scholarly journals The acute-phase response in (NZB X NZW)F1 and MRL/l MICE.

1982 ◽  
Vol 156 (4) ◽  
pp. 1268-1273 ◽  
Author(s):  
C Rordorf ◽  
H P Schnebli ◽  
M L Baltz ◽  
G A Tennent ◽  
M B Pepys
Keyword(s):  
Acute Phase ◽  
Acute Phase Response ◽  
Acute Phase Proteins ◽  
Acute Phase Protein ◽  
Phase Response ◽  
Serum Amyloid ◽  
Human Rheumatoid Arthritis ◽  
Amyloid A ◽  
Serum Amyloid A Protein ◽  
Phase Protein

The acute-phase plasma protein response to disease activity in murine models of autoimmune lupus-like disease was investigated by measurement of the concentration of serum amyloid P component (SAP) in NZB X W and MRL/l mice. The levels of SAP, which is a major acute-phase protein in mice, did not rise at all in response to progression of disease in NZB X W mice between the ages of 1 and 9 mo. This resembles the behavior of acute-phase proteins such as C-reactive protein and serum amyloid A protein in human systemic lupus erythematosus, and just as in human lupus, where the occurrence of intercurrent microbial infection can stimulate an acute-phase response, so injection of bacterial lipopolysaccharide or casein into the NZB X W mice stimulated "normal" acute-phase SAP production. In marked contrast, MRL/l mice developed greatly increased levels of SAP, which correlated closely with progression of their pathology as they aged. The disease profile of the MRL/l strain includes rheumatoid factors and spontaneous polyarthritis and their SAP response resembles the behavior of acute phase proteins in human rheumatoid arthritis. Different patterns of acute-phase response in different autoimmune disorders may thus be a reflection of the genetic predisposition to particular diseases and/or contribute to their pathogenesis. The existence of animal counterparts for the various clinical patterns of human acute-phase protein production will assist in experimental investigation of the underlying mechanisms and of the biological role of the acute-phase response.

The acute phase response and C-reactive protein

2020 ◽  
pp. 2199-2207
Author(s):  
Mark B. Pepys
Keyword(s):  
Acute Phase ◽  
Acute Phase Response ◽  
Serum Amyloid A ◽  
Acute Phase Proteins ◽  
Phase Response ◽  
Serum Amyloid ◽  
C Reactive Protein ◽  
Reactive Protein ◽  
Amyloid A ◽  
Serum Amyloid A Protein

The acute phase response—trauma, tissue necrosis, infection, inflammation, and malignant neoplasia induce a complex series of nonspecific systemic, physiological, and metabolic responses including fever, leucocytosis, catabolism of muscle proteins, greatly increased de novo synthesis and secretion of a number of ‘acute phase’ plasma proteins, and decreased synthesis of albumin, transthyretin, and high- and low-density lipoproteins. The altered plasma protein concentration profile is called the acute phase response. Acute phase proteins—these are mostly synthesized by hepatocytes, in which transcription is controlled by cytokines including interleukin 1, interleukin 6, and tumour necrosis factor. The circulating concentrations of complement proteins and clotting factors increase by up to 50 to 100%; some of the proteinase inhibitors and α‎1-acid glycoprotein can increase three- to fivefold; but C-reactive protein (CRP) and serum amyloid A protein (an apolipoprotein of high-density lipoprotein particles) are unique in that their concentrations can change by more than 1000-fold. C-reactive protein—this consists of five identical, nonglycosylated, noncovalently associated polypeptide subunits. It binds to autologous and extrinsic materials which contain phosphocholine, including bacteria and their products. Ligand-bound CRP activates the classical complement pathway and triggers the inflammatory and opsonizing activities of the complement system, thereby contributing to innate host resistance to pneumococci and probably to recognition and safe ‘scavenging’ of cellular debris. Clinical features—(1) determination of CRP in serum or plasma is the most useful marker of the acute phase response in most inflammatory and tissue damaging conditions. (2) Acute phase proteins may be harmful in some circumstances. Sustained increased production of serum amyloid A protein can lead to the deposition of AA-type, reactive systemic amyloid.

