scholarly journals The pentraxins, C-reactive protein and serum amyloid P component, are cleared and catabolized by hepatocytes in vivo.

1994 ◽  
Vol 94 (4) ◽  
pp. 1390-1396 ◽  
Author(s):  
W L Hutchinson ◽  
G E Noble ◽  
P N Hawkins ◽  
M B Pepys
Keyword(s):  
Serum Amyloid ◽  
C Reactive Protein ◽  
Amyloid P Component ◽  
Reactive Protein ◽  
Serum Amyloid P ◽  
Serum Amyloid P Component ◽  
Amyloid P

scholarly journals Investigating interactions of the pentraxins serum amyloid P component and C-reactive protein by mass spectrometry

2003 ◽  
Vol 375 (2) ◽  
pp. 323-328 ◽  
Author(s):  
J. Andrew AQUILINA ◽  
Carol V. ROBINSON
Keyword(s):  
Protein A ◽  
Serum Amyloid ◽  
C Reactive Protein ◽  
Oligomeric State ◽  
Amyloid P Component ◽  
Reactive Protein ◽  
Serum Amyloid P ◽  
Serum Amyloid P Component ◽  
Amyloid P

The oligomeric state of human SAP (serum amyloid P component) in the absence and presence of known ligands has been investigated using nanoelectrospray ionization MS. At pH 8.0, in the absence of Ca2+, SAP has been shown to consist of pentameric and decameric forms. In the presence of physiological levels of Ca2+, SAP was observed to exist primarily as a pentamer, reflecting its in vivo state. dAMP was shown not only to promote decamerization, but also to lead to decamer stacking involving up to 30 monomers. A mechanism for this finding is proposed. CRP (C-reactive protein), a pentraxin closely related to SAP, exists as a pentamer in the presence or absence of Ca2+. Pentamers of CRP and SAP were shown to form mixed decamers in Ca2+-free buffer; however, in the presence of Ca2+, this interaction was not observed. Furthermore, no exchange of monomeric subunits was observed between the SAP and CRP oligomers, suggesting a remarkable stability of the individual pentameric complexes.

scholarly journals Specific localization and imaging of amyloid deposits in vivo using 123I-labeled serum amyloid P component.

1988 ◽  
Vol 167 (3) ◽  
pp. 903-913 ◽  
Author(s):  
P N Hawkins ◽  
M J Myers ◽  
A A Epenetos ◽  
D Caspi ◽  
M B Pepys
Keyword(s):  
Serum Amyloid ◽  
C Reactive Protein ◽  
Amyloid P Component ◽  
Reactive Protein ◽  
Amyloid A ◽  
Serum Amyloid P ◽  
Serum Amyloid P Component ◽  
Amyloid Deposits ◽  
Amyloid P

Highly specific, high-resolution scintigraphic images of amyloid-laden organs in mice with experimentally induced amyloid A protein (AA) amyloidosis were obtained after intravenous injection of 123I-labeled serum amyloid P component (SAP). Interestingly, a much higher proportion (up to 40%) of the injected dose of heterologous human SAP localized to amyloid and was retained there than was the case with isologous mouse SAP, indicating that human SAP binds more avidly to mouse AA fibrils than does mouse SAP. Specificity of SAP localization was established by the failure of the related proteins, human C-reactive protein and Limulus C-reactive protein, to deposit significantly in amyloid and by the absence of human SAP deposition in nonamyloidotic organs. However, only partial correlations were observed between the quantity of SAP localized and two independent estimates, histology and RIA for AA of the amount of amyloid in particular organs. It is not clear which of the three methods used reflects better the extent or clinical significance of the amyloid deposits but in vivo localization of radiolabeled SAP, detectable and quantifiable by gamma camera imaging, is apparently extremely sensitive. These findings establish the use of labeled SAP as a noninvasive in vivo diagnostic probe in experimental amyloidosis, potentially capable of revealing the natural history of the condition, and suggest that it may also be applicable generally as a specific targeting agent for diagnostic and even therapeutic purposes in clinical amyloidosis.

scholarly journals Vitamin D Correction Down-Regulates Serum Amyloid P Component Levels in Vitamin D Deficient Arab Adults: A Single-Arm Trial

Nutrients ◽  
2020 ◽  
Vol 12 (9) ◽  
pp. 2880
Author(s):  
Osama Amer ◽  
Malak Khattak ◽  
Abdullah Alnaami ◽  
Naji Aljohani ◽  
Nasser Al-Daghri
Keyword(s):  
Vitamin D ◽  
Serum Amyloid ◽  
C Reactive Protein ◽  
Post Intervention ◽  
Amyloid P Component ◽  
Reactive Protein ◽  
Serum Amyloid P ◽  
Serum Amyloid P Component ◽  
Study Participants ◽  
Amyloid P

Vitamin D (VD) has been observed to have anti-inflammatory properties. However, the effects of VD supplementation on the serum amyloid P component (SAP) has not been established. This study aimed to investigate the effect of VD supplementation on serum SAP levels in Arab adults. A total of 155 VD-deficient adult Saudis (56 males and 99 females) were recruited in this non-randomized, 6-month, single-arm trial. The intervention was as follows; cholecalciferol 50,000 international units (IU) every week for the first 2 months, followed by 50,000 twice a month for the next two months, and for the last two months, 1000 IU daily. Serum 25(OH)D, SAP, C-reactive protein (CRP), lipid profile, and glucose were assessed at baseline and post-intervention. At post-intervention, VD levels were significantly increased, while SAP levels significantly decreased in all study participants. Remarkably, this reduction in SAP was more significant in males than females after stratification. SAP was inversely correlated with VD overall (r = −0.17, p < 0.05), and only in males (r = −0.27, p < 0.05) after stratification according to sex after 6 months of VD supplementation. Such a relationship was not observed at baseline. VD supplementation can favorably modulate serum SAP concentrations in Arab adults, particularly in males.

Antiamyloidogenic and proamyloidogenic chaperone effects of C-reactive protein and serum amyloid P component

Amyloid ◽  
2017 ◽  
Vol 24 (sup1) ◽  
pp. 28-29 ◽  
Author(s):  
Daisaku Ozawa ◽  
Ryo Nomura ◽  
P. Patrizia Mangione ◽  
Kazuhiro Hasegawa ◽  
Tadakazu Okoshi ◽  
...  
Keyword(s):  
Serum Amyloid ◽  
C Reactive Protein ◽  
Amyloid P Component ◽  
Reactive Protein ◽  
Serum Amyloid P ◽  
Serum Amyloid P Component ◽  
Amyloid P
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