Changes in Serum Inflammatory Proteins during Peritonitis in CAPD Patients

1983 ◽  
Vol 3 (4) ◽  
pp. 201-204 ◽  
Author(s):  
Janet Gilmour ◽  
Rosemary Tymiansky ◽  
Andreas Pierratos ◽  
Stephen Vas ◽  
Michael Kline ◽  
...  
Keyword(s):  
Acute Phase ◽  
Acute Phase Reactant ◽  
Serum Concentrations ◽  
C Reactive Protein ◽  
Acid Glycoprotein ◽  
Reactive Protein ◽  
Phase Reactant ◽  
Inflammatory Proteins ◽  
Baseline Values ◽  
Normal Controls

The serum concentrations of IgG, IgA, IgM, C3, C4, haptoglobin, tranferrin, αl-antitrypsin, αl-acid glycoprotein, and C-reactive protein were measured in 14 CAPD patients during the course of peritonitis and at one, two and three months thereafter. Of these parameters only the CRP showed consistent changes paralleling the course of the peritonitis. The CRP baseline values in CAPD patients (second and third month after peritonitis) were similar to those found in non-dialysed normal controls, suggesting that the CRP changes, which were observed, can be attributed to the peritonitis; CRP may be a valid acute phase reactant during peritonitis in PD patients.

scholarly journals Mouse C-reactive protein. Generation of cDNA clones, structural analysis, and induction of mRNA during inflammation

1990 ◽  
Vol 266 (1) ◽  
pp. 283-290 ◽  
Author(s):  
A S Whitehead ◽  
K Zahedi ◽  
M Rits ◽  
R F Mortensen ◽  
J M Lelias
Keyword(s):  
Acute Phase ◽  
Acute Phase Reactant ◽  
Untranslated Regions ◽  
Leader Peptide ◽  
Cdna Clones ◽  
C Reactive Protein ◽  
Reactive Protein ◽  
Phase Reactant ◽  
Inflammatory Stimuli ◽  
A Minor

A full-length C-reactive protein (CRP) cDNA clone has been isolated from a CBA/J-strain-mouse acute-phase liver library. The 1614-nucleotide cDNA specifies mRNA 5′ and 3′ untranslated regions of 81 and 858 bases respectively that flank 675 bases encoding mouse pre-CRP. The derived amino acid sequence predicts a 19-residue leader peptide followed by a 206-residue mature mouse CRP that shows considerable sequence identity with both human and rabbit CRP. Northern-blot analysis of mouse liver CRP mRNA concentrations after inflammatory stimuli and comparison with hepatic induction of mRNA for the major mouse acute-phase protein serum amyloid P component established that CRP, a major acute-phase reactant in human and rabbit, is a minor acute-phase reactant in mouse. The size and organization of the mouse CRP mRNA 5′ and 3′ untranslated regions are significantly different from those of human and rabbit CRP mRNA and may have implications for its anomalous minimal induction during acute inflammation.

scholarly journals Platelet agonist synergism by the acute phase reactant C-reactive protein

Blood ◽  
1985 ◽  
Vol 65 (2) ◽  
pp. 264-269
Author(s):  
BA Fiedel
Keyword(s):  
Acute Phase ◽  
Creatine Phosphokinase ◽  
Platelet Rich Plasma ◽  
Adenosine Diphosphate ◽  
Creatine Phosphate ◽  
Acute Phase Reactant ◽  
C Reactive Protein ◽  
Reactive Protein ◽  
Phase Reactant ◽  
Irreversible Aggregation

C-reactive protein is the prototypic acute phase reactant. A self- complexed form (H-CRP) can induce isolated platelets to undergo aggregation, secretion of dense and alpha-granule constituents, and generation of thromboxane A2, but fails to function in platelet-rich plasma (PRP) as a direct agonist. In contrast, when PRP was activated with an amount of adenosine diphosphate (ADP) that produced only reversible platelet aggregation, the presence of H-CRP resulted in irreversible aggregation and the secretion of adenosine triphosphate (ATP). Following a maximum stimulus with ADP alone, where platelet secretion occurred late during the aggregation response, the presence of H-CRP shifted and increased the secretory burst to a time simultaneous with the onset of aggregation. This hypersecretion required H-CRP to be present prior to platelet stimulation or to be added within 15 to 30 seconds following the addition of ADP. H-CRP also potentiated platelet activation stimulated with epinephrine, thrombin, and collagen. When the synergism generated in PRP by H-CRP in the presence of ADP or epinephrine was compared to the synergism similarly produced by aggregated human IgG, collagen, or thrombin, it more closely resembled that of collagen, as reflected by the kinetics and characteristics of synergism and sensitivity to creatine phosphate/creatine phosphokinase or 5,8,11,14-eicosatetraynoic acid. These data provide a philosophically ideal niche for the acute phase (and C-reactive protein) in that a platelet-directed activity associated with this acute phase reactant is not utilized unless platelets are otherwise challenged.

