scholarly journals Measurement of whole body interleukin-6 (IL-6) production: prediction of the efficacy of anti-IL-6 treatments

Blood ◽  
1995 ◽  
Vol 86 (8) ◽  
pp. 3123-3131 ◽  
Author(s):  
ZY Lu ◽  
H Brailly ◽  
J Wijdenes ◽  
R Bataille ◽  
JF Rossi ◽  
...  
Keyword(s):  
Immune Complexes ◽  
Interleukin 6 ◽  
Acute Phase Protein ◽  
Whole Body ◽  
Tumor Proliferation ◽  
C Reactive Protein ◽  
Reactive Protein ◽  
Phase Protein ◽  
New Strategies

A major limitation on the therapeutic use of cytokine antagonists is that the amount of cytokine to be neutralized in vivo is not presently known. We previously reported that anti-interleukin-6 (IL-6) monoclonal antibody (MoAb) administered to a patient with multiple myeloma (MM) induced high amounts of IL-6 to circulate in the form of monomeric immune complexes. Based on this observation, the present study developed a new methodology to estimate daily IL-6 production in 13 patients with MM or renal cancer who received anti-IL-6 MoAb. Treatment was considered effective when the production of C-reactive protein (CRP) was inhibited. The production of this acute-phase protein by hepatocytes is dependent on the activation of IL-6 gp130 transducer. Inhibition of tumor proliferation was also evaluated in patients with MM. In 7 of 13 patients whose CRP production was completely inhibited (> 96%) and who showed some antitumoral effects, whole-body IL-6 production in vivo was less than 18 micrograms/d (median, 5.7 micrograms/d; range, 0.5 to 17.5 micrograms/d). In the other 6 patients, subtotal inhibition of CRP production and a lack of antitumoral response were associated with high IL-6 production (median, 180 micrograms/d; range, 18 to 358 micrograms/d). These in vivo observations were consistent with mathematical modeling that predicted that anti-IL-6 MoAb treatment would be efficient only in low IL-6 producers. These data indicate the difficulty of neutralizing IL-6 with a single anti-IL-6 MoAb in vivo and call for new strategies to avoid accumulation of IL-6 in the form of stable immune complexes.

scholarly journals Measurement of whole body interleukin-6 (IL-6) production: prediction of the efficacy of anti-IL-6 treatments

Blood ◽  
1995 ◽  
Vol 86 (8) ◽  
pp. 3123-3131 ◽  
Author(s):  
ZY Lu ◽  
H Brailly ◽  
J Wijdenes ◽  
R Bataille ◽  
JF Rossi ◽  
...  
Keyword(s):  
Immune Complexes ◽  
Interleukin 6 ◽  
Acute Phase Protein ◽  
Whole Body ◽  
Tumor Proliferation ◽  
C Reactive Protein ◽  
Reactive Protein ◽  
Phase Protein ◽  
New Strategies

Abstract A major limitation on the therapeutic use of cytokine antagonists is that the amount of cytokine to be neutralized in vivo is not presently known. We previously reported that anti-interleukin-6 (IL-6) monoclonal antibody (MoAb) administered to a patient with multiple myeloma (MM) induced high amounts of IL-6 to circulate in the form of monomeric immune complexes. Based on this observation, the present study developed a new methodology to estimate daily IL-6 production in 13 patients with MM or renal cancer who received anti-IL-6 MoAb. Treatment was considered effective when the production of C-reactive protein (CRP) was inhibited. The production of this acute-phase protein by hepatocytes is dependent on the activation of IL-6 gp130 transducer. Inhibition of tumor proliferation was also evaluated in patients with MM. In 7 of 13 patients whose CRP production was completely inhibited (> 96%) and who showed some antitumoral effects, whole-body IL-6 production in vivo was less than 18 micrograms/d (median, 5.7 micrograms/d; range, 0.5 to 17.5 micrograms/d). In the other 6 patients, subtotal inhibition of CRP production and a lack of antitumoral response were associated with high IL-6 production (median, 180 micrograms/d; range, 18 to 358 micrograms/d). These in vivo observations were consistent with mathematical modeling that predicted that anti-IL-6 MoAb treatment would be efficient only in low IL-6 producers. These data indicate the difficulty of neutralizing IL-6 with a single anti-IL-6 MoAb in vivo and call for new strategies to avoid accumulation of IL-6 in the form of stable immune complexes.

