Biology of Serum Amyloid P Component*

Pepys, Mark B.; Baltz, M L; Beer, Frederick C. de; Dyck, Roland; Holford, Sarah; Breathnach, S.M.; Black, Martin M.; Tribe, C. R.; Evans, David J.; Feinstein, A.

doi:10.1111/j.1749-6632.1982.tb22144.x

Cited by 139 publications

(75 citation statements)

References 23 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Once shed, however, the heavy chain undergoes rapid degradation, and <2% of human p2m in serum and urine remains associated with soluble HLA antigens (39). Copurification offibrils and P component is consistent with the presence of the latter in association with other forms of amyloidosis (40). Although P component binds to amyloid fibrils in vitro (41), there is little reason at present to assume a facilitating role in fibril formation.…”

Section: Arg-val-asn-his-val-thr-leu-ser-gln-pro-lys-ile-val-lys-trp-mentioning

confidence: 51%

Polymerization of intact beta 2-microglobulin in tissue causes amyloidosis in patients on chronic hemodialysis.

Gorevic¹,

Muñoz²,

Casey³

et al. 1986

Proc. Natl. Acad. Sci. U.S.A.

159

View full text Add to dashboard Cite

Systemic amyloidosis with a predilection for bone and synovium may complicate the course of patients on long-term hemodialysis. This form of amyloidosis can be typed as distinct from other amyloid diseases by using small tissue samples obtained by bone biopsy and at postmortem. Immunoblot analysis of two-dimensional gels of partially solubilized amyloid fibrils established that tissue deposits are composed of monomers, dimers, and higher polymers of beta 2-microglobulin (beta 2m) and that amyloid P component was also present. Anti-beta 2m antiserum recognized fibrils, as shown by immunoelectron microscopy. Purified monomer isolated from dissociated fibrils yielded peptides corresponding to the entire known sequence of beta 2m. Virtually all serum beta 2m, as well as that present in tissue fluid bathing amyloid fibrils, was monomeric. Hemodialysis-related amyloidosis is an example of a deposition disease occurring in hemodialysis patients. We have shown conclusively that, in this amyloid disease, polymerization of an intact normal serum protein to a fibrillar configuration may occur without proteolysis. We propose the designation A beta 2m for this form of amyloid fibril subunit protein.

show abstract

Section: Arg-val-asn-his-val-thr-leu-ser-gln-pro-lys-ile-val-lys-trp-mentioning

confidence: 51%

Polymerization of intact beta 2-microglobulin in tissue causes amyloidosis in patients on chronic hemodialysis.

Gorevic¹,

Muñoz²,

Casey³

et al. 1986

Proc. Natl. Acad. Sci. U.S.A.

159

View full text Add to dashboard Cite

show abstract

“…It is found in all types of amyloid deposits (17), including in plaque from Alzheimer's disease (18), in glomerular basement membrane, and in elastic fibers in blood vessels (19,20). It also binds in a calcium-dependent manner to a variety of ligands, including DNA and chromatin (21,22), fibronectin (23), C4-binding protein (23,24), glycosaminoglycans (25,26), collagen (27), and laminin (28).…”

Section: Discussionmentioning

confidence: 99%

Serum Amyloid P Component Is the Shiga Toxin 2-neutralizing Factor in Human Blood

Kimura

Tani

Matsumoto

et al. 2001

Journal of Biological Chemistry

View full text Add to dashboard Cite

Because analysis of this factor is important to understanding the pathology induced by Shiga toxin-producing Escherichia coli, we purified this factor from human plasma and identified it. Purification was carried out by serially subjecting human plasma to Con A-Sepharose, DEAE-Sepharose, hydroxyapatite, and gel-filtration high performance liquid chromatography (HPLC), using Stx2-neutralizing activity as the indicator. The gel-filtration HPLC fraction yielded a single band on SDSpolyacrylamide gel electrophoresis. Twenty N-terminal amino acid residues of this fraction were analyzed and found to correspond perfectly to human serum amyloid P component (HuSAP). Because commercially available HuSAP also showed Stx2 binding and neutralizing activity, we identified this factor as HuSAP.

show abstract

“…hSAP and mSAP was purified from human serum and mouse acute phase serum, respectively, as described earlier. 39,49 A chemical SAP inhibitor DHPHC was synthesized according to previous reports. 27 Plasmid pGL4.17-CMV was constructed by inserting a DNA fragment containing a CMV promoter into the multiple cloning site of pGL4.17 (Promega, Madison, WI, USA).…”

Section: Cell Culturementioning

confidence: 99%

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

et al. 2011

View full text Add to dashboard Cite

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.

show abstract

Biology of Serum Amyloid P Component*

Cited by 139 publications

References 23 publications

Polymerization of intact beta 2-microglobulin in tissue causes amyloidosis in patients on chronic hemodialysis.

Polymerization of intact beta 2-microglobulin in tissue causes amyloidosis in patients on chronic hemodialysis.

Serum Amyloid P Component Is the Shiga Toxin 2-neutralizing Factor in Human Blood

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

Contact Info

Product

Resources

About