Localization of C‐reactive protein in synovium of patients with rheumatoid arthritis

Gitlin, Jonathan D.; Gitlin, Joan I.; Gitlin, David

doi:10.1002/art.1780200808

Cited by 81 publications

(24 citation statements)

References 36 publications

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“…Copper is a cofactor for several major cartilage enzymes but the mechanisms involved in intracellular copper transport in chondrocyte s are unknown. Recent studies have revealed that many cells and tissues express transcripts of ceruloplasminlike proteins, including human neonatal cartilage, human fetal chondrocytes, chondrosarcom a cells (19), synovial cells (20). A cartilage matrix glycoprotein (GMGP) (21), a disul® de bounded 550kDa protein, which possesses an amino acid sequence homology with ceruloplasmin, synthesized by chondrocytes , was demonstrated to bind copper and have some oxidase activity similar to that of ceruloplasmin (22) and might serve as a copper transport protein in chondrocytes .…”

Section: Discussionmentioning

confidence: 99%

Copper modulation of extracellular matrix synthesis by human articular chondrocytes

Heraud

Savineau

Harmand

2002

Scandinavian Journal of Rheumatology

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Section: Discussionmentioning

confidence: 99%

Copper modulation of extracellular matrix synthesis by human articular chondrocytes

Heraud

Savineau

Harmand

2002

Scandinavian Journal of Rheumatology

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“…CRP binds histones [74], small nuclear ribonucleoproteins [7] and ribonucleoprotein particles [75]. In keeping to this, CRP deposition is known to be abundant in proximity of the nuclei of necrotic cells in humans affected by chronic inflammatory diseases such as rheumatoid arthritis [76]. Finally, CRP has been reported to exert a certain tumoricidal activity [77] and protect mice against cellular toxicity following the exposition to bacterial lipopolysaccharide [78].…”

Section: In Vivo Studiesmentioning

confidence: 99%

C-Reactive Protein: Interaction with the Vascular Endothelium and Possible Role in Human Atherosclerosis

Ferri¹,

Croce²,

Cofini³

et al. 2007

CPD

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C-reactive protein (CRP) is the first acute phase protein that has been described in the literature. It is phylogenetically ancient and - with serum amyloid P - belongs to proteins named as "pentraxin". After being considered a marker of acute inflammation for several decades and fruitfully used in clinical practice, CRP has been recently considered as a potential contributor to inflammatory diseases including atherosclerosis as well as a marker of cardiovascular risk. With regard to the first topic, inflammation is now believed to represent the underlying mechanism leading to the formation of human atheroma and favouring both the destabilization of vulnerable plaques and the formation of occlusive thrombi. In this regard, numerous studies indicated that modest changes in circulating CRP levels, as detected by highly sensitive methods, can be extremely useful in predicting cardiovascular and perhaps cerebrovascular diseases in apparently healthy individuals as well as in patients affected by atherosclerosis. Subjects manifesting with identical low density cholesterol and/or blood pressure levels have different rates of cardiovascular accidents on the basis of different circulating CRP concentrations. In addition, women with identical cardiovascular risk profiles developed more type 2 diabetes in the presence of higher circulating CRP levels and thereby are expected to display divergent cardiovascular prognosis. Therefore, even slight changes in circulating CRP concentrations - assuming that blood is collected appropriately and CRP is measured with correct methods - could help clinicians in defining individual cardiovascular risk. In this review, we have firstly described the current understanding of the structure of CRP, its function, and interaction with the vascular endothelial cell. Then, we have discussed how to measure circulating CRP and the more recent findings on the suggested role of circulating CRP as a novel cardiovascular risk factor.

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“…74–77 The interaction is Ca 2+ -dependent and involves the PCh-binding site of CRP. 75–77 CRP, however, does not bind chromatin in serum suggesting that this interaction occurs only if CRP or chromatin is deposited at sites of inflammation.…”

Section: Short Pentraxins: Crp and Sapmentioning

confidence: 99%

Pattern Recognition by Pentraxins

Agrawal

Singh

Bottazzi

et al. 2009

Advances in Experimental Medicine and Biology

137

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Pentraxins are a family of evolutionarily conserved pattern-recognition proteins that are made up of five identical subunits. Based on the primary structure of the subunit, the pentraxins are divided into two groups: short pentraxins and long pentraxins. C-reactive protein (CRP) and serum amyloid P-component (SAP) are the two short pentraxins. The prototype protein of the long pentraxin group is pentraxin 3 (PTX3). CRP and SAP are produced primarily in the liver while PTX3 is produced in a variety of tissues during inflammation. The main functions of short pentraxins are to recognize a variety of pathogenic agents and then to either eliminate them or neutralize their harmful effects by utilizing the complement pathways and macrophages in the host. CRP binds to modified low-density lipoproteins, bacterial polysaccharides, apoptotic cells, and nuclear materials. By virtue of these recognition functions, CRP participates in the resolution of cardiovascular, infectious, and autoimmune diseases. SAP recognizes carbohydrates, nuclear substances, and amyloid fibrils and thus participates in the resolution of infectious diseases, autoimmunity, and amyloidosis. PTX3 interacts with several ligands, including growth factors, extracellular matrix component and selected pathogens, playing a role in complement activation and facilitating pathogen recognition by phagocytes. In addition, data in gene-targeted mice show that PTX3 is essential in female fertility, participating in the assembly of the cumulus oophorus extra-cellular matrix. PTX3 is therefore a nonredundant component of the humoral arm of innate immunity as well as a tuner of inflammation. Thus, in conjunction with the other components of innate immunity, the pentraxins use their pattern-recognition property for the benefit of the host.

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Localization of C‐reactive protein in synovium of patients with rheumatoid arthritis

Cited by 81 publications

References 36 publications

Copper modulation of extracellular matrix synthesis by human articular chondrocytes

Copper modulation of extracellular matrix synthesis by human articular chondrocytes

C-Reactive Protein: Interaction with the Vascular Endothelium and Possible Role in Human Atherosclerosis

Pattern Recognition by Pentraxins

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