scholarly journals Cloning and tissue-specific expression of the gene for mouse C-reactive protein

1993 ◽  
Vol 295 (2) ◽  
pp. 379-386 ◽  
Author(s):  
N O Ku ◽  
R F Mortensen
Keyword(s):  
Acute Phase ◽  
Transcriptional Start Site ◽  
Interleukin 1 ◽  
Acute Phase Reactant ◽  
C Reactive Protein ◽  
Specific Expression ◽  
Tissue Specific ◽  
Tissue Specific Expression ◽  
Reactive Protein ◽  
Phase Reactant

C-reactive protein is a serum acute-phase reactant that increases several thousand-fold in concentration during inflammation in most mammals. However, mouse C-reactive protein is considered to be a minor acute-phase reactant, since its blood level increases only from approx. 0.1 to 1-2 micrograms/ml. A mouse genomic clone of approximately 5 kb was obtained to determine the molecular basis for the regulation of the expression of mouse C-reactive protein. Several cis-acting elements in the 5′ flanking region that potentially regulate transcription were identified: two glucocorticoid-responsive elements, two CCAAT-enhancer-binding protein C (C/EBP) consensus elements that are required for the interleukin-1 responsiveness of some acute-phase reactant genes, an interleukin-6-responsive element, two hepatocyte nuclear factor-1 (HNF-1) elements and a single heat-shock element. Transfection of the hepatoma cell line Hep 3B.2 with a pCAT expression vector containing the 5′ flanking sequence from -1083 to -3 bp from the transcriptional start site, and truncations of this sequence, localized elements that control the tissue-specific expression of mouse C-reactive protein to the two HNF-1 elements and a C/EBP, interleukin-1-responsive element located between -220 and -153, and -90 and -50 bp from the transcriptional start site. A constitutive nuclear protein from mouse-liver hepatocytes specifically binds to the HNF-1 elements. These findings explain the tissue-specific expression of the gene, as well as its limited expression during the acute-phase response.

scholarly journals Platelet agonist synergism by the acute phase reactant C-reactive protein

Blood ◽  
1985 ◽  
Vol 65 (2) ◽  
pp. 264-269 ◽  
Author(s):  
BA Fiedel
Keyword(s):  
Acute Phase ◽  
Creatine Phosphokinase ◽  
Platelet Rich Plasma ◽  
Adenosine Diphosphate ◽  
Creatine Phosphate ◽  
Acute Phase Reactant ◽  
C Reactive Protein ◽  
Reactive Protein ◽  
Phase Reactant ◽  
Irreversible Aggregation

Abstract C-reactive protein is the prototypic acute phase reactant. A self- complexed form (H-CRP) can induce isolated platelets to undergo aggregation, secretion of dense and alpha-granule constituents, and generation of thromboxane A2, but fails to function in platelet-rich plasma (PRP) as a direct agonist. In contrast, when PRP was activated with an amount of adenosine diphosphate (ADP) that produced only reversible platelet aggregation, the presence of H-CRP resulted in irreversible aggregation and the secretion of adenosine triphosphate (ATP). Following a maximum stimulus with ADP alone, where platelet secretion occurred late during the aggregation response, the presence of H-CRP shifted and increased the secretory burst to a time simultaneous with the onset of aggregation. This hypersecretion required H-CRP to be present prior to platelet stimulation or to be added within 15 to 30 seconds following the addition of ADP. H-CRP also potentiated platelet activation stimulated with epinephrine, thrombin, and collagen. When the synergism generated in PRP by H-CRP in the presence of ADP or epinephrine was compared to the synergism similarly produced by aggregated human IgG, collagen, or thrombin, it more closely resembled that of collagen, as reflected by the kinetics and characteristics of synergism and sensitivity to creatine phosphate/creatine phosphokinase or 5,8,11,14-eicosatetraynoic acid. These data provide a philosophically ideal niche for the acute phase (and C-reactive protein) in that a platelet-directed activity associated with this acute phase reactant is not utilized unless platelets are otherwise challenged.

scholarly journals Binding of fibronectin by the acute phase reactant C-reactive protein.

