Occurrence of C-reactive protein in cryoglobulins

Weiner, Stefan M.; Prasauskas, V; Lebrecht, Dirk; Weber, Sabine; Peter, Hans; Vaith, P

doi:10.1046/j.1365-2249.2001.01606.x

Cited by 21 publications

(16 citation statements)

References 38 publications

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“…This is in agreement with the findings of a normal CRP turnover in SLE and resembles other inflammatory disorders [67]. However, the remarkably low CRP levels seen in SLE patients with nephritis, often in contrast to raised levels of other acute-phase reactants, may in fact be due to CRP consumption by ICs [68][69][70].…”

Section: Crp In Sle Crp In Atherosclerosissupporting

confidence: 91%

CRP and Anti-CRP Autoantibodies in Systemic Lupus Erythematosus

Sjöwall¹,

Bengtsson²

2005

CRR

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Systemic lupus erythematosus (SLE) is an autoimmune disease characterized by multiple organ involvement, production of a wide range of autoantibodies and by formation and tissue deposition of immune complexes in the inflamed organs. In contrast to most systemic inflammatory conditions, and despite raised levels of pro-inflammatory cytokines, SLE flares are rarely reflected by elevated C-reactive protein (CRP), an important acute-phase reactant in man with homologues in vertebrates and several invertebrates. Normally, the circulating concentration of liver-derived CRP rises rapidly in response to infections and tissue injury, and CRP measurement is widely employed as a marker of ongoing inflammation. With sensitive methods, detection of small elevations of CRP is also valuable as a prognostic marker in cardiovascular disease. As a part of the innate immune system, CRP binds certain molecules exposed on the surface of dying cells/apoptotic bodies and on the surface of pathogens and mediates their elimination by uptake in the reticuloendothelial system. CRP also interacts with IgG-containing immune complexes, binds Fc-receptors and activates the complement system via C1q. In murine lupus, CRP has been found to decrease autoantibody levels and increase the survival rates. In this review we discuss possible explanations for, and consequences of, the relative CRP failure in SLE, as well as pathogenetic implications of anti-CRP autoantibodies.

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Section: Crp In Sle Crp In Atherosclerosissupporting

confidence: 91%

CRP and Anti-CRP Autoantibodies in Systemic Lupus Erythematosus

Sjöwall¹,

Bengtsson²

2005

CRR

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“…This is in agreement with the findings of a normal CRP turnover in SLE and resembles other inflammatory disorders [92]. However, the remarkably low CRP levels seen in patients with hypocomplementemic disease involving skin and kidneys, often in contrast to raised levels of other acute-phase reactants, could hypothetically be due to CRP consumption by ICs [93][94][95][96][97] and indeed CRP has been identified as a component in isolated ICs from SLE patients [98].…”

Section: Sle and The Waste Disposal Hypothesissupporting

confidence: 88%

Pathogenic implications for autoantibodies against C-reactive protein and other acute phase proteins

Sjöwall

Wetterö

2007

Clinica Chimica Acta

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Systemic lupus erythematosus (SLE) is a systemic rheumatic disease characterized clinically by multiorgan involvement and serologically by the occurrence of antinuclear antibodies. SLE patients may present with multiple autoantibodies to cytoplasmic and cell surface antigens as well as to circulating plasma proteins. Another feature of SLE is that serum levels of C-reactive protein (CRP) often remain low despite high disease activity and despite high levels of other acute phase proteins and interleukin-6, i.e. the main CRP inducing cytokine. Apart from its important role as a laboratory marker of inflammation, CRP attracts increasing interest due to its many intriguing biological functions, one of which is a role as an opsonin contributing to the elimination of apoptotic cell debris, e.g. nucleosomes, thereby preventing immunization against autoantigens. Recently, autoantibodies against CRP and other acute phase proteins have been reported in certain rheumatic conditions, including SLE. Although the presence of anti-CRP autoantibodies does not explain the failed CRP response in SLE, antibodies directed against acute phase proteins have several implications of pathogenetic interest. This paper thus highlights the biological and clinical aspects of native and monomeric CRP and anti-CRP, as well as autoantibodies against mannose-binding lectin, serum amyloid A and serum amyloid P component. © 2006 Elsevier B.V. All rights reserved

