Serum Amyloid P‐Component Levels in Patients with Malignancy
- 1 August 1986
- journal article
- research article
- Published by Wiley in Scandinavian Journal of Immunology
- Vol. 24 (2) , 147-151
- https://doi.org/10.1111/j.1365-3083.1986.tb02080.x
Abstract
The P component of amyloid is a normal serum protein designated SAP. SAP has substantial homology with C-reactive protein (CRP). However, unlike CRP, SAP is not an acute-phase reactant in man. Recent studies have established SAP as a major acute-phase protein in mice. Moreover, mice which have received tumour implants have also been found to have raised serum concentrations of SAP. The aim of the present study was to determine possible association between the serum level of SAP and human cancer. We found that patients with carcinoma of the breast have significantly increased serum concentrations of SAP. Moreoever, in these patients SAP levels correlated with the severity of the disease. Patients with carcinoma of the colon, however, did not differ from healthy individuals in the serum level of SAP. Possible explanations for this discrepancy are discussed.This publication has 30 references indexed in Scilit:
- Human Amyloid P Component: A Circulating Lectin that Modulates Immunological ResponsesScandinavian Journal of Immunology, 1984
- BIOSYNTHESIS OF C‐REACTIVE PROTEIN*Annals of the New York Academy of Sciences, 1982
- Monokine-induced synthesis of serum amyloid A protein by hepatocytesNature, 1980
- Classification of amyloid: 1979‐1980Arthritis & Rheumatism, 1980
- Serum amyloid P-component is an acute-phase reactant in the mouseNature, 1979
- Human plasma P component: isolation and characterizationBiochemistry, 1978
- Analogues in other mammals and in fish of human plasma proteins, C-reactive protein and amyloid P componentNature, 1978
- Amino acid sequence similarities between amyloid P component C1t and CRPNature, 1977
- Interactions of C-reactive protein with the complement system. II. C-reactive protein-mediated consumption of complement by poly-L-lysine polymers and other polycations.The Journal of Experimental Medicine, 1975
- Humanserumproteine mit hoher Affinität zu Carboxymethyl- Cellulose, III. Physikalisch-chemische und immunologische Charakterisierung eines metallbindenden 9,5S-αi-Glykoproteins (CM-Protein III)Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1972