1984 ◽  
Vol 259 (3) ◽  
pp. 1496-1501 ◽  
Author(s):  
E M Salonen ◽  
T Vartio ◽  
K Hedman ◽  
A Vaheri
Keyword(s):  
Acute Phase ◽  
Acute Phase Reactant ◽  
C Reactive Protein ◽  
Reactive Protein ◽  
Phase Reactant

Serum amyloid A versus C-reactive protein in acute pancreatitis: Clinical value of an alternative acute-phase reactant

2000 ◽  
Vol 28 (3) ◽  
pp. 736-742 ◽  
Author(s):  
Bettina Rau ◽  
Gerald Steinbach ◽  
Katja Baumgart ◽  
Frank Gansauge ◽  
Adolf Grünert ◽  
...  
Keyword(s):  
Acute Pancreatitis ◽  
Acute Phase ◽  
Serum Amyloid A ◽  
Acute Phase Reactant ◽  
Serum Amyloid ◽  
C Reactive Protein ◽  
Clinical Value ◽  
Reactive Protein ◽  
Amyloid A ◽  
Phase Reactant

scholarly journals Serum Protein Changes after Abdominal Surgery

1989 ◽  
Vol 26 (1) ◽  
pp. 49-57 ◽  
Author(s):  
Peter G Shakespeare ◽  
Andrew J Ball ◽  
Errol D Spurr
Keyword(s):  
Acute Phase ◽  
Prognostic Value ◽  
Serum Proteins ◽  
Recovery Period ◽  
Acute Phase Reactant ◽  
C Reactive Protein ◽  
Reactive Protein ◽  
Phase Reactant ◽  
Patients At Risk ◽  
Main Factor

Changes in the concentrations of 11 serum proteins following surgery for a variety of conditions have been investigated. Protein changes were analogous to those observed after injury or trauma, but showed differences in the detailed behaviour of the pattern of change. Marked increases in the concentrations of five acute-phase reactant proteins (APRP) were seen, with maximum concentrations usually being reached 2 days after surgery in patients who made an uncomplicated recovery from their operations. Considerable differences were observed between the patterns of change of APRP in patients who developed complications during recovery and in patients who made an uncomplicated recovery from surgery. Concentrations of C-reactive protein and alpha-1 antichymotrypsin (ACT) were much higher in the patients who developed complications, with ACT concentrations providing the clearest separation between the groups. The main factor influencing the changes in APRP during the recovery period appeared to be the development of sepsis. Preoperative concentrations of APRP had no prognostic value for identifying patients at risk of developing complications. The study suggests that the localisation of inflamed tissue involved in the disease processes may influence the detailed behaviour of the acute-phase reactant proteins.

scholarly journals Luminometric assays of seven acute-phase proteins in minimal volumes of serum, plasma, sputum, and bronchioalveolar lavage.

1986 ◽  
Vol 32 (5) ◽  
pp. 743-747 ◽  
Author(s):  
J Braun ◽  
T Schultek ◽  
K F Tegtmeier ◽  
A Florenz ◽  
C Rohde ◽  
...  
Keyword(s):  
Acute Phase ◽  
Acute Phase Proteins ◽  
Immunoglobulin A ◽  
C Reactive Protein ◽  
Acid Glycoprotein ◽  
Reactive Protein ◽  
Coefficients Of Variation ◽  
Alpha 1 Antitrypsin ◽  
Heel Prick ◽  
Secretory Immunoglobulin

Abstract We describe immunoluminometric assays for seven acute-phase proteins, which can be determined in minimal volumes of plasma, serum, sputum, and bronchioalveolar lavage. The theoretical volume of serum or plasma required to measure all seven analytes in duplicate is 130 nL, although in practice the smallest volume of sample was enough to fill a hematocrit tube (about 25 microL of blood), collected from neonates by the heel-prick method. The assays could be performed with 10 microL of sputum or with 100 microL of bronchioalveolar lavage. We measured alpha 1-antitrypsin, alpha 2-macroglobulin, alpha 1-acid glycoprotein, thyroxin-binding prealbumin, C-reactive protein, and total and secretory immunoglobulin A. The assays are rapid enough for all results to be returned to the ward on the same day and are suitable for monitoring neonatal sepsis. All coefficients of variation, derived from compound precision profiles, were less than 7% for clinically relevant analyte concentrations. Correlation with commercially available nephelometric assays was good.

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