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“…The limited information available stems from studies showing that some MM patients had an impaired alternative pathway activity [12,13]. Moreover, cryoglobulins, which are a common finding in MM, have the ability to activate complement [14,15].Complement is part of the innate immune system and it has a major role as a first line defense against pathogens. Complement also contributes to the clearance of immune complexes and apoptotic cells [16] and enhances development of adaptive immune responses.…”

mentioning

confidence: 99%

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confidence: 99%

Serglycin inhibits the classical and lectin pathways of complement via its glycosaminoglycan chains: Implications for multiple myeloma

et al. 2010

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Serglycin (SG) is a proteoglycan expressed by hematopoietic cells and is constitutively secreted by multiple myeloma (MM) cells. SG participates in the regulation of various inflammatory events. We found that SG secreted by human MM cell lines inhibits both the classical and lectin pathways of complement, without influencing alternative pathway activity. The inhibitory effect of SG is due to direct interactions with C1q and mannosebinding lectin (MBL). C1q-binding is mediated through the glycosaminoglycan moieties of SG, whereas MBL binds additionally to SG protein core. Interactions between SG and C1q as well as MBL are diminished in the presence of chondroitin sulfate type E. In addition, we localized the SG-binding site to the collagen-like stalk of C1q. Interactions between SG and C1q as well as MBL are ionic in character and only the interaction with MBL was found to be partially dependent on the presence of calcium. We found the serum levels of SG to be elevated in patients with MM compared to healthy controls. Moreover, we found that SG expressed from myeloma plasma cells protects these cells from complement activation induced by treatment with anti-thymocyte immunoglobulins. This might protect myeloma cells during immunotherapy and promote survival of malignant cells.Keywords: Complement . Multiple myeloma . Serglycin Introduction Serglycin (SG) is a proteoglycan with a 17 kDa protein moiety containing a characteristic domain rich in serine/glycine repeats, which serves as the attachment site for glycosaminoglycan (GAG) chains [1]. SG is mainly expressed by cells of hematopoietic origin and is a key intracellular proteoglycan [2,3]. SG can carry eight GAG chains, which depending on cell-type, can be either chondroitin sulfate (CS), dermatan sulfate (DS), heparan sulfate (HS), and heparin [3,4]. SG is constitutively secreted from monocytes [5] and macrophages [6] into the extracellular matrix and the secretion increases upon activation of these cells. The Eur. J. Immunol. 2011. 41: 437-449 DOI 10.1002 Innate immunity 437 biological function of SG is not fully elucidated, but the results obtained from studies with SG-knockout mice suggest a role for SG in the delivery of proteins into secretory granules and/or directing the secretion of these molecules [2]. It appears that SG interacts with a plethora of molecules, playing a role in the delivery of these components into secretory vesicles and further into their targets via its highly negatively charged GAG chains.Other studies have demonstrated that SG plays a key role in the storage of mast cell proteases and granzyme B and the maturation of secretory granules of mast cells and cytotoxic T-cells [7,8]. Furthermore, SG plays a crucial role in cytotoxic T-cells, as part of a multimolecular complex with perforin and granzyme B, in the delivery of the latter to the target cells during cytotoxic cell-granule-mediated cell death [9]. SG is constitutively secreted but also present on the cell surface of myeloma plasma cells and affects bone mineralization [1...

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Occurrence of C-reactive protein in cryoglobulins

Cited by 21 publications

References 38 publications

CRP and Anti-CRP Autoantibodies in Systemic Lupus Erythematosus

CRP and Anti-CRP Autoantibodies in Systemic Lupus Erythematosus

Pathogenic implications for autoantibodies against C-reactive protein and other acute phase proteins

Serglycin inhibits the classical and lectin pathways of complement via its glycosaminoglycan chains: Implications for multiple myeloma

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