (1,2).…”

Section: Introductionmentioning

confidence: 94%

“…Although C-reactive protein (CRP)l has been detected in the plasma of many species (1,2), it has been shown to behave as a striking acute phase reactant in only man (3), monkey (4), and the rabbit (5). In man and rabbits, CRP concentration rises rapidly after tissue injury or infection (6,7) and the magnitude of the response is remarkable; concentrations as much as 1,000 or more times normal levels may be attained.…”

Section: Introductionmentioning

confidence: 99%

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In Vivo Studies of Serum C-reactive Protein Turnover in Rabbits

Chelladurai¹,

Macintyre²,

Kushner³

1983

J. Clin. Invest.

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A B S T R A C T We determined the plasma half-life of the acute phase protein C-reactive protein (CRP) both in normal rabbits and in rabbits that had received inflammatory stimuli. Rabbit CRP was purified from acute phase serum by Cx-polysaccharide affinity chromatography, radiolabeled, and rendered pyrogen-free. Six unstimulated rabbits were injected intravenously with '25I-CRP prepared by the lactoperoxidase method and four were injected with CRP labeled by methylation using ['4C]formaldehyde. Blood samples were obtained at 0.25 h and at intervals thereafter. Plasma half-life of CRP was calculated from the data generated during the first 12 h, by which time an average of 86% of labeled protein had disappeared from the blood stream. The mean half-life for CRP was 4.45±0.2 h, with no significant difference (0.40 < P < 0.45) between 125I-and '4C-labeled CRP. In six animals stimulated with either endotoxin or turpentine 24 h before injection of labeled CRP, a mean half-life of 5.8±0.6 h was found, not significantly different (0.30

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Section: Introductionmentioning

confidence: 94%

Section: Introductionmentioning

confidence: 99%

In Vivo Studies of Serum C-reactive Protein Turnover in Rabbits

Chelladurai¹,

Macintyre²,

Kushner³

1983

J. Clin. Invest.

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“…This is because, despite the considerable phylogenetic conservation of CRP structure, there are substantial differences between CRPs of different species with respect to the fine details of ligand recognition, secondary effects of ligand binding including complement activation, normal concentrations, and behavior as acute-phase reactants. 37,38 In regard to human intervention studies, randomized trials have shown that statins can lower CRP concentration in healthy participants and in people with stable vascular disease. 39 The Justification for the Use of Statins in Primary Prevention: an Intervention Trial Evaluating Rosuvastatin (JUPITER trial) showed that rosuvastatin reduced the risk of first-ever vascular disease in people who have lower than average LDL cholesterol concentration and higher than average CRP concentration.…”

Section: Article See P 2088mentioning

confidence: 99%

C-Reactive Protein and Coronary Disease

Danesh

Pepys

2009

Circulation

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“…These artifactual heterologous systems may not provide physiologically relevant information. Despite the evolutionary conservation of sequence, subunit organization, and protein fold, there are considerable variations between CRPs of different species with respect to fine ligand-binding specificity, presence and nature of glycosylation, protomer assembly, capacity to precipitate and aggregate ligands, base-line circulating concentrations, behavior as acute-phase proteins, and capacity to activate autologous complement (7)(8)(9). Indeed, only human CRP has been rigorously shown to activate complement in isologous serum.…”

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confidence: 99%

C-reactive protein: a critical update

Pepys¹,

Hirschfield²

2003

J. Clin. Invest.

3,061

715

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IntroductionIn the mid 1990s, immunoassays for C-reactive protein (CRP), with greater sensitivity than those previously in routine use, revealed that increased CRP values, even within the range previously considered normal, strongly predict future coronary events. These findings triggered widespread interest, especially, remarkably, in the US, where the clinical use of CRP measurement had been largely ignored for about 30 years. CRP production is part of the nonspecific acute-phase response to most forms of inflammation, infection, and tissue damage and was therefore considered not to provide clinically useful information. Indeed, CRP values can never be diagnostic on their own and can only be interpreted at the bedside, in full knowledge of all other clinical and pathological results. However, they can then contribute powerfully to management, just as universal recording of the patient's temperature, an equally nonspecific parameter, is of great clinical utility.The present torrent of studies of CRP in cardiovascular disease and associated conditions is facilitated by the ready commercial availability of automated CRP assays and of CRP itself as a research reagent. However, unlike the earlier rejection in the US of CRP as an empirical test because of its perceived lack of specificity, the current enthusiasm over CRP in cardiovascular disease is widely characterized by failure to recognize appropriately the nonspecific nature of the acutephase response, and by lack of critical biological judgment. Quality control of the source, purity, and structural and functional integrity of the CRP, and the relevance of experimental design before ascribing pathophysiological functions, are also often ignored.This article provides information about CRP as a protein and an acute-phase reactant, and a knowledge-based framework for interpretation and analysis of clinical observations of CRP in relation to cardiovascular and other diseases. We also review the properties of CRP, its possible role in pathogenesis of disease, and our own observations that identify it as a possible therapeutic target.The acute-phase response CRP, named for its capacity to precipitate the somatic C-polysaccharide of Streptococcus pneumoniae, was the first acute-phase protein to be described and is an exquisitely sensitive systemic marker of inflammation and tissue damage (1). The acute-phase response comprises the nonspecific physiological and biochemical responses of endothermic animals to most forms of tissue damage, infection, inflammation, and malignant neoplasia. In particular, the synthesis of a number of proteins is rapidly upregulated, principally in hepatocytes, under the control of cytokines originating at the site of pathology. Other acute-phase proteins include proteinase inhibitors and coagulation, complement, and transport proteins, but the only molecule that displays sensitivity, response speed, and dynamic range comparable to those of CRP is serum amyloid A protein (SAA) (Table 1) (1). Circulating CRP concentrationIn healthy young adul...

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Phylogenetic Aspects of C‐reactive Protein and Related Proteins*

Cited by 154 publications

References 56 publications

In Vivo Studies of Serum C-reactive Protein Turnover in Rabbits

In Vivo Studies of Serum C-reactive Protein Turnover in Rabbits

C-Reactive Protein and Coronary Disease

C-reactive protein: a critical update

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