scholarly journals THE LIVER AS THE SITE OF C-REACTIVE PROTEIN FORMATION

1966 ◽  
Vol 123 (2) ◽  
pp. 365-378 ◽  
Author(s):  
J. Hurlimann ◽  
G. J. Thorbecke ◽  
G. M. Hochwald
Keyword(s):  
Amino Acid ◽  
Serum Proteins ◽  
Acute Phase Protein ◽  
Human Beings ◽  
C Reactive Protein ◽  
Amino Acid Incorporation ◽  
Reactive Protein ◽  
Acid Incorporation ◽  
Phase Protein

The site of formation of C-reactive protein (CxRP, CRP) has been studied with tissues from rabbits, monkeys, and human beings. Rabbits and monkeys were stimulated to produce the acute phase protein by injection of turpentine, croton oil, endotoxin, paratyphoid-typhoid vaccine, or pneumococci. C14-amino acid incorporation in vitro was demonstrated by means of autoradiography of immunoelectrophoretic patterns made with culture fluids. It was found that among many different tissues tested liver was the only tissue which incorporated C14-lysine and isoleucine into CxRP or CRP. Only livers taken 16 to 24 hr after various stimuli were active; livers from normal animals or from animals killed 3 to 9 hr after stimulation did not produce detectable amounts of CxRP. Inflamed muscle from the injection site did not show C14-amino acid incorporation into CxRP. Several human tissues were also cultured, and a few liver cultures found to contain labeled CRP. The formation of CxRP or CRP by the liver was always accompanied by enhanced C14-amino acid incorporation into other serum proteins, but the reverse was not always found.

Serum Amyloid A and C-Reactive Protein Concentrations Are Differently Associated with Markers of Autoimmunity in Patients with Primary Sjögren’s Syndrome

2009 ◽  
Vol 36 (11) ◽  
pp. 2487-2490 ◽  
Author(s):  
MARJA PERTOVAARA ◽  
JUULIA JYLHÄVÄ ◽  
HANNU UUSITALO ◽  
JUHANI PUKANDER ◽  
HEIKKI HELIN ◽  
...  
Keyword(s):  
Acute Phase ◽  
Serum Amyloid A ◽  
Acute Phase Protein ◽  
Inverse Correlation ◽  
C Reactive Protein ◽  
Reactive Protein ◽  
Amyloid A ◽  
Phase Protein ◽  
Sicca Symptoms ◽  
Protein Serum

Objective.Primary Sjögren’s syndrome (pSS) is an autoimmune disease in which the concentration of the acute-phase protein serum C-reactive protein (CRP) is low. We investigated whether levels of another acute-phase protein, serum amyloid A (SAA), are increased in patients with pSS and whether the immunological markers in patients with pSS are associated with variation in SAA levels.Methods.Serum SAA concentrations were measured by ELISA in 74 patients with pSS and in 56 control subjects with sicca symptoms.Results.Median SAA levels did not differ significantly between patients with pSS and subjects with sicca symptoms. In patients with pSS SAA concentrations correlated significantly with age, leukocyte count, CRP, interleukin 6, and C4. Unlike CRP, there was a significant inverse correlation between SAA and serum IgG levels and anti-SSA antibody titers, as well as a trend towards an inverse correlation between SAA and antinuclear antibody and rheumatoid factor titers.Conclusion.Our data imply that high SAA production could constitute a protective element in pSS: high SAA levels inhibit in particular various signs of B cell hyperreactivity, i.e., IgG and autoantibody production.

scholarly journals AN IMMUNOLOGICAL AND ELECTROPHORETIC COMPARISON OF THE ANTIBODY TO C POLYSACCHARIDE AND THE C-REACTIVE PROTEIN OF ACUTE PHASE SERUM

