Development of a Radioimmunoassay for Human Group-II Phospholipase A2 and Demonstration of Postoperative Elevation

Abstract

A radioimmunoassay (RIA) for the determination of human group-II phospholipase A(2) (M-PLA(2)) has been developed. M-PLA(2) was purified from human spleen. Monoclonal antibody (IgG) was prepared by fusion of splenic cells from immunized mice with M-PLA(2) and the mouse myeloma cell line NS-1. The RIA was carried out by a single antibody method. The assay is sensitive (0.78 μg/1), reproducible and specific. In healthy individuals, the serum M-PLA2 concentration ranges from 1.4 to 4.2 μg/l, the average being 2.2 ± 0.1 μg/1 (mean ± SE). Using the RIA, we found increased serum M-PLA(2) in patients with various infections and malignant tumors. We also showed the postoperative transient elevation of serum M-PLA(2) in cases without any infectious complications. The elevation was independent of the surgical procedure or site. The maximum serum M-PLA(2) level was seen on the 2nd to 4th postoperative day. In these patients, the serum M-PLA(2) and C-reactive protein levels were significantly correlated. The present study indicated that serum M-PLA(2) is an acute phase reactant.

Overexpression of group II phospholipase A2 in human breast cancer tissues is closely associated with their malignant potency

“…M-PLA2 concentration was measured by a radioimmunoassay using anti-M-PLA2 monoclonal antibody as described by Matsuda et al (1991). There is no cross-reactivity of this antibody with human P-PLA2, pancreatic trypsin, chymotrypsin, elastase 1 and pancreatic secretory trypsin inhibitor (Matsuda et al, 1991).…”

“…M-PLA2 concentration was measured by a radioimmunoassay using anti-M-PLA2 monoclonal antibody as described by Matsuda et al (1991). There is no cross-reactivity of this antibody with human P-PLA2, pancreatic trypsin, chymotrypsin, elastase 1 and pancreatic secretory trypsin inhibitor (Matsuda et al, 1991). The purified M-PLA2 was iodinated with [125I]sodium iodide (New England Nuclear, Boston, MA, USA) by the chloramine-T method (Hunter & Greenwood, 1962), and the 251I-labelled M-PLA2 was purified by gel filtration on a PD-10 column (Pharmacia Fine Chemicals, Sweden).…”

“…Recently, we developed a specific radioimmunoassay for human M-PLA2 (Matsuda et al, 1991) and reported that the tissue concentration of M-PLA2 in human breast cancer is likely to be a prognostic factor (S. Yamashita et al, 1993). In the previous study including 78 patients (S. Yamashita et al, 1993), we determined the optimal cut-off point of 50 ng 100 mg-' protein according to the method of Tandon et al (1990).…”

Phospholipase A2: A Potential Therapeutic Target in Inflammation and Cancer (In silico, In vitro, In vivo and Clinical Approach)

“…Group PLA2-II concentration is increases in serum after extensive surgery and decreasing gradually thereafter. Postoperative group II PLA2 values correlate well with the concentration of Creactive protein in serum [8]. Zieve and Vogel firstly reported that increased PLA2 activity in serum in acute pancreatitis patients in 1961 [8].…”

“…Postoperative group II PLA2 values correlate well with the concentration of Creactive protein in serum [8]. Zieve and Vogel firstly reported that increased PLA2 activity in serum in acute pancreatitis patients in 1961 [8]. The elevation of PLA2 was correlated with the severity of the disease [9,10].…”