TY - JOUR
T1 - A novel enzyme immunoassay for the determination of phosphatidylserine-specific phospholipase A1 in human serum samples
AU - Nakamura, Kazuhiro
AU - Igarashi, Koji
AU - Ohkawa, Ryunosuke
AU - Saiki, Naoya
AU - Nagasaki, Mika
AU - Uno, Kansei
AU - Hayashi, Naoto
AU - Sawada, Tetsuji
AU - Syukuya, Kenichi
AU - Yokota, Hiromitsu
AU - Arai, Hiroyuki
AU - Ikeda, Hitoshi
AU - Aoki, Junken
AU - Yatomi, Yutaka
PY - 2010/8
Y1 - 2010/8
N2 - Background: The bioactive lipid lysophosphatidylserine (LPS) is postulated to induce important biological responses and to be produced by phosphatidylserine-specific phospholipase A1 (PS-PLA1). To evaluate the functional roles of LPS in vivo, a facile assay method for PS-PLA1 has been awaited. Methods: Recombinant human PS-PLA1 was produced using a baculovirus system, and anti-human PS-PLA1 monoclonal antibodies were generated. Two clones were then selected for a 2-site immunoassay. The resulting PS-PLA1 assay reagent was applied to a commercial automated immunoassay analyzer. Results: Satisfactory results were obtained for the within-run and between-run precision, interference, detection limit, and linearity of this PS-PLA1 assay. The mean±SD of the serum PS-PLA1 antigen concentration in the 191 healthy subjects was 33.8±16.6μg/l, and the central 95th percentile reference interval for the serum PS-PLA1 antigen concentration was 13.8-74.1μg/l. The concentration was significantly (p<0.001) higher among men (13.8-80.6μg/l) than among women (12.1-68.8μg/l). We did not find a correlation between PS-PLA1 and existing laboratory tests. Conclusions: The present PS-PLA1 assay method can be applied to clinical laboratory testing, and further studies are warranted to establish its clinical significance.
AB - Background: The bioactive lipid lysophosphatidylserine (LPS) is postulated to induce important biological responses and to be produced by phosphatidylserine-specific phospholipase A1 (PS-PLA1). To evaluate the functional roles of LPS in vivo, a facile assay method for PS-PLA1 has been awaited. Methods: Recombinant human PS-PLA1 was produced using a baculovirus system, and anti-human PS-PLA1 monoclonal antibodies were generated. Two clones were then selected for a 2-site immunoassay. The resulting PS-PLA1 assay reagent was applied to a commercial automated immunoassay analyzer. Results: Satisfactory results were obtained for the within-run and between-run precision, interference, detection limit, and linearity of this PS-PLA1 assay. The mean±SD of the serum PS-PLA1 antigen concentration in the 191 healthy subjects was 33.8±16.6μg/l, and the central 95th percentile reference interval for the serum PS-PLA1 antigen concentration was 13.8-74.1μg/l. The concentration was significantly (p<0.001) higher among men (13.8-80.6μg/l) than among women (12.1-68.8μg/l). We did not find a correlation between PS-PLA1 and existing laboratory tests. Conclusions: The present PS-PLA1 assay method can be applied to clinical laboratory testing, and further studies are warranted to establish its clinical significance.
KW - Enzyme immunoassay
KW - Laboratory medicine
KW - Lysophosphatidylserine
KW - Phosphatidylserine-specific phospholipase A
UR - http://www.scopus.com/inward/record.url?scp=77953290528&partnerID=8YFLogxK
U2 - 10.1016/j.cca.2010.04.006
DO - 10.1016/j.cca.2010.04.006
M3 - 記事
C2 - 20388504
AN - SCOPUS:77953290528
SN - 0009-8981
VL - 411
SP - 1090
EP - 1094
JO - Clinica Chimica Acta
JF - Clinica Chimica Acta
IS - 1-16
ER -