Molecular characterization of the murine eosinophil secondary granule proteins and their potential relevance to the evolution of effector function

K. A. Larson, M. A. Horton, E. V. Olson, G. J. Gleich, N. A. Lee, J. J. Lee

Research output: Contribution to journalArticlepeer-review

Abstract

The secreted protein products contained within the eosinophilic leukocyte granule are believed to be important mediators of effector function(s). We have identified and cloned the abundant cationic proteins of the murine eosinophtl secondary granule: major basic protein (mMBP), eosinophil peroxidase (mEPO}. and the eosinophil associated ribonucleases (mEAR-1 and mEAR-2). mMBP and mEPO were cloned using human cDNA clones as heterologous probes in low criteria screens of murine genomic and bone marrow cDNA libraries. The mEAR genes were cloned via degenerative PCR using amino acid mlcrosequencing data derived from purified granule proteins. Homology/alignment analyses among the known eosinophil granule genes reveal a strong conservation of protein structure between species, thus providing additional clues to their putative role(s) in effector function. The evolutionary conservation of several genes also reveals that each mammalian species may not simply express a direct homologue of a given eosinophil granule protein gene; i.e., some of the proteins found in the eosinonhil granule are unique to the mammalian order under study.

Original languageEnglish (US)
Pages (from-to)A1023
JournalFASEB Journal
Volume10
Issue number6
StatePublished - Dec 1 1996

ASJC Scopus subject areas

  • Biotechnology
  • Biochemistry
  • Molecular Biology
  • Genetics

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