Serum Amyloid P Component in Chronic Renal Failure and Dialysis

Nelson, Stephen R.; Tennent, Glenys A.; Sethi, D.; Gower, P E; Ballardie, F. W.; Amatayakul-Chantler, S.; Pepys, Mark B.

doi:10.1007/978-94-011-3284-8_220

Cited by 33 publications

(48 citation statements)

References 2 publications

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“…healthy control subjects (10 women and 3 men; median age 34 years [range 22-60 years]) were tested in the same assays (Figure 1), and the results (median 25 mg/liter, mean Ϯ SD 28 Ϯ 9 mg/liter [range 14-44]) were typical of those in the larger series (13,15,16) on which the reference ranges for these analytes are based.…”

Section: Resultsmentioning

confidence: 96%

“…Protein assays. SAP concentrations, in samples stored frozen (Ϫ20°C) until used, were measured by electroimmunoassay (180 V constant for 6 hours at 15°C), using monospecific polyclonal sheep anti-human SAP antibodies in 1% weight/ volume agarose gels (Indubiose A37; BioSepra, Borehamwood, UK) and calibrated with standards of normal serum spiked with isolated pure SAP, as described previously (13). Standard curves (by nonlinear curve fitting) were produced in Origin version 7.0 (OriginLab, Northampton, MA), with calibrators from 8-126 mg/liter and assay sensitivity increased by inclusion of a zero-concentration standard to allow extrapolation of values from 1-8 mg/liter.…”

Section: Methodsmentioning

confidence: 99%

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Normal circulating serum amyloid P component concentration in systemic sclerosis

Tennent¹,

Dziadzio²,

Triantafillidou³

et al. 2007

Arthritis & Rheumatism

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Objective. The observation of reduced circulating concentrations of the constitutive plasma pentraxin protein, serum amyloid P component (SAP), in serum samples obtained from a small number of patients with systemic sclerosis (SSc) has been reported as confirmation of an antifibrotic role of this protein. Because neither sustained SAP depletion in humans nor SAP deficiency in mice is associated with fibrosis, we sought to establish rigorously the serum SAP concentration in well-characterized patients with SSc.Methods. Serum concentrations of SAP were measured by electroimmunoassay in a cross-sectional cohort of 20 patients with diffuse cutaneous SSc and 12 patients with limited cutaneous SSc, and in a separate 12-month longitudinal cohort of 13 patients with diffuse disease and 37 patients with limited disease. The extent and severity of disease were characterized in detail at the time of serum sampling. Serum concentrations of the classic acute-phase reactants, C-reactive protein and serum amyloid A protein, were measured by immunonephelometric assays.Results. SAP values were entirely within the normal range, regardless of the extent and severity of disease, apart from a very few isolated raised values associated with acute intercurrent complications causing major acute-phase responses.Conclusion. We observed no reduced circulating concentrations of SAP in patients with SSc, nor any evidence of an association between SAP levels and the extent or severity of fibrosis.

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Section: Resultsmentioning

confidence: 96%

Section: Methodsmentioning

confidence: 99%

Normal circulating serum amyloid P component concentration in systemic sclerosis

Tennent¹,

Dziadzio²,

Triantafillidou³

et al. 2007

Arthritis & Rheumatism

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“…Interestingly, the role of SAP in DNA clearance is very different in human beings versus mice. As reported in many studies, hSAP has a stable physiological concentration around 20-40 mg l À1 with an even higher C H P H C h C R P m S A P h S A P + C H P H C h S A P U N C H P H C h C R P m S A P h S A P + C H P H C h S A P U N C H P H C h C R P m S A P h S A P + C H P H C h S A P U N C H P H C h C R P m S A P h S A P + C H P H C h S A P U N DNA-binding affinity, 38 whereas mSAP is a major acute phase protein with widely differing concentration in different mouse strains. Although its value in all strains of mice rise greatly during the acute phase response, 39 the normal mice have a low concentration of SAP (around 5-10 mg l À1 in C57BL/6 mice and 40-60 mg l À1 in BALB/c mice), and their binding ability are much more weaker.…”