1943 ◽  
Vol 77 (2) ◽  
pp. 97-110 ◽  
Author(s):  
Ely Perlman ◽  
Jesse G. M. Bullowa ◽  
Ruth Goodkind
Keyword(s):  
Acute Phase ◽  
Gamma Globulin ◽  
Acute Phase Protein ◽  
Precipitation Reaction ◽  
Globulin Fraction ◽  
C Reactive Protein ◽  
C Protein ◽  
Reactive Protein ◽  
Phase Protein ◽  
Acute Phase Serum

1. Studies of the precipitation reaction of C polysaccharide with C protein, and of C polysaccharide with C antibody are reported. The similarity between these two systems in this respect is demonstrated. 2. The differences between C protein and C antibody are emphasized. The differences between this protein and antibodies in general have been reported previously by others. 3. Electrophoretic studies show that C antibody is in the gamma globulin fraction of serum whereas C protein migrates with the alpha1 globulin fraction of acute phase protein.

Biominetic-mineralized multifunctional nanoflowers for anodic-stripping voltammetric immunoassay of rehabilitation-related proteins

The Analyst ◽  
2021 ◽  
Author(s):  
Fan Cai ◽  
Jun Wang ◽  
Yao Lin ◽  
Dianping Tang
Keyword(s):  
Cerebral Infarction ◽  
Acute Phase ◽  
Acute Phase Protein ◽  
Acute Cerebral Infarction ◽  
Neurological Rehabilitation ◽  
C Reactive Protein ◽  
Reactive Protein ◽  
Anodic Stripping ◽  
Phase Protein ◽  
Related Proteins

C-reactive protein (CRP; an acute-phase protein) in patients with initial acute cerebral infarction neurological rehabilitation prediction has a significant correlation. Herein, a simple and sensitive anodic-stripping voltammetric (ASV) immunosensing system...

C-reactive protein: a predominant LPS-binding acute phase protein responsive to Pseudomonas infection

2004 ◽  
Vol 10 (3) ◽  
pp. 163-174 ◽  
Author(s):  
Patricia M.L. Ng ◽  
Zhenxiao Jin ◽  
Sandra S.H. Tan ◽  
Bow Ho ◽  
Jeak L. Ding
Keyword(s):  
Acute Phase ◽  
Acute Phase Protein ◽  
Protein A ◽  
C Reactive Protein ◽  
Reactive Protein ◽  
Phase Protein ◽  
Pseudomonas Infection ◽  
Lps Binding

scholarly journals THE RELATIONSHIP BETWEEN THE ACUTE PHASE RESPONSE AND ANTIBODY PRODUCTION IN THE RABBIT

1953 ◽  
Vol 98 (4) ◽  
pp. 321-329 ◽  
Author(s):  
Harrison F. Wood
Keyword(s):  
Acute Phase ◽  
Gamma Globulin ◽  
Acute Phase Protein ◽  
Mineral Oil ◽  
C Reactive Protein ◽  
Reactive Protein ◽  
Phase Protein ◽  
Human Gamma Globulin ◽  
Protein Response ◽  
The Relationship

The ability of an adjuvant and its individual constituents to induce the production of Cx-reactive protein in rabbits has been studied. It was found that the adjuvant stimulated rabbits to produce large amounts of the acute phase protein for 3 to 6 days. Melted aquaphor blended with saline stimulated the production of Cx-reactive protein for 3 or 4 days. Mineral oil was less effective in stimulating the production of the protein than either adjuvant or aquaphor. Heat-killed Jamaica strain tubercle bacilli suspended in mineral oil did not induce the Cx-protein response. The ability of subcutaneously administered adjuvant without antigen incorporated in the saline phase to potentiate the antibody response of rabbits to the intravenously administered antigens, C-reactive protein and human gamma globulin, was investigated. It was found that the adjuvant-treated animals produced more precipitating antibody to the two intravenously administered antigens than did the control animals given intravenous antigen alone.

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