Corticotrophin-releasing factor as a mediator of the acute-phase response in rats, mice and rabbits

1993 ◽  
Vol 136 (2) ◽  
pp. 207-216 ◽  
Author(s):  
P. M. Hagan ◽  
S. Poole ◽  
A. F. Bristow
Keyword(s):  
Protein Synthesis ◽  
Acute Phase ◽  
Acute Phase Response ◽  
Acute Phase Proteins ◽  
Acute Phase Protein ◽  
Phase Response ◽  
Interleukin 1Β ◽  
Corticotrophin Releasing Factor ◽  
Phase Protein

ABSTRACT The acute-phase response involves a number of separate physiological components, including induction of acute-phase protein synthesis by the liver. This response can be induced in vivo by administration of the endogenous leucocytic mediator interleukin-1β. A number of in-vivo effects of interleukin-1β have been reported to be mediated by corticotrophin-releasing factor (CRF), including activation of the hypothalamo-pituitary-adrenal axis and induction of fever, and in this report we have examined a possible involvement of CRF in mediating interleukin-1β-induced acute-phase protein synthesis. Interleukin-1β stimulated the elevation of species-specific plasma acute-phase proteins in rats, mice and rabbits. Co-injection of interleukin-1β with the specific CRF receptor antagonist α-helical-CRF9–41 NH2 abolished or attenuated acute-phase protein synthesis induced by interleukin-1β in all three species for up to 12 h after injection. The inhibitory effect of α-helical-CRF9–41NH2 was reduced or absent 24 h after injection. Neutralizing anti-CRF antisera had no effect on acute-phase protein synthesis in the mouse and, paradoxically, potentiated acute-phase protein synthesis induced by interleukin-1β in the rat. These results indicate a possible mediatory role for CRF in regulation of acute-phase protein synthesis, and suggest that CRF may mediate induction of acute-phase protein synthesis by a different mechanism from that involved in regulation of corticotrophin secretion. Journal of Endocrinology (1993) 136, 207–216

scholarly journals Determination of selected acute phase proteins during the treatment of limb diseases in dairy cows

2008 ◽  
Vol 53 (No. 4) ◽  
pp. 173-183 ◽  
Author(s):  
P. Jawor ◽  
S. Steiner ◽  
T. Stefaniak ◽  
W. Baumgartner ◽  
A. Rzasa
Keyword(s):  
Treatment Group ◽  
Dairy Cows ◽  
Acute Phase ◽  
Serum Amyloid A ◽  
Acute Phase Proteins ◽  
Acute Phase Protein ◽  
Serum Amyloid ◽  
Blood Samples ◽  
Amyloid A ◽  
Phase Protein

The purpose of this study was to assess the diagnostic value of fibrinogen, haptoglobin, and serum amyloid A determination in the monitoring of the treatment of limb diseases in dairy cows. Fourteen lame cows were examined, while 10 clinically healthy cows constituted the control group. Blood samples from the ill animals were collected on three occasions: (1) upon arrival at the clinic, (2) between the third and sixth day after arriving, and (3) upon return to the owner. Blood samples from the control cows were collected once. Plasma levels of fibrinogen, haptoglobin, serum amyloid A, and total serum protein and its fractions (albumin, &alpha;-, &beta;-, &gamma;-globulins) were measured. Significantly higher fibrinogen, haptoglobin, and serum amyloid A levels were observed in the affected cows upon arrival at the clinic than in the control cows. Based on the changes in fibrinogen, haptoglobin, and serum amyloid A concentrations, the cows were divided into those with a systematic decrease in acute-phase protein levels during treatment (Group I, <I>n</I> = 6) and those which showed an increase in one or more acute-phase proteins despite treatment (Group II, <I>n</I> = 8). A stepwise decrease in the examined acute-phase proteins was observed in the first group and indicated an uncomplicated course of treatment; however, treatment of the second group did not appear to be wholly successful. A majority of the cows under treatment (<I>n</I> = 13) exhibited abnormal levels of the examined acute-phase proteins upon return to the owner. This indicates that these patients did not recover completely. The monitoring of plasma acute-phase protein concentrations can be a valuable complement to the clinical assessment of the treatment course and in the early detection of disease complications.

Serum amyloid A protein (SAA) in horses: objective measurement of the acute phase response

1989 ◽  
Vol 21 (2) ◽  
pp. 106-109 ◽  
Author(s):  
M. B. PEPYS ◽  
MARILYN L. BALTZ ◽  
GLENYS A. TENNENT ◽  
JOYCE KENT ◽  
JENNIFER OUSEY ◽  
...  
Keyword(s):  
Acute Phase ◽  
Acute Phase Response ◽  
Serum Amyloid A ◽  
Objective Measurement ◽  
Phase Response ◽  
Serum Amyloid ◽  
Amyloid A ◽  
Serum Amyloid A Protein

The Acute-Phase Protein Serum Amyloid A Induces G-CSF Expression.

