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The production of the eosinophil proteins ECP and EPX / EDN are regulated in a reciprocal manner
Author(s) -
Jönsson UllaBritt,
Blom Kristin,
Stålenheim Gunnemar,
Håkansson Lena Douhan,
Venge Per
Publication year - 2014
Publication title -
apmis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.909
H-Index - 88
eISSN - 1600-0463
pISSN - 0903-4641
DOI - 10.1111/apm.12142
Subject(s) - eosinophil cationic protein , microbiology and biotechnology , single nucleotide polymorphism , biology , eosinophil , immunology , genotype , chemistry , gene , genetics , asthma
Previous studies showed that the biological activity and the eosinophil content of eosinophil cationic protein ( ECP , RN ase 3) are determined by single‐nucleotide polymorphisms ( SNP s) in the ECP ( RNase 3) gene . In this study, we report the prevalence of a common SNP in the eosinophil protein x/eosinophil‐derived neurotoxin ( EPX / EDN , RNase 2) and the association with the cellular contents of EPX / EDN and ECP . The genes were sequenced and the EPX / EDN 405(G>C) rs2013109 SNP s were also determined by TaqMan 5′nuclease allelic discrimination assay. ECP and EPX / EDN in purified eosinophils or in whole blood extracts were analysed by sensitive immunoassays. The study included 379 non‐allergic and allergic subjects. The genotype prevalence of the EPX / EDN 405(G>C) polymorphism was GG 59%, GC 36% and CC 6%. The cellular contents of ECP and EPX / EDN were related in a reciprocal fashion with the sums of the protein contents being constant. The contents were associated with the ECP 562(G>C) rs2233860 and EPX / EDN 405(G>C) gene polymorphisms. The cellular content of eosinophil peroxidase ( EPO ) was not associated with the ECP and EPX / EDN genotypes. The prevalence of the EPX / EDN 405(G>C) genotypes and the contents of the proteins were similar in non‐allergic and allergic subjects. The production and storage of the two ancestral proteins, ECP and EPX / EDN likely share common regulatory mechanisms, which result in opposing productions of the two proteins.