Section: Discussionmentioning

confidence: 99%

“…Although its value in all strains of mice rise greatly during the acute phase response, 39 the normal mice have a low concentration of SAP (around 5-10 mg l À1 in C57BL/6 mice and 40-60 mg l À1 in BALB/c mice), and their binding ability are much more weaker. 20,38 We therefore suggest that human beings may have developed the highly effective regulation of SAP expression, and the subsequent capability to prevent invasion of exogenous DNA, during the evolution of the innate immune system. Unfortunately, hSAP may therefore be a barrier to effective DNA-based immunization and greatly limit the immunogenicity of DNA vaccines in the human beings.…”

Section: Discussionmentioning

confidence: 99%

Serum amyloid P component facilitates DNA clearance and inhibits plasmid transfection: implications for human DNA vaccine

et al. 2011

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The demonstration that naked plasmid DNA can induce strong immune responses in mice has attracted considerable attention in the vaccine community. However, similar immunizations have been less/not effective in clinical trials during the past decade, and the underlying mechanisms remain unknown. In this study, we hypothesized that some DNA-binding proteins in human serum may serve as host barriers, responsible for the low efficiency of plasmids' transfection in vivo. Using proteomics, we showed that human serum amyloid P component (hSAP) is specifically present in human DNA-protein complexes. Further analysis indicated that hSAP effectively binds plasmid DNA, inhibits DNA transfection into somatic cells and facilitates the endocytosis of DNA by macrophages, whereas mouse SAP (mSAP) has similar, but much weaker, activities. In the presence of hSAP, the plasmid DNA expression in vivo and plasmid DNA-induced immune responses also significantly decreased. Therefore, our results suggest that hSAP contributes to extracellular DNA clearance and the inhibition of plasmid DNA transfection in vivo. This mechanism may be partly responsible for the insufficient immune responses to DNA vaccination in human beings; therefore, it may serve as a novel target for the improvement of DNA vaccines and DNA-based gene therapy.

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“…In these patients' sera ( Table 2) the fall in SAP from the pre-ENL value was significant in the two patients whose serum anti-sulphatide IgM was shown to fall 2·5-5-fold in titre as described in a previous paper [9], at the onset of ENL. There was no relationship between possible renal dysfunction, which was indicated by proteinuria (see the section 'Human sera used in this study') and SAP content, but such a relationship has been established elsewhere [17] and it might become evident on leprosy patients if studied systematically, since renal function is known to be impaired in patients with LL [18], and one of the main line leprosy drugs, rifampin, is nephrotoxic in some patients [19].…”

Section: Sap Content Of Leprosy Seramentioning

confidence: 98%

Sulphatide-binding properties are shared by serum amyloid P component and a polyreactive germ-line IgM autoantibody, the TH3 idiotype

Wheeler

Raynes

O’Sullivan

et al. 1998

Clinical and Experimental Immunology

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SUMMARYSerum amyloid P component (SAP) concentration was elevated in sera from leprosy patients, significantly so above endemic controls in lepromatous cases. In the sera of lepromatous leprosy (LL) patients who experienced an erythema nodosum leprosum (ENL) episode the SAP fell at the onset of ENL and remained low throughout, in two of three cases. Changes in SAP concentration parallel antisulphatide IgM concentrations. TH3, a monoclonal IgM germ-line antibody derived from a LL patient, and SAP share similar binding patterns. In this study we demonstrate binding to heparin and sulphatide. Moreover, SAP inhibited the binding of TH3 to sulphatide, as well as anti-sulphatide IgM found in a range of sera, and anti-sulphatide IgG in the only sera sample in which it was found. The observation that anti-TH3 idiotype monoclonal and polyclonal anti-SAP antibodies both inhibited the binding of TH3 and IgM in sera (but not IgG) to sulphatide without binding to sulphatide themselves further demonstrated similar binding specificities. The observations of similarity in binding reinforce ideas that SAP may function as a primitive opsonin, but the clear ability to inhibit binding of autoantibodies suggests that SAP may play a role in ameliorating tissue and particularly nerve damage in leprosy patients.

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Serum Amyloid P Component in Chronic Renal Failure and Dialysis

Cited by 33 publications

References 2 publications

Normal circulating serum amyloid P component concentration in systemic sclerosis

Normal circulating serum amyloid P component concentration in systemic sclerosis

Serum amyloid P component facilitates DNA clearance and inhibits plasmid transfection: implications for human DNA vaccine

Sulphatide-binding properties are shared by serum amyloid P component and a polyreactive germ-line IgM autoantibody, the TH3 idiotype

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