Blood ◽  
2006 ◽  
Vol 108 (11) ◽  
pp. 3855-3855
Author(s):  
Rong He ◽  
Jian Zhou ◽  
Richard D. Ye
Keyword(s):  
Acute Phase ◽  
Blood Circulation ◽  
Serum Amyloid A ◽  
Acute Phase Proteins ◽  
Acute Phase Protein ◽  
Inflammatory Diseases ◽  
Serum Amyloid ◽  
Amyloid A ◽  
Phase Protein ◽  
Blood Neutrophils

Abstract Host response to injury and infection is accompanied by a rapid rise of acute-phase proteins in the blood. Serum amyloid A (SAA) is a major acute-phase protein, and has been used as a marker for inflammatory diseases. However, its precise role in inflammation has not been defined. In our previous study, we found that SAA can induce IL-8 and TNF-alpha secretion from peripheral blood neutrophils, which indicates that SAA has cytokine-like functions. We have also identified SAA as an endogenous ligand that induces the expression of interleukin-23 (IL-23), a hetero-dimeric cytokine that promotes autoimmune inflammation. In this study, we reported that SAA stimulates monocytes to secret granulocyte colony-stimulated factor (G-CSF), a cytokine and a major hematopoietic growth factor. Injection of SAA into mouse peritoneum significantly increases the number of neutrophils in both peritoneal cavity and blood circulation. These results suggest that SAA can induce granulocytosis during infection and inflammation. We hypothesize that during the inflammation, locally or systematically produced SAA can increase the number of neutrophils in blood circulation and recruits them to injured or infected sites through induction of G-CSF.

scholarly journals Acute-phase response factor, a nuclear factor binding to acute-phase response elements, is rapidly activated by interleukin-6 at the posttranslational level

1993 ◽  
Vol 13 (1) ◽  
pp. 276-288
Author(s):  
U M Wegenka ◽  
J Buschmann ◽  
C Lütticken ◽  
P C Heinrich ◽  
F Horn
Keyword(s):  
Transcriptional Regulation ◽  
Acute Phase ◽  
Interleukin 6 ◽  
Acute Phase Response ◽  
Acute Phase Protein ◽  
Phase Response ◽  
Response Factor ◽  
Nuclear Factor ◽  
Response Elements ◽  
Phase Protein

Interleukin-6 (IL-6) is known to be a major mediator of the acute-phase response in liver. We show here that IL-6 triggers the rapid activation of a nuclear factor, termed acute-phase response factor (APRF), both in rat liver in vivo and in human hepatoma (HepG2) cells in vitro. APRF bound to IL-6 response elements in the 5'-flanking regions of various acute-phase protein genes (e.g., the alpha 2-macroglobulin, fibrinogen, and alpha 1-acid glycoprotein genes). These elements contain a characteristic hexanucleotide motif, CTGGGA, known to be required for the IL-6 responsiveness of these genes. Analysis of the binding specificity of APRF revealed that it is different from NF-IL6 and NF-kappa B, transcription factors known to be regulated by cytokines and involved in the transcriptional regulation of acute-phase protein genes. In HepG2 cells, activation of APRF was observed within minutes after stimulation with IL-6 or leukemia-inhibitory factor and did not require ongoing protein synthesis. Therefore, a preexisting inactive form of APRF is activated by a posttranslational mechanism. We present evidence that this activation occurs in the cytoplasm and that a phosphorylation is involved. These results lead to the conclusions that APRF is an immediate target of the IL-6 signalling cascade and is likely to play a central role in the transcriptional regulation of many IL-6-induced genes.

Serum Amyloid A, an Acute Phase Protein, Inhibits Platelet Activation

1991 ◽  
pp. 133-134 ◽  
Author(s):  
Shulamit Zimlichman ◽  
Abraham Danon ◽  
Ilana Nathan ◽  
Gabriel Mozes ◽  
Ruth Shainkin-Kestenbaum
Keyword(s):  
Platelet Activation ◽  
Acute Phase ◽  
Serum Amyloid A ◽  
Acute Phase Protein ◽  
Serum Amyloid ◽  
Amyloid A ◽  
Phase Protein
Sign in / Sign up

Export Citation Format

Share Document